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Conserved domains on  [gi|32528297|ref|NP_872198|]
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ribosomal protein S6 kinase alpha-5 isoform b [Homo sapiens]

Protein Classification

protein kinase family protein; serine/threonine-protein kinase( domain architecture ID 10145238)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins; serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
48-337 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 631.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKL 127
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIVQKAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd05613  81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd05613 161 ERAYSFCGTIEYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 288 DLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05613 241 DIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
418-548 4.11e-96

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14179:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 310  Bit Score: 295.03  E-value: 4.11e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 418 PFYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd14179   1 PFYQHYELDLKDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14179  81 MELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPE 131
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
320-379 2.98e-16

Extension to Ser/Thr-type protein kinases;


:

Pssm-ID: 214529  Cd Length: 64  Bit Score: 73.16  E-value: 2.98e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297    320 KINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPA---ALPQSSEKLFQGYSFVA 379
Cdd:smart00133   2 GIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVdspLSGGIQQEPFRGFSYVF 64
 
Name Accession Description Interval E-value
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
48-337 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 631.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKL 127
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIVQKAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd05613  81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd05613 161 ERAYSFCGTIEYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 288 DLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05613 241 DIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
49-318 1.05e-100

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 304.45  E-value: 1.05e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297     49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAkttEHTRTERQVLEHIRqSPFLVTLHYAFQTETKLH 128
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDK---KTGKLVAIKVIKKKKIKKDR---ERILREIKILKKLK-HPNIVRLYDVFEDEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvaDETE 208
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL--DPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    209 RAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKD 288
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLLG--KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKD 229
                          250       260       270
                   ....*....|....*....|....*....|
gi 32528297    289 LIQRLLMKDPKKRLGcgprdADEIKEHLFF 318
Cdd:smart00220 230 LIRKLLVKDPEKRLT-----AEEALQHPFF 254
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
418-548 4.11e-96

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 295.03  E-value: 4.11e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 418 PFYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd14179   1 PFYQHYELDLKDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14179  81 MELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPE 131
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
46-375 9.49e-88

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 274.00  E-value: 9.49e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   46 IENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTET 125
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKG---TGEYYAIKCLKKREIL-KMKQVQHVAQEKSILMELSH-PFIVNMMCSFQDEN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvad 205
Cdd:PTZ00263  92 RVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV--- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  206 eTERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQEMSAL 285
Cdd:PTZ00263 169 -PDRTFTLCGTPEYLAPEVIQ--SKGHGKAVDWWTMGVLLYEFIAGYPPFFDD----TPFRIYEKILAGRLKFPNWFDGR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  286 AKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFaEEFTEmDPTYSPAALP 365
Cdd:PTZ00263 242 ARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNF-EKYPD-SPVDRLPPLT 319
                        330
                 ....*....|
gi 32528297  366 QSSEKLFQGY 375
Cdd:PTZ00263 320 AAQQAEFAGF 329
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
46-316 1.68e-60

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 207.56  E-value: 1.68e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKkATIVQKAKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTET 125
Cdd:COG0515   6 LGRYRILRLLGRGGMGVVYLARDL---RLGRPVALKVLR-PELAADPEARERFRREARALARLN-HPNIVRVYDVGEEDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:COG0515  81 RPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQEMS-- 283
Cdd:COG0515 161 TLTQTGTVVGTPGYMAPEQARGEPVDP--RSDVYSLGVTLYELLTGRPPFDGD----SPAELLRAHLREPPPPPSELRpd 234
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32528297 284 ---ALAkDLIQRLLMKDPKKRlgcgPRDADEIKEHL 316
Cdd:COG0515 235 lppALD-AIVLRALAKDPEER----YQSAAELAAAL 265
Pkinase pfam00069
Protein kinase domain;
49-318 1.99e-59

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 196.31  E-value: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIvqKAKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTETKLH 128
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKEKI--KKKKDKNILREIKILKKLN-HPNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLgiiyrdiklenilldsnghvvltdfglskefvadete 208
Cdd:pfam00069  75 LVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLESGSSL------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   209 raYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILkSEPPYPQEMSALAKD 288
Cdd:pfam00069 118 --TTFVGTPWYMAPEVLGG--NPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPY-AFPELPSNLSEEAKD 192
                         250       260       270
                  ....*....|....*....|....*....|
gi 32528297   289 LIQRLLMKDPKKRLGcgprdADEIKEHLFF 318
Cdd:pfam00069 193 LLKKLLKKDPSKRLT-----ATQALQHPWF 217
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
430-548 4.25e-43

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 154.22  E-value: 4.25e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR----MEANTQKEITALKLCeGHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIKKKkikkDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYCEGGD 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 32528297    506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:smart00220  84 LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPE 126
Pkinase pfam00069
Protein kinase domain;
428-532 3.23e-28

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 111.95  E-value: 3.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIISKR-----MEANTQKEITALKLCeGHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:pfam00069   3 VLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEkikkkKDKNILREIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEYVE 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 32528297   503 GGELFERIKKKKHFSETEASYIMRKLVSAV 532
Cdd:pfam00069  82 GGSLFDLLSEKGAFSEREAKFIMKQILEGL 111
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
430-548 1.01e-24

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 107.41  E-value: 1.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT------QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:COG0515  13 RLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPearerfRREARALARLN-HPNIVRVYDVGEEDGRPYLVMEYVEG 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:COG0515  92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPA 136
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
154-292 3.57e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 97.17  E-value: 3.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  154 VQIyVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERAY--SFCGTIEYMAPDIVRGGDSg 231
Cdd:NF033483 110 VEI-MIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIAR--ALSSTTMTQtnSVLGTVHYLSPEQARGGTV- 185
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297  232 hDKAVDWWSLGVLMYELLTGASPFtvDGEknSQAEISRRILKSEPPYPQE-------------MSALAKDLIQR 292
Cdd:NF033483 186 -DARSDIYSLGIVLYEMLTGRPPF--DGD--SPVSVAYKHVQEDPPPPSElnpgipqsldavvLKATAKDPDDR 254
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
320-379 2.98e-16

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 73.16  E-value: 2.98e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297    320 KINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPA---ALPQSSEKLFQGYSFVA 379
Cdd:smart00133   2 GIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVdspLSGGIQQEPFRGFSYVF 64
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
415-548 2.98e-16

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 79.86  E-value: 2.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  415 KDSPFYQHYDLDLKDKpLGEGSFSICRKCVHKKSNQAFAVKIISKR--MEANTQKEITALK--LCE-GHPNIVKLHEVFH 489
Cdd:PTZ00263  10 PDTSSWKLSDFEMGET-LGTGSFGRVRIAKHKGTGEYYAIKCLKKReiLKMKQVQHVAQEKsiLMElSHPFIVNMMCSFQ 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297  490 DQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:PTZ00263  89 DENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPE 147
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
478-548 8.63e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.43  E-value: 8.63e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297  478 HPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:NF033483  66 HPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQ 136
Pkinase_C pfam00433
Protein kinase C terminal domain;
339-377 2.07e-08

Protein kinase C terminal domain;


Pssm-ID: 459809 [Multi-domain]  Cd Length: 42  Bit Score: 50.28  E-value: 2.07e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 32528297   339 IRDELDVSNFAEEFTEMDPTYSPA---ALPQSSEKLFQGYSF 377
Cdd:pfam00433   1 VKSETDTSNFDPEFTEEPPVLTPPdssILSSNDQEEFRGFSY 42
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
460-548 3.35e-07

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 53.31  E-value: 3.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    460 RMEANTQKEITalkLCEG--HPNIVKLHE--VFHDQLhTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHM 535
Cdd:TIGR03903   20 HQRARFRRETA---LCARlyHPNIVALLDsgEAPPGL-LFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACA 95
                           90
                   ....*....|...
gi 32528297    536 HDVGVVHRDLKPE 548
Cdd:TIGR03903   96 HNQGIVHRDLKPQ 108
 
Name Accession Description Interval E-value
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
48-337 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 631.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKL 127
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIVQKAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd05613  81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd05613 161 ERAYSFCGTIEYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 288 DLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05613 241 DIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
48-380 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 625.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKL 127
Cdd:cd05614   1 NFELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd05614  81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd05614 161 ERTYSFCGTIEYMAPEIIR-GKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKCDPPFPSFIGPVAR 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 288 DLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAALPQS 367
Cdd:cd05614 240 DLLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVYSPAGTPPS 319
                       330
                ....*....|...
gi 32528297 368 SEKLFQGYSFVAP 380
Cdd:cd05614 320 GARVFQGYSFIAP 332
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
54-321 0e+00

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 588.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDY 133
Cdd:cd05583   1 VLGTGAYGKVFLVRKVGGHDAGKLYAMKVLKKATIVQKAKTAEHTMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSF 213
Cdd:cd05583  81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYSF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 214 CGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRL 293
Cdd:cd05583 161 CGTIEYMAPEVVRGGSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRILKSHPPIPKTFSAEAKDFILKL 240
                       250       260
                ....*....|....*....|....*...
gi 32528297 294 LMKDPKKRLGCGPRDADEIKEHLFFQKI 321
Cdd:cd05583 241 LEKDPKKRLGAGPRGAHEIKEHPFFKGL 268
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
52-380 4.31e-156

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 448.78  E-value: 4.31e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLHLIL 131
Cdd:cd05584   1 LKVLGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKASIVRNQKDTAHTKAERNILEAV-KHPFIVDLHYAFQTGGKLYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVaDETERAY 211
Cdd:cd05584  80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESI-HDGTVTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILK---SEPPYpqeMSALAKD 288
Cdd:cd05584 159 TFCGTIEYMAPEILT--RSGHGKAVDWWSLGALMYDMLTGAPPFTAENRK----KTIDKILKgklNLPPY---LTNEARD 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 289 LIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSP--AALPQ 366
Cdd:cd05584 230 LLKKLLKRNVSSRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFTKQTPVDSPddSTLSE 309
                       330
                ....*....|....
gi 32528297 367 SSEKLFQGYSFVAP 380
Cdd:cd05584 310 SANQVFQGFTYVAP 323
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
55-318 2.88e-139

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 402.67  E-value: 2.88e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd05123   1 LGKGSFGKVLLVRKK---DTGKLYAMKVLRKKEIIKR-KEVEHTLNERNILERVN-HPFIVKLHYAFQTEEKLYLVLDYV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVaDETERAYSFC 214
Cdd:cd05123  76 PGGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELS-SDGDRTYTFC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 215 GTIEYMAPDIVRGGdsGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQEMSALAKDLIQRLL 294
Cdd:cd05123 155 GTPEYLAPEVLLGK--GYGKAVDWWSLGVLLYEMLTGKPPFYAE----NRKEIYEKILKSPLKFPEYVSPEAKSLISGLL 228
                       250       260
                ....*....|....*....|....
gi 32528297 295 MKDPKKRLGCGPrdADEIKEHLFF 318
Cdd:cd05123 229 QKDPTKRLGSGG--AEEIKAHPFF 250
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
53-378 2.15e-134

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 392.92  E-value: 2.15e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIvqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05582   1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATL--KVRDRVRTKMERDILADVNH-PFIVKLHYAFQTEGKLYLILD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVaDETERAYS 212
Cdd:cd05582  78 FLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESI-DHEKKAYS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd05582 157 FCGTVEYMAPEVV--NRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRK----ETMTMILKAKLGMPQFLSPEAQSLLRA 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 293 LLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAALPQ-SSEKL 371
Cdd:cd05582 231 LFKRNPANRLGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSaNAHQL 310

                ....*..
gi 32528297 372 FQGYSFV 378
Cdd:cd05582 311 FRGFSFV 317
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
53-378 8.45e-128

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 376.17  E-value: 8.45e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRkisGHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05570   1 KVLGKGSFGKVMLAE---RKKTDELYAIKVLKKEVIIED-DDVECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAdETERAYS 212
Cdd:cd05570  77 YVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIW-GGNTTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd05570 156 FCGTPDYIAPEILREQD--YGFSVDWWALGVLLYEMLAGQSPFEGDDED----ELFEAILNDEVLYPRWLSREAVSILKG 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 293 LLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAA---LPQSSE 369
Cdd:cd05570 230 LLTKDPARRLGCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDsdlLTNIDQ 309

                ....*....
gi 32528297 370 KLFQGYSFV 378
Cdd:cd05570 310 EEFRGFSYI 318
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
53-380 1.75e-118

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 352.81  E-value: 1.75e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05571   1 KVLGKGTFGKVILCRE---KATGELYAIKILKKEVIIAKDEVA-HTLTENRVLQNTRH-PFLTSLKYSFQTNDRLCFVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD-ETERay 211
Cdd:cd05571  76 YVNGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYgATTK-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPF-TVDGEKnsqaeISRRILKSEPPYPQEMSALAKDLI 290
Cdd:cd05571 154 TFCGTPEYLAPEVLEDNDYGR--AVDWWGLGVVMYEMMCGRLPFyNRDHEV-----LFELILMEEVRFPSTLSPEAKSLL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 291 QRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPA------AL 364
Cdd:cd05571 227 AGLLKKDPKKRLGGGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPdrgdllGL 306
                       330
                ....*....|....*.
gi 32528297 365 PQSSEKLFQGYSFVAP 380
Cdd:cd05571 307 EEEERPHFEQFSYSAS 322
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
47-348 5.63e-115

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 342.25  E-value: 5.63e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVqKAKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTETK 126
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHK---DSGKYYALKILKKAKII-KLKQVEHVLNEKRILSEVR-HPFIVNLLGSFQDDRN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVade 206
Cdd:cd05580  76 LYMVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 tERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtVDgekNSQAEISRRILKSEPPYPQEMSALA 286
Cdd:cd05580 153 -DRTYTLCGTPEYLAPEIILS--KGHGKAVDWWALGILIYEMLAGYPPF-FD---ENPMKIYEKILEGKIRFPSFFDPDA 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 287 KDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNF 348
Cdd:cd05580 226 KDLIKRLLVVDLTKRLGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNF 287
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
53-378 4.21e-114

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 341.60  E-value: 4.21e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05575   1 KVIGKGSFGKVLLARHK---AEGKLYAVKVLQKKAILKR-NEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLsQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADeTERAY 211
Cdd:cd05575  77 YVNGGELFFHL-QRERhFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEP-SDTTS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQEMSALAKDLIQ 291
Cdd:cd05575 155 TFCGTPEYLAPEVLRKQP--YDRTVDWWCLGAVLYEMLYGLPPFY----SRDTAEMYDNILHKPLRLRTNVSPSARDLLE 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 292 RLLMKDPKKRLGCGpRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAALPQSSEKL 371
Cdd:cd05575 229 GLLQKDRTKRLGSG-NDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPVPASVGKSADSVAVS 307
                       330
                ....*....|....*.
gi 32528297 372 ---------FQGYSFV 378
Cdd:cd05575 308 asvqeadnaFDGFSYV 323
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
53-361 4.53e-104

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 315.79  E-value: 4.53e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05595   1 KLLGKGTFGKVILVREKA---TGRYYAMKILRKEVIIAKDEVA-HTVTESRVLQNTRH-PFLTALKYAFQTHDRLCFVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAyS 212
Cdd:cd05595  76 YANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMK-T 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPF-TVDGEKnsqaeISRRILKSEPPYPQEMSALAKDLIQ 291
Cdd:cd05595 155 FCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFyNQDHER-----LFELILMEEIRFPRTLSPEAKSLLA 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 292 RLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSP 361
Cdd:cd05595 228 GLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITP 297
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
53-380 5.74e-104

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 315.48  E-value: 5.74e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKaTIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05592   1 KVLGKGSFGKVMLAEL---KGTNQYFAIKALKK-DVVLEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETErAYS 212
Cdd:cd05592  77 YLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENK-AST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd05592 156 FCGTPDYIAPEILKG--QKYNQSVDWWSFGVLLYEMLIGQSPFHGEDED----ELFWSICNDTPHYPRWLTKEAASCLSL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 293 LLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAA---LPQSSE 369
Cdd:cd05592 230 LLERNPEKRLGVPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVLTPVDkklLASMDQ 309
                       330
                ....*....|.
gi 32528297 370 KLFQGYSFVAP 380
Cdd:cd05592 310 EQFKGFSFTNP 320
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
49-380 4.85e-103

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 313.08  E-value: 4.85e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTtEHTRTERQVLEHIRQS--PFLVTLHYAFQTETK 126
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEY---KPTGELFAIKALKKGDIIARDEV-ESLMCEKRIFETVNSArhPFLVNLFACFQTPEH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQrERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAdE 206
Cdd:cd05589  77 VCFVMEYAAGGDLMMHIHE-DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMG-F 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEMSALA 286
Cdd:cd05589 155 GDRTSTFCGTPEFLAPEVLT--DTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEE----EVFDSIVNDEVRYPRFLSTEA 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 287 KDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAA--- 363
Cdd:cd05589 229 ISIMRRLLRKNPERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPKepr 308
                       330
                ....*....|....*...
gi 32528297 364 -LPQSSEKLFQGYSFVAP 380
Cdd:cd05589 309 pLTEEEQALFKDFDYVAD 326
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
52-378 6.31e-102

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 310.09  E-value: 6.31e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLIL 131
Cdd:cd05587   1 LMVLGKGSFGKVMLAER---KGTDELYAIKILKKDVIIQD-DDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA-DETERa 210
Cdd:cd05587  77 EYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFgGKTTR- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 ySFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvDGEknSQAEISRRILKSEPPYPQEMSALAKDLI 290
Cdd:cd05587 156 -TFCGTPDYIAPEIIA--YQPYGKSVDWWAYGVLLYEMLAGQPPF--DGE--DEDELFQSIMEHNVSYPKSLSKEAVSIC 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 291 QRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSP------AAL 364
Cdd:cd05587 229 KGLLTKHPAKRLGCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPtdklviMNI 308
                       330
                ....*....|....
gi 32528297 365 PQSSeklFQGYSFV 378
Cdd:cd05587 309 DQSE---FEGFSFV 319
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
47-378 9.30e-102

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 310.76  E-value: 9.30e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRqSPFLVTLHYAFQTETK 126
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDK---DTGQVYAMKILRKSDMLKREQIA-HVRAERDILADAD-SPWIVRLHYAFQDEDH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd05573  76 LYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TE----------------------------RAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVD 258
Cdd:cd05573 156 DResylndsvntlfqdnvlarrrphkqrrvRAYSAVGTPDYIAPEVLRG--TGYGPECDWWSLGVILYEMLYGFPPFYSD 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 259 geknSQAEISRRILKSE-----PPYPqEMSALAKDLIQRLLmKDPKKRLGcgprDADEIKEHLFFQKINWDDLaaKKVPA 333
Cdd:cd05573 234 ----SLVETYSKIMNWKeslvfPDDP-DVSPEAIDLIRRLL-CDPEDRLG----SAEEIKAHPFFKGIDWENL--RESPP 301
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 334 PFKPVIRDELDVSNFaEEFTEmDPTYSPaALPQSSEKLF--QGYSFV 378
Cdd:cd05573 302 PFVPELSSPTDTSNF-DDFED-DLLLSE-YLSNGSPLLGkgKQLAFV 345
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
49-344 9.86e-101

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 306.86  E-value: 9.86e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd05574   3 FKKIKLLGKGDVGRVYLVRLK---GTGKLFAMKVLDKEEMIKRNKVK-RVLTEREILATLDH-PFLPTLYASFQTSTHLC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFtHLSQRE---RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK----- 200
Cdd:cd05574  78 FVMDYCPGGELF-RLLQKQpgkRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvt 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 ----------------------EFVADE-TERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTV 257
Cdd:cd05574 157 pppvrkslrkgsrrssvksiekETFVAEpSARSNSFVGTEEYIAPEVIKG--DGHGSAVDWWTLGILLYEMLYGTTPFKG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 258 DgeknSQAEISRRILKSEPPYPQ--EMSALAKDLIQRLLMKDPKKRLGCgPRDADEIKEHLFFQKINWDDLaaKKVPAPF 335
Cdd:cd05574 235 S----NRDETFSNILKKELTFPEspPVSSEAKDLIRKLLVKDPSKRLGS-KRGASEIKRHPFFRGVNWALI--RNMTPPI 307

                ....*....
gi 32528297 336 KPVIRDELD 344
Cdd:cd05574 308 IPRPDDPID 316
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
49-318 1.05e-100

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 304.45  E-value: 1.05e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297     49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAkttEHTRTERQVLEHIRqSPFLVTLHYAFQTETKLH 128
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDK---KTGKLVAIKVIKKKKIKKDR---ERILREIKILKKLK-HPNIVRLYDVFEDEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvaDETE 208
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL--DPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    209 RAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKD 288
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLLG--KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKD 229
                          250       260       270
                   ....*....|....*....|....*....|
gi 32528297    289 LIQRLLMKDPKKRLGcgprdADEIKEHLFF 318
Cdd:smart00220 230 LIRKLLVKDPEKRLT-----AEEALQHPFF 254
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
54-377 2.01e-98

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 301.03  E-value: 2.01e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIrQSPFLVTLHYAFQTETKLHLILDY 133
Cdd:cd05585   1 VIGKGSFGKVMQVRK---KDTSRIYALKTIRKAHIVSRSEVT-HTLAERTVLAQV-DCPFIVPLKFSFQSPEKLYLVLAF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADeTERAYSF 213
Cdd:cd05585  76 INGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKD-DDKTNTF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 214 CGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtVDGEKNsqaEISRRILKSEPPYPQEMSALAKDLIQRL 293
Cdd:cd05585 155 CGTPEYLAPELLLG--HGYTKAVDWWTLGVLLYEMLTGLPPF-YDENTN---EMYRKILQEPLRFPDGFDRDAKDLLIGL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 294 LMKDPKKRLGCGprDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTE---MDPTYSPAALPQSSEK 370
Cdd:cd05585 229 LNRDPTKRLGYN--GAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTRekpIDSVVDDSHLSESVQQ 306

                ....*..
gi 32528297 371 LFQGYSF 377
Cdd:cd05585 307 QFEGWSY 313
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
47-377 1.97e-97

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 298.76  E-value: 1.97e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd05599   1 EDFEPLKVIGRGAFGEVRLVRK---KDTGHVYAMKKLRKSEMLEK-EQVAHVRAERDILAEA-DNPWVVKLYYSFQDEEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvaDE 206
Cdd:cd05599  76 LYLIMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGL--KK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDgekNSQaEISRRIL--KSEPPYPQEM-- 282
Cdd:cd05599 154 SHLAYSTVGTPDYIAPEVF--LQKGYGKECDWWSLGVIMYEMLIGYPPFCSD---DPQ-ETCRKIMnwRETLVFPPEVpi 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 283 SALAKDLIQRLLMkDPKKRLgcGPRDADEIKEHLFFQKINWDDLaaKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPA 362
Cdd:cd05599 228 SPEAKDLIERLLC-DAEHRL--GANGVEEIKSHPFFKGVDWDHI--RERPAPILPEVKSILDTSNFDEFEEVDLQIPSSP 302
                       330       340
                ....*....|....*....|.
gi 32528297 363 ALPQSSEKL------FQGYSF 377
Cdd:cd05599 303 EAGKDSKELkskdwvFIGYTY 323
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
418-548 4.11e-96

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 295.03  E-value: 4.11e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 418 PFYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd14179   1 PFYQHYELDLKDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14179  81 MELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPE 131
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
52-380 2.96e-95

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 293.41  E-value: 2.96e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRkisGHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLIL 131
Cdd:cd05604   1 LKVIGKGSFGKVLLAK---RKRDGKYYAVKVLQKKVILNR-KEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLsQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAdETERA 210
Cdd:cd05604  77 DFVNGGELFFHL-QRERsFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGIS-NSDTT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 YSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQEMSALAKDLI 290
Cdd:cd05604 155 TTFCGTPEYLAPEVIR--KQPYDNTVDWWCLGSVLYEMLYGLPPFY----CRDTAEMYENILHKPLVLRPGISLTAWSIL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 291 QRLLMKDPKKRLGCGpRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYS------PAAL 364
Cdd:cd05604 229 EELLEKDRQLRLGAK-EDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEEMVPYSvcvssdYSIV 307
                       330
                ....*....|....*....
gi 32528297 365 PQS---SEKLFQGYSFVAP 380
Cdd:cd05604 308 NASvleADDAFVGFSYAPP 326
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
53-378 3.17e-95

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 293.03  E-value: 3.17e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKC---DGKFYAVKVLQKKTILKK-KEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADEtERAYS 212
Cdd:cd05603  77 YVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPE-ETTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd05603 156 FCGTPEYLAPEVLR--KEPYDRTVDWWCLGAVLYEMLYGLPPFY----SRDVSQMYDNILHKPLHLPGGKTVAACDLLQG 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 293 LLMKDPKKRLGcGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFT-EMDP-----TYSPAALPQ 366
Cdd:cd05603 230 LLHKDQRRRLG-AKADFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTqEAVPhsvgrTPDLTASSS 308
                       330
                ....*....|..
gi 32528297 367 SSEKLFQGYSFV 378
Cdd:cd05603 309 SSSSAFLGFSYA 320
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
58-323 4.29e-94

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 288.35  E-value: 4.29e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  58 GAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTtEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLHLILDYINGG 137
Cdd:cd05579   4 GAYGRVYLAKKKS---TGDLYAIKVIKKRDMIRKNQV-DSVLAERNILSQA-QNPFVVKLYYSFQGKKNLYLVMEYLPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 138 ELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE--------------FV 203
Cdd:cd05579  79 DLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVglvrrqiklsiqkkSN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQ--E 281
Cdd:cd05579 159 GAPEKEDRRIVGTPDYLAPEILLG--QGHGKTVDWWSLGVILYEFLVGIPPFHAE----TPEEIFQNILNGKIEWPEdpE 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 32528297 282 MSALAKDLIQRLLMKDPKKRLGCGPrdADEIKEHLFFQKINW 323
Cdd:cd05579 233 VSDEAKDLISKLLTPDPEKRLGAKG--IEEIKNHPFFKGIDW 272
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
55-377 1.61e-93

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 289.08  E-value: 1.61e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEH--IRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05586   1 IGKGTFGQVYQVRK---KDTRRIYAMKVLSKKVIVAK-KEVAHTIGERNILVRtaLDESPFIVGLKFSFQTPTDLYLVTD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefvADETERAY- 211
Cdd:cd05586  77 YMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSK---ADLTDNKTt 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 -SFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDgekNSQaEISRRILKSEPPYPQE-MSALAKDL 289
Cdd:cd05586 154 nTFCGTTEYLAPEVLL-DEKGYTKMVDFWSLGVLVFEMCCGWSPFYAE---DTQ-QMYRNIAFGKVRFPKDvLSDEGRSF 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 290 IQRLLMKDPKKRLGcGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTE--------------- 354
Cdd:cd05586 229 VKGLLNRNPKHRLG-AHDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFTNasllnanivpwaqrp 307
                       330       340
                ....*....|....*....|...
gi 32528297 355 MDPTYSPAALPQSSEKLFQGYSF 377
Cdd:cd05586 308 GLPGATSTPLSPSVQANFRGFTF 330
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
38-361 8.74e-93

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 287.75  E-value: 8.74e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  38 TGHAEKVGIENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQsPFLVTL 117
Cdd:cd05593   6 TTHHKRKTMNDFDYLKLLGKGTFGKVILVREKA---SGKYYAMKILKKEVIIAKDEVA-HTLTESRVLKNTRH-PFLTSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 118 HYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd05593  81 KYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEFVADETERAySFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPF-TVDGEKnsqaeISRRILKSEP 276
Cdd:cd05593 161 LCKEGITDAATMK-TFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFyNQDHEK-----LFELILMEDI 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 277 PYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMD 356
Cdd:cd05593 233 KFPRTLSADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQT 312

                ....*
gi 32528297 357 PTYSP 361
Cdd:cd05593 313 ITITP 317
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
37-381 8.06e-90

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 280.38  E-value: 8.06e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  37 LTGHAEKVGIENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQsPFLVT 116
Cdd:cd05594  15 LTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKA---TGRYYAMKILKKEVIVAKDEVA-HTLTENRVLQNSRH-PFLTA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 117 LHYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLH-KLGIIYRDIKLENILLDSNGHVVLTD 195
Cdd:cd05594  90 LKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 196 FGLSKEFVADETERAySFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPF-TVDGEKnsqaeISRRILKS 274
Cdd:cd05594 170 FGLCKEGIKDGATMK-TFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFyNQDHEK-----LFELILME 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 275 EPPYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTE 354
Cdd:cd05594 242 EIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTA 321
                       330       340       350
                ....*....|....*....|....*....|....
gi 32528297 355 MDPTYSPAALPQSSEKL-------FQGYSFVAPS 381
Cdd:cd05594 322 QMITITPPDQDDSMETVdnerrphFPQFSYSASA 355
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
48-378 7.03e-89

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 276.88  E-value: 7.03e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKL 127
Cdd:cd05616   1 DFNFLMVLGKGSFGKVMLAER---KGTDELYAVKILKKDVVIQD-DDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd05616  77 YFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAySFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFtvDGEknSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd05616 157 TTK-TFCGTPDYIAPEIIAYQPYG--KSVDWWAFGVLLYEMLAGQAPF--EGE--DEDELFQSIMEHNVAYPKSMSKEAV 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 288 DLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDElDVSNFAEEFTEMDPTYSPA---AL 364
Cdd:cd05616 230 AICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGR-NAENFDRFFTRHPPVLTPPdqeVI 308
                       330
                ....*....|....
gi 32528297 365 PQSSEKLFQGYSFV 378
Cdd:cd05616 309 RNIDQSEFEGFSFV 322
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
53-378 1.01e-88

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 276.30  E-value: 1.01e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05591   1 KVLGKGSFGKVMLAER---KGTDEVYAIKVLKKDVILQD-DDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADEtERAYS 212
Cdd:cd05591  77 YVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNG-KTTTT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd05591 156 FCGTPDYIAPEILQELEYG--PSVDWWALGVLMYEMMAGQPPFEADNED----DLFESILHDDVLYPVWLSKEAVSILKA 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 293 LLMKDPKKRLGCGPRDADE--IKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSP---AALPQS 367
Cdd:cd05591 230 FMTKNPAKRLGCVASQGGEdaIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPvdpAVIKQI 309
                       330
                ....*....|.
gi 32528297 368 SEKLFQGYSFV 378
Cdd:cd05591 310 NQEEFRGFSFV 320
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
48-380 1.36e-88

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 276.51  E-value: 1.36e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGHdtgKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKL 127
Cdd:cd05602   8 DFHFLKVIGKGSFGKVLLARHKSDE---KFYAVKVLQKKAILKK-KEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLsQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVaDE 206
Cdd:cd05602  84 YFVLDYINGGELFYHL-QRERcFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENI-EP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQEMSALA 286
Cdd:cd05602 162 NGTTSTFCGTPEYLAPEVLH--KQPYDRTVDWWCLGAVLYEMLYGLPPFY----SRNTAEMYDNILNKPLQLKPNITNSA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 287 KDLIQRLLMKDPKKRLGcGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEM----------D 356
Cdd:cd05602 236 RHLLEGLLQKDRTKRLG-AKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEpvpnsigqspD 314
                       330       340
                ....*....|....*....|....
gi 32528297 357 PTYSPAALPQSSEKlFQGYSFVAP 380
Cdd:cd05602 315 SILVTASIKEAAEA-FLGFSYAPP 337
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
53-382 1.49e-88

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 276.02  E-value: 1.49e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05590   1 RVLGKGSFGKVMLARL---KESGRLYAVKVLKKDVILQD-DDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAyS 212
Cdd:cd05590  77 FVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTS-T 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd05590 156 FCGTPDYIAPEILQ--EMLYGPSVDWWAMGVLLYEMLCGHAPF----EAENEDDLFEAILNDEVVYPTWLSQDAVDILKA 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 293 LLMKDPKKRLGCGPRDADE-IKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSP---AALPQSS 368
Cdd:cd05590 230 FMTKNPTMRLGSLTLGGEEaILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPieeSLLPMIN 309
                       330
                ....*....|....
gi 32528297 369 EKLFQGYSFVAPSI 382
Cdd:cd05590 310 QDEFRNFSYTAPEL 323
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
55-325 2.33e-88

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 272.95  E-value: 2.33e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd05572   1 LGVGGFGRVELVQLKS---KGRTFALKCVKKRHIVQT-RQQEHIFSEKEILEECN-SPFIVKLYRTFKDKKYLYMLMEYC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERAYSFC 214
Cdd:cd05572  76 LGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAK--KLGSGRKTWTFC 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 215 GTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRILKSEPP--YPQEMSALAKDLIQR 292
Cdd:cd05572 154 GTPEYVAPEIILN--KGYDFSVDYWSLGILLYELLTGRPPFG--GDDEDPMKIYNIILKGIDKieFPKYIDKNAKNLIKQ 229
                       250       260       270
                ....*....|....*....|....*....|...
gi 32528297 293 LLMKDPKKRLGCGPRDADEIKEHLFFQKINWDD 325
Cdd:cd05572 230 LLRRNPEERLGYLKGGIRDIKKHKWFEGFDWEG 262
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
53-378 6.37e-88

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 274.30  E-value: 6.37e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKAtIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05588   1 RVIGRGSYAKVLMVELKK---TKRIYAMKVIKKE-LVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV--ADETEra 210
Cdd:cd05588  77 FVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLrpGDTTS-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 ySFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTVDG-----EKNSQAEISRRILKSEPPYPQEMSAL 285
Cdd:cd05588 155 -TFCGTPNYIAPEILRGED--YGFSVDWWALGVLMFEMLAGRSPFDIVGssdnpDQNTEDYLFQVILEKPIRIPRSLSVK 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 286 AKDLIQRLLMKDPKKRLGCGPRDA-DEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAAl 364
Cdd:cd05588 232 AASVLKGFLNKNPAERLGCHPQTGfADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQLTPDD- 310
                       330
                ....*....|....*...
gi 32528297 365 PQSSEKL----FQGYSFV 378
Cdd:cd05588 311 PDVIEKIdqseFEGFEYV 328
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
46-375 9.49e-88

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 274.00  E-value: 9.49e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   46 IENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTET 125
Cdd:PTZ00263  17 LSDFEMGETLGTGSFGRVRIAKHKG---TGEYYAIKCLKKREIL-KMKQVQHVAQEKSILMELSH-PFIVNMMCSFQDEN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvad 205
Cdd:PTZ00263  92 RVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV--- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  206 eTERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQEMSAL 285
Cdd:PTZ00263 169 -PDRTFTLCGTPEYLAPEVIQ--SKGHGKAVDWWTMGVLLYEFIAGYPPFFDD----TPFRIYEKILAGRLKFPNWFDGR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  286 AKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFaEEFTEmDPTYSPAALP 365
Cdd:PTZ00263 242 ARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNF-EKYPD-SPVDRLPPLT 319
                        330
                 ....*....|
gi 32528297  366 QSSEKLFQGY 375
Cdd:PTZ00263 320 AAQQAEFAGF 329
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
419-548 3.81e-86

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 269.17  E-value: 3.81e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 419 FYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMeaNTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVM 498
Cdd:cd14092   1 FFQNYELDLREEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL--DTSREVQLLRLCQGHPNIVKLHEVFQDELHTYLVM 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 499 ELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14092  79 ELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPE 128
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
41-383 4.92e-85

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 268.04  E-value: 4.92e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  41 AEKVGIENFELLKVLGTGAYGKVFLVRKISGHDTgklYAMKVLKKAtIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYA 120
Cdd:cd05617   9 SQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQI---YAMKVVKKE-LVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 121 FQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK 200
Cdd:cd05617  85 FQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFV--ADETEraySFCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPF---TVDGEKNSQAEISRRILKSE 275
Cdd:cd05617 165 EGLgpGDTTS---TFCGTPNYIAPEILRGEEYGF--SVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQVILEKP 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 276 PPYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDA-DEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTE 354
Cdd:cd05617 240 IRIPRFLSVKASHVLKGFLNKDPKERLGCQPQTGfSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTS 319
                       330       340       350
                ....*....|....*....|....*....|..
gi 32528297 355 MDPTYSP---AALPQSSEKLFQGYSFVAPSIL 383
Cdd:cd05617 320 EPVQLTPddeDVIKRIDQSEFEGFEYINPLLL 351
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
47-350 1.38e-84

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 264.27  E-value: 1.38e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVqKAKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTETK 126
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRH---KETGNYYAMKILDKQKVV-KLKQVEHTLNEKRILQAIN-FPFLVKLEYSFKDNSN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvade 206
Cdd:cd14209  76 LYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV---- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQEMSALA 286
Cdd:cd14209 152 KGRTWTLCGTPEYLAPEIIL--SKGYNKAVDWWALGVLIYEMAAGYPPFFAD----QPIQIYEKIVSGKVRFPSHFSSDL 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 287 KDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAE 350
Cdd:cd14209 226 KDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFDD 289
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
49-370 1.78e-84

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 265.72  E-value: 1.78e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLH 128
Cdd:cd05598   3 FEKIKTIGVGAFGEVSLVRK---KDTNALYAMKTLRKKDVLKR-NQVAHVKAERDILAEA-DNEWVVKLYYSFQDKENLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGL---------S 199
Cdd:cd05598  78 FVMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KEFVadeterAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVdgekNSQAEISRRILKSE---- 275
Cdd:cd05598 158 KYYL------AHSLVGTPNYIAPEVLL--RTGYTQLCDWWSVGVILYEMLVGQPPFLA----QTPAETQLKVINWRttlk 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 276 -PPYPQeMSALAKDLIQRLLMkDPKKRLGCGprDADEIKEHLFFQKINWDDLaaKKVPAPFKPVIRDELDVSNFaeefte 354
Cdd:cd05598 226 iPHEAN-LSPEAKDLILRLCC-DAEDRLGRN--GADEIKAHPFFAGIDWEKL--RKQKAPYIPTIRHPTDTSNF------ 293
                       330
                ....*....|....*.
gi 32528297 355 mDPTySPAALPQSSEK 370
Cdd:cd05598 294 -DPV-DPEKLRSSDEE 307
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
47-348 4.16e-84

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 263.14  E-value: 4.16e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVR-KISGHdtgkLYAMKVLKKATIVqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTET 125
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRdRISEH----YYALKVMAIPEVI-RLKQEQHVHNEKRVLKEVSH-PFIIRLFWTEHDQR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVad 205
Cdd:cd05612  75 FLYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 etERAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQEMSAL 285
Cdd:cd05612 153 --DRTWTLCGTPEYLAPEVI--QSKGHNKAVDWWALGILIYEMLVGYPPFFDD----NPFGIYEKILAGKLEFPRHLDLY 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 286 AKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNF 348
Cdd:cd05612 225 AKDLIKKLLVVDRTRRLGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNF 287
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
44-383 5.14e-84

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 265.74  E-value: 5.14e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  44 VGIENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKAtIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQT 123
Cdd:cd05618  17 LGLQDFDLLRVIGRGSYAKVLLVRL---KKTERIYAMKVVKKE-LVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV 203
Cdd:cd05618  93 ESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 --ADETEraySFCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDG-----EKNSQAEISRRILKSEP 276
Cdd:cd05618 173 rpGDTTS---TFCGTPNYIAPEILRGEDYGF--SVDWWALGVLMFEMMAGRSPFDIVGssdnpDQNTEDYLFQVILEKQI 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 277 PYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDA-DEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEM 355
Cdd:cd05618 248 RIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGfADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNE 327
                       330       340       350
                ....*....|....*....|....*....|.
gi 32528297 356 DPTYSP---AALPQSSEKLFQGYSFVAPSIL 383
Cdd:cd05618 328 PVQLTPdddDIVRKIDQSEFEGFEYINPLLM 358
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
55-337 3.87e-83

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 260.15  E-value: 3.87e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIvQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd05577   1 LGRGGFGEVCACQV---KATGKMYACKKLDKKRI-KKKKGETMALNEKIILEKV-SSPFIVSLAYAFETKDKLCLVLTLM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRER--FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYS 212
Cdd:cd05577  76 NGGDLKYHIYNVGTrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 fcGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd05577 156 --GTHGYMAPEVLQKEVA-YDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEG 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 32528297 293 LLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05577 233 LLQKDPERRLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
38-383 1.35e-82

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 261.08  E-value: 1.35e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  38 TGHAEKVGIENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQSPFLVTL 117
Cdd:cd05615   1 SNNLDRVRLTDFNFLMVLGKGSFGKVMLAERKG---SDELYAIKILKKDVVIQD-DDVECTMVEKRVLALQDKPPFLTQL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 118 HYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd05615  77 HSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEFVADE-TERaySFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFtvDGEknSQAEISRRILKSEP 276
Cdd:cd05615 157 MCKEHMVEGvTTR--TFCGTPDYIAPEIIAYQPYG--RSVDWWAYGVLLYEMLAGQPPF--DGE--DEDELFQSIMEHNV 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 277 PYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDElDVSNFAEEFTEMD 356
Cdd:cd05615 229 SYPKSLSKEAVSICKGLMTKHPAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGK-GAENFDKFFTRGQ 307
                       330       340       350
                ....*....|....*....|....*....|...
gi 32528297 357 PTYSP------AALPQSSeklFQGYSFVAPSIL 383
Cdd:cd05615 308 PVLTPpdqlviANIDQAD---FEGFSYVNPQFV 337
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
48-318 1.46e-82

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 257.96  E-value: 1.46e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd05578   1 HFQILRVIGKGSFGKVCIVQK---KDTKKMFAMKYMNKQKCIEK-DSVRNVLNELEILQELEH-PFLVNLWYSFQDEEDM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADet 207
Cdd:cd05578  76 YMVVDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDG-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQaEISRRILKSEPPYPQEMSALAK 287
Cdd:cd05578 154 TLATSTSGTKPYMAPEVFMR--AGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIE-EIRAKFETASVLYPAGWSEEAI 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 32528297 288 DLIQRLLMKDPKKRLGCgprdADEIKEHLFF 318
Cdd:cd05578 231 DLINKLLERDPQKRLGD----LSDLKNHPYF 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
48-319 4.47e-82

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 256.63  E-value: 4.47e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIvQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKK---SGFIVALKVISKSQL-QKSGLEHQLRREIEIQSHLRH-PNILRLYGYFEDKKRI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfvaDET 207
Cdd:cd14007  76 YLILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVH---APS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd14007 153 NRRKTFCGTLDYLPPEMVEGKE--YDYKVDIWSLGVLCYELLVGKPPF----ESKSHQETYKRIQNVDIKFPSSVSPEAK 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 32528297 288 DLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd14007 227 DLISKLLQKDPSKRL-----SLEQVLNHPWIK 253
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
43-382 8.12e-82

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 258.70  E-value: 8.12e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  43 KVGIENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKaTIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQ 122
Cdd:cd05619   1 KLTIEDFVLHKMLGKGSFGKVFLAELKG---TNQFFAIKALKK-DVVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF 202
Cdd:cd05619  77 TKENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKEN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETeRAYSFCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEM 282
Cdd:cd05619 157 MLGDA-KTSTFCGTPDYIAPEILLGQKYNT--SVDWWSFGVLLYEMLIGQSPFHGQDEE----ELFQSIRMDNPFYPRWL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 283 SALAKDLIQRLLMKDPKKRLGCgprdADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPA 362
Cdd:cd05619 230 EKEAKDILVKLFVREPERRLGV----RGDIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEFLNEKPRLSFA 305
                       330       340
                ....*....|....*....|...
gi 32528297 363 --ALPQS-SEKLFQGYSFVAPSI 382
Cdd:cd05619 306 drALINSmDQNMFRNFSFVNPKM 328
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
53-380 4.04e-81

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 256.41  E-value: 4.04e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVrKISGhdTGKLYAMKVLKKaTIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd05620   1 KVLGKGSFGKVLLA-ELKG--KGEYFAVKALKK-DVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETeRAYS 212
Cdd:cd05620  77 FLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDN-RAST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnsqaEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd05620 156 FCGTPDYIAPEILQG--LKYTFSVDWWSFGVLLYEMLIGQSPFHGDDED----ELFESIRVDTPHYPRWITKESKDILEK 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 293 LLMKDPKKRLGCgprdADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDP--TYSPAALPQSSEK 370
Cdd:cd05620 230 LFERDPTRRLGV----VGNIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPrlSYSDKNLIDSMDQ 305
                       330
                ....*....|.
gi 32528297 371 -LFQGYSFVAP 380
Cdd:cd05620 306 sAFAGFSFINP 316
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
49-337 4.42e-81

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 254.97  E-value: 4.42e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFL--VRKisghdTGKLYAMKVLKKATIvQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd05605   2 FRQYRVLGKGGFGEVCAcqVRA-----TGKMYACKKLEKKRI-KKRKGEAMALNEKQILEKV-NSRFVVSLAYAYETKDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRER--FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd05605  75 LCLVLTIMNGGDLKFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYsfCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd05605 155 GETIRGR--VGTVGYMAPEVVKNERYTF--SPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEKFSE 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 285 LAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05605 231 EAKSICSQLLQKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
47-318 1.86e-80

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 253.29  E-value: 1.86e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTtEHTRTERQVLEHIRqSPFLVTLHYAFQTETK 126
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEK---ETGKEYAIKVLDKRHIIKEKKV-KYVTIEKEVLSRLA-HPGIVKLYYTFQDESK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK------ 200
Cdd:cd05581  76 LYFVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKvlgpds 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 -----EFVADETE-----RAYSFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRR 270
Cdd:cd05581 156 spestKGDADSQIaynqaRAASFVGTAEYVSPELLNEKPAG--KSSDLWALGCIIYQMLTGKPPF----RGSNEYLTFQK 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 271 ILKSEPPYPQEMSALAKDLIQRLLMKDPKKRLGCGP-RDADEIKEHLFF 318
Cdd:cd05581 230 IVKLEYEFPENFPPDAKDLIQKLLVLDPSKRLGVNEnGGYDELKAHPFF 278
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
47-377 3.83e-80

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 254.19  E-value: 3.83e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHtRTERQVLEHiRQSPFLVTLHYAFQTETK 126
Cdd:cd05597   1 DDFEILKVIGRGAFGEVAVVKLKS---TEKVYAMKILNKWEMLKRAETACF-REERDVLVN-GDRRWITKLHYAFQDENY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd05597  76 LYLVMDYYCGGDLLTLLSKFEdRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLRED 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGDSGHDK---AVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSE-----PP 277
Cdd:cd05597 156 GTVQSSVAVGTPDYISPEILQAMEDGKGRygpECDWWSLGVCMYEMLYGETPFYAE----SLVETYGKIMNHKehfsfPD 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 278 YPQEMSALAKDLIQRLLMkDPKKRLGCGprDADEIKEHLFFQKINWDDLaaKKVPAPFKPVIRDELDVSNF---AEEFTE 354
Cdd:cd05597 232 DEDDVSEEAKDLIRRLIC-SRERRLGQN--GIDDFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNFdvdDDDLRH 306
                       330       340
                ....*....|....*....|....
gi 32528297 355 MDPTYSPAALPQSSEKL-FQGYSF 377
Cdd:cd05597 307 TDSLPPPSNAAFSGLHLpFVGFTY 330
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
48-315 7.21e-80

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 250.86  E-value: 7.21e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIvqKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKL 127
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKK---TGEEYAVKIIDKKKL--KSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS---NGHVVLTDFGLSKEFva 204
Cdd:cd05117  75 YLVMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASkdpDSPIKIIDFGLAKIF-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvDGEknSQAEISRRILKS----EPPYPQ 280
Cdd:cd05117 153 EEGEKLKTVCGTPYYVAPEVLKG--KGYGKKCDIWSLGVILYILLCGYPPF--YGE--TEQELFEKILKGkysfDSPEWK 226
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 281 EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd05117 227 NVSEEAKDLIKRLLVVDPKKRL-----TAAEALNH 256
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
48-315 3.45e-79

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 248.97  E-value: 3.45e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIvqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHK---LTGEKVAIKIIDKSKL--KEEIEEKIKREIEIMKLLNH-PNIIKLYEVIETENKI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADet 207
Cdd:cd14003  75 YLVMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGG-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd14003 153 SLLKTFCGTPAYAAPEVLL-GRKYDGPKADVWSLGVILYAMLTGYLPFDDD----NDSKLFRKILKGKYPIPSHLSPDAR 227
                       250       260
                ....*....|....*....|....*...
gi 32528297 288 DLIQRLLMKDPKKRLGcgprdADEIKEH 315
Cdd:cd14003 228 DLIRRMLVVDPSKRIT-----IEEILNH 250
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
54-337 4.27e-77

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 244.65  E-value: 4.27e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQ---SPFLVTLHYAFQTETKLHLI 130
Cdd:cd05606   1 IIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGET-LALNERIMLSLVSTggdCPFIVCMTYAFQTPDKLCFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvadETERA 210
Cdd:cd05606  77 LDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDF---SKKKP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 YSFCGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQaEISRRILKSEPPYPQEMSALAKDLI 290
Cdd:cd05606 154 HASVGTHGYMAPEVLQKGVA-YDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKH-EIDRMTLTMNVELPDSFSPELKSLL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 291 QRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05606 232 EGLLQRDVSKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
419-548 1.43e-75

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 241.70  E-value: 1.43e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 419 FYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVM 498
Cdd:cd14180   1 FFQCYELDLEEPALGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVM 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 499 ELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14180  81 ELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPE 130
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
52-324 8.72e-73

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 232.76  E-value: 8.72e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLIL 131
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRS---TGDYFAIKVLKKSDMIAKNQVT-NVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERAY 211
Cdd:cd05611  77 EYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSR--NGLEKRHNK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQE----MSALAK 287
Cdd:cd05611 155 KFVGTPDYLAPETILG--VGDDKMSDWWSLGCVIFEFLFGYPPF----HAETPDAVFDNILSRRINWPEEvkefCSPEAV 228
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 288 DLIQRLLMKDPKKRLGCgpRDADEIKEHLFFQKINWD 324
Cdd:cd05611 229 DLINRLLCMDPAKRLGA--NGYQEIKSHPFFKSINWD 263
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
49-353 5.84e-72

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 234.93  E-value: 5.84e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATiVQKAKTTEHTRTERQVLEhIRQSPFLVTLHYAFQTETKLH 128
Cdd:cd05600  13 FQILTQVGQGGYGSVFLARK---KDTGEICALKIMKKKV-LFKLNEVNHVLTERDILT-TTNSPWLVKLLYAFQDPENVY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV----- 203
Cdd:cd05600  88 LAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTLspkki 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 -------------------------------ADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGA 252
Cdd:cd05600 168 esmkirleevkntafleltakerrniyramrKEDQNYANSVVGSPDYMAPEVLRG--EGYDLTVDYWSLGCILFECLVGF 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 253 SPFTVDGEKNSQA------EISRRILKSEPPYPQEMSALAKDLIQRLLMkDPKKRLgCGPRDadeIKEHLFFQKINWDDL 326
Cdd:cd05600 246 PPFSGSTPNETWAnlyhwkKTLQRPVYTDPDLEFNLSDEAWDLITKLIT-DPQDRL-QSPEQ---IKNHPFFKNIDWDRL 320
                       330       340
                ....*....|....*....|....*..
gi 32528297 327 AAKKVPaPFKPVIRDELDVSNFaEEFT 353
Cdd:cd05600 321 REGSKP-PFIPELESEIDTSYF-DDFN 345
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
47-377 7.20e-72

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 234.36  E-value: 7.20e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHiRQSPFLVTLHYAFQTETK 126
Cdd:cd05629   1 EDFHTVKVIGKGAFGEVRLVQKK---DTGKIYAMKTLLKSEMFKKDQLA-HVKAERDVLAE-SDSPWVVSLYYSFQDAQY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF---- 202
Cdd:cd05629  76 LYLIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFhkqh 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 --------------------------------------VAD--ETER--AYSFCGTIEYMAPDIVRGGDSGHDkaVDWWS 240
Cdd:cd05629 156 dsayyqkllqgksnknridnrnsvavdsinltmsskdqIATwkKNRRlmAYSTVGTPDYIAPEIFLQQGYGQE--CDWWS 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 241 LGVLMYELLTGASPFTvdgEKNSQaEISRRILKSEPP--YPQE--MSALAKDLIQRlLMKDPKKRLGCGprDADEIKEHL 316
Cdd:cd05629 234 LGAIMFECLIGWPPFC---SENSH-ETYRKIINWRETlyFPDDihLSVEAEDLIRR-LITNAENRLGRG--GAHEIKSHP 306
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 317 FFQKINWDDLaaKKVPAPFKPVIRDELDVSNFAEEFTEMDP--TYSPAALPQSSEKL------FQGYSF 377
Cdd:cd05629 307 FFRGVDWDTI--RQIRAPFIPQLKSITDTSYFPTDELEQVPeaPALKQAAPAQQEESveldlaFIGYTY 373
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
47-374 1.37e-71

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 231.82  E-value: 1.37e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHtRTERQVLEHiRQSPFLVTLHYAFQTETK 126
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKA---TGDIYAMKVLKKSETLAQEEVSFF-EEERDIMAK-ANSPWITKLQYAFQDSEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd05601  76 LYLVMEYHPGGDLLSLLSRYDdIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIV----RGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISrRIL--KSEPPYP 279
Cdd:cd05601 156 KTVTSKMPVGTPDYIAPEVLtsmnGGSKGTYGVECDWWSLGIVAYEMLYGKTPFT---EDTVIKTYS-NIMnfKKFLKFP 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 280 QE--MSALAKDLIQRLLmKDPKKRLGcgprdADEIKEHLFFQKINWDDLaaKKVPAPFKPVIRDELDVSNFaEEFTEMDP 357
Cdd:cd05601 232 EDpkVSESAVDLIKGLL-TDAKERLG-----YEGLCCHPFFSGIDWNNL--RQTVPPFVPTLTSDDDTSNF-DEFEPKKT 302
                       330
                ....*....|....*..
gi 32528297 358 TysPAALPQSSEKLFQG 374
Cdd:cd05601 303 R--PSYENFNKSKGFSG 317
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
47-375 7.30e-71

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 232.59  E-value: 7.30e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHtRTERQVLEHiRQSPFLVTLHYAFQTETK 126
Cdd:cd05624  72 DDFEIIKVIGRGAFGEVAVVKMKN---TERIYAMKILNKWEMLKRAETACF-REERNVLVN-GDCQWITTLHYAFQDENY 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd05624 147 LYLVMDYYVGGDLLTLLSKFEdKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDD 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGDSGHDK---AVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSE-----PP 277
Cdd:cd05624 227 GTVQSSVAVGTPDYISPEILQAMEDGMGKygpECDWWSLGVCMYEMLYGETPFYAE----SLVETYGKIMNHEerfqfPS 302
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 278 YPQEMSALAKDLIQRLLMKDpKKRLgcGPRDADEIKEHLFFQKINWDDLaaKKVPAPFKPVIRDELDVSNFAeefTEMDP 357
Cdd:cd05624 303 HVTDVSEEAKDLIQRLICSR-ERRL--GQNGIEDFKKHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNFD---VDDDV 374
                       330
                ....*....|....*...
gi 32528297 358 TYSPAALPQSSEKLFQGY 375
Cdd:cd05624 375 LRNPEILPPSSHTGFSGL 392
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
49-337 1.98e-70

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 227.46  E-value: 1.98e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIvQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLH 128
Cdd:cd05608   3 FLDFRVLGKGGFGEVSACQMRA---TGKLYACKKLNKKRL-KKRKGYEGAMVEKRILAKV-HSRFIVSLAYAFQTKTDLC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRER----FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVA 204
Cdd:cd05608  78 LVMTIMNGGDLRYHIYNVDEenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVE-LK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd05608 157 DGQTKTKGYAGTPGFMAPELLLGEE--YDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSP 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 285 LAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05608 235 ASKSICEALLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
46-378 4.57e-69

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 226.10  E-value: 4.57e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRkisgH-DTGKLYAMKVLKKATIVQKAKTT---EhtrtERQVLEHIRqSPFLVTLHYAF 121
Cdd:cd05596  25 AEDFDVIKVIGRGAFGEVQLVR----HkSTKKVYAMKLLSKFEMIKRSDSAffwE----ERDIMAHAN-SEWIVQLHYAF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQRErFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd05596  96 QDDKYLYMVMDYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMK 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETERAYSFCGTIEYMAPDIVR--GGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYP 279
Cdd:cd05596 175 MDKDGLVRSDTAVGTPDYISPEVLKsqGGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKNSLQFPDD 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 280 QEMSALAKDLIQRLLMkDPKKRLgcGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFaEEFTEMDPty 359
Cdd:cd05596 255 VEISKDAKSLICAFLT-DREVRL--GRNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNF-DDIEEDET-- 328
                       330       340
                ....*....|....*....|....
gi 32528297 360 SPAALPQSSEKL-----FQGYSFV 378
Cdd:cd05596 329 PEETFPVPKAFVgnhlpFVGFTYS 352
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
49-337 2.92e-68

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 221.82  E-value: 2.92e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFL--VRKisghdTGKLYAMKVLKKATIvQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd05630   2 FRQYRVLGKGGFGEVCAcqVRA-----TGKMYACKKLEKKRI-KKRKGEAMALNEKQILEKV-NSRFVVSLAYAYETKDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQ--RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd05630  75 LCLVLTLMNGGDLKFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYsfCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd05630 155 GQTIKGR--VGTVGYMAPEVVK--NERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSP 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 285 LAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05630 231 QARSLCSMLLCKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
49-337 1.27e-64

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 212.55  E-value: 1.27e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFL--VRKisghdTGKLYAMKVLKKATIvQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd05631   2 FRHYRVLGKGGFGEVCAcqVRA-----TGKMYACKKLEKKRI-KKRKGEAMALNEKRILEKV-NSRFVVSLAYAYETKDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQ--RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd05631  75 LCLVLTIMNGGDLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYsfCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd05631 155 GETVRGR--VGTVGYMAPEVIN--NEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEKFSE 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 285 LAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05631 231 DAKSICRMLLTKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
26-348 9.45e-64

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 211.76  E-value: 9.45e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   26 LTVKHELRTANLTGHAEKVGIENFELLKVLGTGAYGKVFLVRKISGHDTGklYAMKVLKKATIVqKAKTTEHTRTERQVL 105
Cdd:PTZ00426   9 LHKKKDSDSTKEPKRKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDFPP--VAIKRFEKSKII-KQKQVDHVFSERKIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  106 EHIRQsPFLVTLHYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL 185
Cdd:PTZ00426  86 NYINH-PFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  186 DSNGHVVLTDFGLSKefVADetERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVdgekNSQA 265
Cdd:PTZ00426 165 DKDGFIKMTDFGFAK--VVD--TRTYTLCGTPEYIAPEILL--NVGHGKAADWWTLGIFIYEILVGCPPFYA----NEPL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  266 EISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDV 345
Cdd:PTZ00426 235 LIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDS 314

                 ...
gi 32528297  346 SNF 348
Cdd:PTZ00426 315 SNF 317
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
46-354 4.83e-63

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 210.30  E-value: 4.83e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQS--PFLVTLHYAFQT 123
Cdd:cd05633   4 MNDFSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGET-LALNERIMLSLVSTGdcPFIVCMTYAFHT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFv 203
Cdd:cd05633  80 PDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDF- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 adETERAYSFCGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQaEISRRILKSEPPYPQEMS 283
Cdd:cd05633 159 --SKKKPHASVGTHGYMAPEVLQKG-TAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIDRMTLTVNVELPDSFS 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 284 ALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPV-----IRDELDVSNFAEEFTE 354
Cdd:cd05633 235 PELKSLLEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPPrgevnAADAFDIGSFDEEDTK 310
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
47-349 4.85e-63

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 209.06  E-value: 4.85e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIvQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd05632   2 NTFRQYRVLGKGGFGEVCACQVRA---TGKMYACKRLEKKRI-KKRKGESMALNEKQILEKV-NSQFVVNLAYAYETKDA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQ--RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd05632  77 LCLVLTIMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYsfCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd05632 157 GESIRGR--VGTVGYMAPEVLN--NQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKFSE 232
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 285 LAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIR-----DELDVSNFA 349
Cdd:cd05632 233 EAKSICKMLLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVPDPRavyckDVLDIEQFS 302
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
48-354 6.52e-63

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 209.13  E-value: 6.52e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQS--PFLVTLHYAFQTET 125
Cdd:cd14223   1 DFSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGET-LALNERIMLSLVSTGdcPFIVCMSYAFHTPD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvad 205
Cdd:cd14223  77 KLSFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDF--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQaEISRRILKSEPPYPQEMSAL 285
Cdd:cd14223 154 SKKKPHASVGTHGYMAPEVLQKG-VAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIDRMTLTMAVELPDSFSPE 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 286 AKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPV-----IRDELDVSNFAEEFTE 354
Cdd:cd14223 232 LRSLLEGLLQRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPPrgevnAADAFDIGSFDEEDTK 305
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
46-386 3.23e-62

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 208.76  E-value: 3.23e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIrQSPFLVTLHYAFQTET 125
Cdd:cd05627   1 LDDFESLKVIGRGAFGEVRLVQK---KDTGHIYAMKILRKADMLEKEQVA-HIRAERDILVEA-DGAWVVKMFYSFQDKR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGL------- 198
Cdd:cd05627  76 NLYLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLctglkka 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 -SKEFVADET--------------------------ERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd05627 156 hRTEFYRNLThnppsdfsfqnmnskrkaetwkknrrQLAYSTVGTPDYIAPEVFM--QTGYNKLCDWWSLGVIMYEMLIG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 252 ASPFTVDGEKNSQAEIS--RRILKSEPPYPqeMSALAKDLIQRLLMkDPKKRLGCGprDADEIKEHLFFQKINWDDLaaK 329
Cdd:cd05627 234 YPPFCSETPQETYRKVMnwKETLVFPPEVP--ISEKAKDLILRFCT-DAENRIGSN--GVEEIKSHPFFEGVDWEHI--R 306
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 330 KVPAPFKPVIRDELDVSNFaEEFTEMDpTYSPAalPQSSEKLFQGYSFVAPSILFKR 386
Cdd:cd05627 307 ERPAAIPIEIKSIDDTSNF-DDFPESD-ILQPA--PNTTEPDYKSKDWVFLNYTYKR 359
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
48-323 3.87e-62

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 205.72  E-value: 3.87e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTtEHTRTERQVLEhIRQSPFLVTLHYAFQTETKL 127
Cdd:cd05609   1 DFETIKLISNGAYGAVYLVRH---RETRQRFAMKKINKQNLILRNQI-QQVFVERDILT-FAENPFVVSMYCSFETKRHL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd05609  76 CMVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAY--------------SFCGTIEYMAPD-IVRggdSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRIL 272
Cdd:cd05609 156 TNLYeghiekdtrefldkQVCGTPEYIAPEvILR---QGYGKPVDWWAMGIILYEFLVGCVPFFGD----TPEELFGQVI 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 273 KSEPPYPQEMSAL---AKDLIQRLLMKDPKKRLGCGprDADEIKEHLFFQKINW 323
Cdd:cd05609 229 SDEIEWPEGDDALpddAQDLITRLLQQNPLERLGTG--GAEEVKQHPFFQDLDW 280
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
47-375 4.87e-62

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 209.49  E-value: 4.87e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTEHtRTERQVLEHiRQSPFLVTLHYAFQTETK 126
Cdd:cd05623  72 EDFEILKVIGRGAFGEVAVVKL---KNADKVFAMKILNKWEMLKRAETACF-REERDVLVN-GDSQWITTLHYAFQDDNN 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd05623 147 LYLVMDYYVGGDLLTLLSKFEdRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMED 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGDSGHDK---AVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSE-----PP 277
Cdd:cd05623 227 GTVQSSVAVGTPDYISPEILQAMEDGKGKygpECDWWSLGVCMYEMLYGETPFYAE----SLVETYGKIMNHKerfqfPT 302
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 278 YPQEMSALAKDLIQRLLMKDpKKRLgcGPRDADEIKEHLFFQKINWDDLaaKKVPAPFKPVIRDELDVSNFAeefTEMDP 357
Cdd:cd05623 303 QVTDVSENAKDLIRRLICSR-EHRL--GQNGIEDFKNHPFFVGIDWDNI--RNCEAPYIPEVSSPTDTSNFD---VDDDC 374
                       330
                ....*....|....*...
gi 32528297 358 TYSPAALPQSSEKLFQGY 375
Cdd:cd05623 375 LKNCETMPPPTHTAFSGH 392
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
46-348 1.37e-60

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 203.96  E-value: 1.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEhIRQSPFLVTLHYAFQTET 125
Cdd:cd05610   3 IEEFVIVKPISRGAFGKVYLGRK---KNNSKLYAVKVVKKADMINK-NMVHQVQAERDALA-LSKSPFIVHLYYSLQSAN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd05610  78 NVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETE--------------RAYS--------------------------------------FCGTIEYMAPDIVRGgdSGHD 233
Cdd:cd05610 158 ELNmmdilttpsmakpkNDYSrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLG--KPHG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 234 KAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYP---QEMSALAKDLIQRLLMKDPKKRLGcgprdAD 310
Cdd:cd05610 236 PAVDWWALGVCLFEFLTGIPPFN----DETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAG-----LK 306
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 32528297 311 EIKEHLFFQKINWDDLAAKkvPAPFKPVIRDELDVSNF 348
Cdd:cd05610 307 ELKQHPLFHGVDWENLQNQ--TMPFIPQPDDETDTSYF 342
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
46-316 1.68e-60

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 207.56  E-value: 1.68e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKkATIVQKAKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTET 125
Cdd:COG0515   6 LGRYRILRLLGRGGMGVVYLARDL---RLGRPVALKVLR-PELAADPEARERFRREARALARLN-HPNIVRVYDVGEEDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:COG0515  81 RPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQEMS-- 283
Cdd:COG0515 161 TLTQTGTVVGTPGYMAPEQARGEPVDP--RSDVYSLGVTLYELLTGRPPFDGD----SPAELLRAHLREPPPPPSELRpd 234
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32528297 284 ---ALAkDLIQRLLMKDPKKRlgcgPRDADEIKEHL 316
Cdd:COG0515 235 lppALD-AIVLRALAKDPEER----YQSAAELAAAL 265
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
48-316 1.91e-60

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 200.51  E-value: 1.91e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkATIVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKL 127
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTL---LGRPVAIKVLR-PELAEDEEFRERFLREARALARL-SHPNIVRVYDVGEDDGRP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd14014  76 YIVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFCGTIEYMAPDIVRGGDSghDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd14014 156 TQTGSVLGTPAYMAPEQARGGPV--DPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALD 233
                       250       260
                ....*....|....*....|....*....
gi 32528297 288 DLIQRLLMKDPKKRlgcgPRDADEIKEHL 316
Cdd:cd14014 234 AIILRALAKDPEER----PQSAAELLAAL 258
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
47-386 1.65e-59

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 201.81  E-value: 1.65e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd05628   1 EDFESLKVIGRGAFGEVRLVQK---KDTGHVYAMKILRKADMLEKEQVG-HIRAERDILVEA-DSLWVVKMFYSFQDKLN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGL-------- 198
Cdd:cd05628  76 LYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLctglkkah 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 --------------------------SKEFVADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGA 252
Cdd:cd05628 156 rtefyrnlnhslpsdftfqnmnskrkAETWKRNRRQLAFSTVGTPDYIAPEVFM--QTGYNKLCDWWSLGVIMYEMLIGY 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 253 SPFTVDGEKNSQAEIS--RRILKSEPPYPqeMSALAKDLIQRLLMKDPKKrlgCGPRDADEIKEHLFFQKINWDDLaaKK 330
Cdd:cd05628 234 PPFCSETPQETYKKVMnwKETLIFPPEVP--ISEKAKDLILRFCCEWEHR---IGAPGVEEIKTNPFFEGVDWEHI--RE 306
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 331 VPAPFKPVIRDELDVSNFaEEFTEMDPTYSPAALPQSSEKLFQGYSFVAPSILFKR 386
Cdd:cd05628 307 RPAAIPIEIKSIDDTSNF-DEFPDSDILKPSVAVSNHPETDYKNKDWVFINYTYKR 361
Pkinase pfam00069
Protein kinase domain;
49-318 1.99e-59

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 196.31  E-value: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIvqKAKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTETKLH 128
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKEKI--KKKKDKNILREIKILKKLN-HPNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLgiiyrdiklenilldsnghvvltdfglskefvadete 208
Cdd:pfam00069  75 LVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLESGSSL------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   209 raYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILkSEPPYPQEMSALAKD 288
Cdd:pfam00069 118 --TTFVGTPWYMAPEVLGG--NPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPY-AFPELPSNLSEEAKD 192
                         250       260       270
                  ....*....|....*....|....*....|
gi 32528297   289 LIQRLLMKDPKKRLGcgprdADEIKEHLFF 318
Cdd:pfam00069 193 LLKKLLKKDPSKRLT-----ATQALQHPWF 217
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
48-312 7.75e-59

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 196.14  E-value: 7.75e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIvqKAKTTEHTRTERQVL---EHirqsPFLVTLHYAFQTE 124
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKS---DGKLYVLKEIDLSNM--SEKEREEALNEVKLLsklKH----PNIVKYYESFEEN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQR----ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK 200
Cdd:cd08215  72 GKLCIVMEYADGGDLAQKIKKQkkkgQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFvADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPP--- 277
Cdd:cd08215 152 VL-ESTTDLAKTVVGTPYYLSPELCEN--KPYNYKSDIWALGCVLYELCTLKHPF----EANNLPALVYKIVKGQYPpip 224
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 278 --YPQEMsalaKDLIQRLLMKDPKKRlgcgPrDADEI 312
Cdd:cd08215 225 sqYSSEL----RDLVNSMLQKDPEKR----P-SANEI 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
55-315 8.33e-57

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 191.23  E-value: 8.33e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQS---------PFLVTLHYAF--QT 123
Cdd:cd14008   1 LGRGSFGKVKLALDT---ETGQLYAIKIFNKSRLRKRREGKNDRGKIKNALDDVRREiaimkkldhPNIVRLYEVIddPE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGEL--FTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSkE 201
Cdd:cd14008  78 SDKLYLVLEYCEGGPVmeLDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVS-E 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETERAYSFCGTIEYMAPDIVRGGDSGHD-KAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKS--EPPY 278
Cdd:cd14008 157 MFEDGNDTLQKTAGTPAFLAPELCDGDSKTYSgKAADIWALGVTLYCLVFGRLPF----NGDNILELYEAIQNQndEFPI 232
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 279 PQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14008 233 PPELSPELKDLLRRMLEKDPEKRI-----TLKEIKEH 264
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
53-318 8.74e-57

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 190.84  E-value: 8.74e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIvQKAKTTEHTRTERQV---LEHirqsPFLVTLHYAFQTETKLHL 129
Cdd:cd14099   7 KFLGKGGFAKCYEVTDMS---TGKVYAGKVVPKSSL-TKPKQREKLKSEIKIhrsLKH----PNIVKFHDCFEDEENVYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVADETER 209
Cdd:cd14099  79 LLELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAAR-LEYDGER 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 AYSFCGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILK---SEPPYPqEMSALA 286
Cdd:cd14099 158 KKTLCGTPNYIAPEVLEKK-KGHSFEVDIWSLGVILYTLLVGKPPF----ETSDVKETYKRIKKneySFPSHL-SISDEA 231
                       250       260       270
                ....*....|....*....|....*....|..
gi 32528297 287 KDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14099 232 KDLIRSMLQPDPTKRP-----SLDEILSHPFF 258
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
53-318 3.73e-56

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 188.88  E-value: 3.73e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRkisGHDTGKLYAMKVLKKATIVQKakTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd06606   6 ELLGKGSFGSVYLAL---NLDTGELMAVKEVELSGDSEE--ELEALEREIRILSSL-KHPNIVRYLGTERTENTLNIFLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERA-Y 211
Cdd:cd06606  80 YVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGtK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVRGGdsGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRRILKSE--PPYPQEMSALAKDL 289
Cdd:cd06606 160 SLRGTPYWMAPEVIRGE--GYGRAADIWSLGCTVIEMATGKPPW---SELGNPVAALFKIGSSGepPPIPEHLSEEAKDF 234
                       250       260
                ....*....|....*....|....*....
gi 32528297 290 IQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd06606 235 LRKCLQRDPKKRP-----TADELLQHPFL 258
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
49-348 1.44e-55

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 191.38  E-value: 1.44e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIrQSPFLVTLHYAFQTETKLH 128
Cdd:cd05626   3 FVKIKTLGIGAFGEVCLACKV---DTHALYAMKTLRKKDVLNRNQVA-HVKAERDILAEA-DNEWVVKLYYSFQDKDNLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF------ 202
Cdd:cd05626  78 FVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFrwthns 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 --------------------------------------VADETER--AYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLG 242
Cdd:cd05626 158 kyyqkgshirqdsmepsdlwddvsncrcgdrlktleqrATKQHQRclAHSLVGTPNYIAPEVLL--RKGYTQLCDWWSVG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 243 VLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKdPKKRLgcGPRDADEIKEHLFFQKIN 322
Cdd:cd05626 236 VILFEMLVGQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCS-AEERL--GRNGADDIKAHPFFSEVD 312
                       330       340
                ....*....|....*....|....*.
gi 32528297 323 WDDlAAKKVPAPFKPVIRDELDVSNF 348
Cdd:cd05626 313 FSS-DIRTQPAPYVPKISHPMDTSNF 337
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
55-316 3.49e-55

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 185.17  E-value: 3.49e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKIsghDTGKLYAMKVLKKAtivQKAKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd00180   1 LGKGSFGKVYKARDK---ETGKKVAVKVIPKE---KLKKLLEELLREIEILKKLN-HPNIVKLYDVFETENFLYLVMEYC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYS- 212
Cdd:cd00180  74 EGGSLKDLLKENKgPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTg 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELltgaspftvdgeknsqaeisrrilkseppypqemsALAKDLIQR 292
Cdd:cd00180 154 GTTPPYYAPPELLGGRY--YGPKVDIWSLGVILYEL-----------------------------------EELKDLIRR 196
                       250       260
                ....*....|....*....|....
gi 32528297 293 LLMKDPKKRLgcgprDADEIKEHL 316
Cdd:cd00180 197 MLQYDPKKRP-----SAKELLEHL 215
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
49-337 4.28e-55

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 187.42  E-value: 4.28e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIvqKAKTTEHTRT-ERQVLEHIrQSPFLVTLHYAFQTETKL 127
Cdd:cd05607   4 FYEFRVLGKGGFGEVCAVQV---KNTGQMYACKKLDKKRL--KKKSGEKMALlEKEILEKV-NSPFIVSLAYAFETKTHL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQ-RERFTEHE-VQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd05607  78 CLVMSLMNGGDLKYHIYNvGERGIEMErVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 E--TERAysfcGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYP-QEM 282
Cdd:cd05607 158 KpiTQRA----GTNGYMAPEILK--EESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLEDEVKFEhQNF 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 283 SALAKDLIQRLLMKDPKKRLGCGPRDaDEIKEHLFFQKINWDDLAAKKVPAPFKP 337
Cdd:cd05607 232 TEEAKDICRLFLAKKPENRLGSRTND-DDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
422-548 1.45e-54

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 184.99  E-value: 1.45e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRM-----EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFL 496
Cdd:cd05117   1 KYELG---KVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKlksedEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYL 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 497 VMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05117  77 VMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPE 128
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
47-348 1.71e-54

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 189.45  E-value: 1.71e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEhIRQSPFLVTLHYAFQTETK 126
Cdd:cd05622  73 EDYEVVKVIGRGAFGEVQLVRHKS---TRKVYAMKLLSKFEMIKRSDSA-FFWEERDIMA-FANSPWVVQLFYAFQDDRY 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRErFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd05622 148 LYMVMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEG 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVR--GGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd05622 227 MVRCDTAVGTPDYISPEVLKsqGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISK 306
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 285 LAKDLIQRLLmKDPKKRLgcGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNF 348
Cdd:cd05622 307 EAKNLICAFL-TDREVRL--GRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNF 367
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
46-302 4.36e-54

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 183.62  E-value: 4.36e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIvQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTET 125
Cdd:cd14116   4 LEDFEIGRPLGKGKFGNVYLARE---KQSKFILALKVLFKAQL-EKAGVEHQLRREVEIQSHLRH-PNILRLYGYFHDAT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSkefVAD 205
Cdd:cd14116  79 RVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS---VHA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSAL 285
Cdd:cd14116 156 PSSRRTTLCGTLDYLPPEMIEG--RMHDEKVDLWSLGVLCYEFLVGKPPF----EANTYQETYKRISRVEFTFPDFVTEG 229
                       250
                ....*....|....*..
gi 32528297 286 AKDLIQRLLMKDPKKRL 302
Cdd:cd14116 230 ARDLISRLLKHNPSQRP 246
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
47-350 7.84e-53

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 184.05  E-value: 7.84e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISGHdtgKLYAMKVLKKATIVQKAKTTeHTRTERQVLEhIRQSPFLVTLHYAFQTETK 126
Cdd:cd05621  52 EDYDVVKVIGRGAFGEVQLVRHKASQ---KVYAMKLLSKFEMIKRSDSA-FFWEERDIMA-FANSPWVVQLFCAFQDDKY 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRErFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd05621 127 LYMVMEYMPGGDLVNLMSNYD-VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETG 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVR--GGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd05621 206 MVHCDTAVGTPDYISPEVLKsqGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNFPDDVEISK 285
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 285 LAKDLIQRLLMkDPKKRLgcGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAE 350
Cdd:cd05621 286 HAKNLICAFLT-DREVRL--GRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFDD 348
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
49-302 8.30e-53

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 180.29  E-value: 8.30e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKaKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTK---TGESVAIKIIDKEQVARE-GMVEQIKREIAIMKLLRH-PNIVELHEVMATKTKIF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS--KEFVADE 206
Cdd:cd14663  77 FVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TeRAYSFCGTIEYMAPDIVRggDSGHDKA-VDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSAL 285
Cdd:cd14663 157 G-LLHTTCGTPNYVAPEVLA--RRGYDGAkADIWSCGVILFVLLAGYLPF----DDENLMALYRKIMKGEFEYPRWFSPG 229
                       250
                ....*....|....*..
gi 32528297 286 AKDLIQRLLMKDPKKRL 302
Cdd:cd14663 230 AKSLIKRILDPNPSTRI 246
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
49-301 2.69e-52

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 178.74  E-value: 2.69e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIrQSPFLVTLHYAFQTETKLH 128
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIE---RATGREVAIKSIKKDKIEDEQDMV-RIRREIEIMSSL-NHPHIIRIYEVFENKDKIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvaDETE 208
Cdd:cd14073  78 IVMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLY--SKDK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKsEPPYPQEMSAlakd 288
Cdd:cd14073 156 LLQTFCGSPLYASPEIVN-GTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYR-EPTQPSDASG---- 229
                       250
                ....*....|...
gi 32528297 289 LIQRLLMKDPKKR 301
Cdd:cd14073 230 LIRWMLTVNPKRR 242
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
55-302 5.97e-52

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 177.46  E-value: 5.97e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKKativqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd14006   1 LGRGRFGVVKRCIEKA---TGREFAAKFIPK-----RDKKKEAVLREISILNQLQH-PRIIQLHEAYESPTELVLILELC 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG--HVVLTDFGLSKEFvaDETERAYS 212
Cdd:cd14006  72 SGGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARKL--NPGEELKE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd14006 150 IFGTPEFVAPEIVNGEPVS--LATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRK 227
                       250
                ....*....|
gi 32528297 293 LLMKDPKKRL 302
Cdd:cd14006 228 LLVKEPRKRP 237
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
49-315 1.45e-51

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 177.13  E-value: 1.45e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKAtivqKAKTTEH-TRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd14095   2 YDIGRVIGDGNFA---VVKECRDKATDKEYALKIIDKA----KCKGKEHmIENEVAILRRVKH-PNIVQLIEEYDTDTEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL--DSNG--HVVLTDFGLSKEFv 203
Cdd:cd14095  74 YLVMELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveHEDGskSLKLADFGLATEV- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 adeTERAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRILKSE----PPYP 279
Cdd:cd14095 153 ---KEPLFTVCGTPTYVAPEIL--AETGYGLKVDIWAAGVITYILLCGFPPFR--SPDRDQEELFDLILAGEfeflSPYW 225
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32528297 280 QEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14095 226 DNISDSAKDLISRMLVVDPEKRY-----SAGQVLDH 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
47-322 2.06e-51

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 176.63  E-value: 2.06e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVlkkatiVQKAKTTEHTRTERQVLEHIR--QSPFLVTLHYAFQTE 124
Cdd:cd06623   1 SDLERVKVLGQGSSGVVYKVRHK---PTGKIYALKK------IHVDGDEEFRKQLLRELKTLRscESPYVVKCYGAFYKE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLH-KLGIIYRDIKLENILLDSNGHVVLTDFGLSKeFV 203
Cdd:cd06623  72 GEISIVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGISK-VL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTvDGEKNSQAEISRRILKSEPPYPQE-- 281
Cdd:cd06623 151 ENTLDQCNTFVGTVTYMSPERIQGESYSY--AADIWSLGLTLLECALGKFPFL-PPGQPSFFELMQAICDGPPPSLPAee 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 32528297 282 MSALAKDLIQRLLMKDPKKRlgcgpRDADEIKEHLFFQKIN 322
Cdd:cd06623 228 FSPEFRDFISACLQKDPKKR-----PSAAELLQHPFIKKAD 263
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
49-348 7.80e-51

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 179.09  E-value: 7.80e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIrQSPFLVTLHYAFQTETKLH 128
Cdd:cd05625   3 FVKIKTLGIGAFGEVCLARKV---DTKALYATKTLRKKDVLLRNQVA-HVKAERDILAEA-DNEWVVRLYYSFQDKDNLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF------ 202
Cdd:cd05625  78 FVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwthds 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 --------------------------------------VADETER--AYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLG 242
Cdd:cd05625 158 kyyqsgdhlrqdsmdfsnewgdpencrcgdrlkplerrAARQHQRclAHSLVGTPNYIAPEVLL--RTGYTQLCDWWSVG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 243 VLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLmKDPKKRLgcGPRDADEIKEHLFFQKIN 322
Cdd:cd05625 236 VILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRL--GKNGADEIKAHPFFKTID 312
                       330       340
                ....*....|....*....|....*..
gi 32528297 323 W-DDLaaKKVPAPFKPVIRDELDVSNF 348
Cdd:cd05625 313 FsSDL--RQQSAPYIPKITHPTDTSNF 337
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
47-304 3.65e-50

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 174.03  E-value: 3.65e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTtehtRTERQVLEHIRQSPfLVTLHYAFQTETK 126
Cdd:cd14166   3 ETFIFMEVLGSGAFSEVYLVKQRS---TGKLYALKCIKKSPLSRDSSL----ENEIAVLKRIKHEN-IVTLEDIYESTTH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL---DSNGHVVLTDFGLSKefv 203
Cdd:cd14166  75 YYLVMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMS 283
Cdd:cd14166 152 MEQNGIMSTACGTPGYVAPEVL--AQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDIS 229
                       250       260
                ....*....|....*....|.
gi 32528297 284 ALAKDLIQRLLMKDPKKRLGC 304
Cdd:cd14166 230 ESAKDFIRHLLEKNPSKRYTC 250
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
53-315 1.16e-49

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 172.58  E-value: 1.16e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLKK-----ATIVQKAKTTEhTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd14084  12 RTLGSGACGEVKLAYDKS---TCKKVAIKIINKrkftiGSRREINKPRN-IETEIEILKKLSH-PCIIKIEDFFDAEDDY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH---VVLTDFGLSKefVA 204
Cdd:cd14084  87 YIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSK--IL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVR-GGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISRRILKSE----PPYP 279
Cdd:cd14084 165 GETSLMKTLCGTPTYLAPEVLRsFGTEGYTRAVDCWSLGVILFICLSGYPPFS---EEYTQMSLKEQILSGKytfiPKAW 241
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32528297 280 QEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14084 242 KNVSEEAKDLVKKMLVVDPSRRP-----SIEEALEH 272
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-304 1.47e-49

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 171.79  E-value: 1.47e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTEHtrtERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd14083   5 YEFKEVLGTGAFSEVVLAED---KATGKLVAIKCIDKKALKGKEDSLEN---EIAVLRKIKH-PNIVQLLDIYESKSHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL---LDSNGHVVLTDFGLSKefvAD 205
Cdd:cd14083  78 LVMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK---ME 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSAL 285
Cdd:cd14083 155 DSGVMSTACGTPGYVAPEVLA--QKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISDS 232
                       250
                ....*....|....*....
gi 32528297 286 AKDLIQRLLMKDPKKRLGC 304
Cdd:cd14083 233 AKDFIRHLMEKDPNKRYTC 251
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
46-318 2.35e-48

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 168.69  E-value: 2.35e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVL----KKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAF 121
Cdd:cd14093   2 YAKYEPKEILGRGVSS---TVRRCIEKETGQEFAVKIIditgEKSSENEAEELREATRREIEILRQVSGHPNIIELHDVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd14093  79 ESPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FvaDETERAYSFCGTIEYMAPDIVR----GGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRIL--KSE 275
Cdd:cd14093 159 L--DEGEKLRELCGTPGYLAPEVLKcsmyDNAPGYGKEVDMWACGVIMYTLLAGCPPFW----HRKQMVMLRNIMegKYE 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 32528297 276 PPYPQ--EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14093 233 FGSPEwdDISDTAKDLISKLLVVDPKKRL-----TAEEALEHPFF 272
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
49-318 8.96e-48

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 166.61  E-value: 8.96e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLH 128
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKK---TGQIVAIKKIN----LESKEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDELW 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGG---ELFTHLSQRerFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvAD 205
Cdd:cd05122  74 IVMEFCSGGslkDLLKNTNKT--LTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQL-SD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERaYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFtvdgeknSQAEISR---RILKSEPP---YP 279
Cdd:cd05122 151 GKTR-NTFVGTPYWMAPEVIQGKP--YGFKADIWSLGITAIEMAEGKPPY-------SELPPMKalfLIATNGPPglrNP 220
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 32528297 280 QEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd05122 221 KKWSKEFKDFLKKCLQKDPEKRP-----TAEQLLKHPFI 254
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
48-318 2.67e-47

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 165.50  E-value: 2.67e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVflvrKISGH-DTGKLYAMKVLKKATIvqkAKTTEHTRTERQV-----LEHirqsPFLVTLHYAF 121
Cdd:cd14081   2 PYRLGKTLGKGQTGLV----KLAKHcVTGQKVAIKIVNKEKL---SKESVLMKVEREIaimklIEH----PNVLKLYDVY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKe 201
Cdd:cd14081  71 ENKKYLYLVLEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAvDWWSLGVLMYELLTGASPFtvDGEknSQAEISRRILKSEPPYPQE 281
Cdd:cd14081 150 -LQPEGSLLETSCGSPHYACPEVIKGEKYDGRKA-DIWSCGVILYALLVGALPF--DDD--NLRQLLEKVKRGVFHIPHF 223
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 282 MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14081 224 ISPDAQDLLRRMLEVNPEKRI-----TIEEIKKHPWF 255
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
47-304 3.01e-47

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 165.59  E-value: 3.01e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHtrtERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd14167   3 DIYDFREVLGTGAFSEVVLAEEKR---TQKLVAIKCIAKKALEGKETSIEN---EIAVLHKIKH-PNIVALDDIYESGGH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL---LDSNGHVVLTDFGLSKefV 203
Cdd:cd14167  76 LYLIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK--I 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEknsqAEISRRILKSE----PPYP 279
Cdd:cd14167 154 EGSGSVMSTACGTPGYVAPEVL--AQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND----AKLFEQILKAEyefdSPYW 227
                       250       260
                ....*....|....*....|....*
gi 32528297 280 QEMSALAKDLIQRLLMKDPKKRLGC 304
Cdd:cd14167 228 DDISDSAKDFIQHLMEKDPEKRFTC 252
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
47-304 3.04e-47

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 165.12  E-value: 3.04e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVlkkatIVQKAKTTEHTRTERQVLEHIRQ--SPFLVTLHYAFQTE 124
Cdd:cd14002   1 ENYHVLELIGEGSFGKVYKGRR---KYTGQVVALKF-----IPKRGKSEKELRNLRQEIEILRKlnHPNIIEMLDSFETK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGgELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVA 204
Cdd:cd14002  73 KEFVVVTEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARA-MS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVdgekNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd14002 151 CNTLVLTSIKGTPLYMAPELVQ--EQPYDHTADLWSLGCILYELFVGQPPFYT----NSIYQLVQMIVKDPVKWPSNMSP 224
                       250       260
                ....*....|....*....|
gi 32528297 285 LAKDLIQRLLMKDPKKRLGC 304
Cdd:cd14002 225 EFKSFLQGLLNKDPSKRLSW 244
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
48-317 1.14e-46

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 164.39  E-value: 1.14e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKAtivQKAKTTEHTRTERQvLEHirqsPFLVTLHYAFQTETKL 127
Cdd:cd14010   1 NYVLYDEIGRGKHSVVYKGRR---KGTIEFVAIKCVDKS---KRPEVLNEVRLTHE-LKH----PNVLKFYEWYETSNHL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd14010  70 WLVVEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEILK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFC---------------GTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRIL 272
Cdd:cd14010 150 ELFGQFSdegnvnkvskkqakrGTPYYMAPELFQGGV--HSFASDLWALGCVLYEMFTGKPPFVAE----SFTELVEKIL 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 273 KSEPPYPQ-----EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLF 317
Cdd:cd14010 224 NEDPPPPPpkvssKPSPDFKSLLKGLLEKDPAKRL-----SWDELVKHPF 268
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
424-548 1.77e-45

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 161.65  E-value: 1.77e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKDKpLGEGSFSICRKCVHKKSNQAFAVKIISKRmEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14091   1 EYEIKEE-IGKGSYSVCKRCIHKATGKEYAVKIIDKS-KRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRG 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14091  79 GELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPS 123
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
55-317 2.08e-45

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 160.58  E-value: 2.08e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVflvrKISGHD-TGKLYAMKVLKKATIVQKAK---TTEHTRTERqvLEHirqsPFLVTLHYAFQTETKLHLI 130
Cdd:cd14075  10 LGSGNFSQV----KLGIHQlTKEKVAIKILDKTKLDQKTQrllSREISSMEK--LHH----PNIIRLYEVVETLSKLHLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERA 210
Cdd:cd14075  80 MEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFST--HAKRGETL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 YSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPF---TVDGEKnsqaeisRRILKSEPPYPQEMSALAK 287
Cdd:cd14075 158 NTFCGSPPYAAPELFK-DEHYIGIYVDIWALGVLLYFMVTGVMPFraeTVAKLK-------KCILEGTYTIPSYVSEPCQ 229
                       250       260       270
                ....*....|....*....|....*....|
gi 32528297 288 DLIQRLLMKDPKKRLgcgprDADEIKEHLF 317
Cdd:cd14075 230 ELIRGILQPVPSDRY-----SIDEIKNSEW 254
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
49-301 3.80e-45

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 159.73  E-value: 3.80e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGhdtgKLYAMKVLKKATIVQKAKTTeHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd14161   5 YEFLETLGKGTYGRVKKARDSSG----RLVAIKSIRKDRIKDEQDLL-HIRREIEIMSSLNH-PHIISVYEVFENSSKIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETE 208
Cdd:cd14161  79 IVMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYsfCGTIEYMAPDIVrGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKsEPPYPQEmsalAKD 288
Cdd:cd14161 159 QTY--CGSPLYASPEIV-NGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYR-EPTKPSD----ACG 230
                       250
                ....*....|...
gi 32528297 289 LIQRLLMKDPKKR 301
Cdd:cd14161 231 LIRWLLMVNPERR 243
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
43-302 6.92e-45

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 159.64  E-value: 6.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  43 KVGIENFELLKVLGTGAYGKVFLVRKISGHdtgKLYAMKVLKKATIVQKAktTEHT-RTERQVLEHIRQsPFLVTLHYAF 121
Cdd:cd14117   2 KFTIDDFDIGRPLGKGKFGNVYLAREKQSK---FIVALKVLFKSQIEKEG--VEHQlRREIEIQSHLRH-PNILRLYNYF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSke 201
Cdd:cd14117  76 HDRKRIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fVADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQE 281
Cdd:cd14117 154 -VHAPSLRRRTMCGTLDYLPPEMIEG--RTHDEKVDLWCIGVLCYELLVGMPPF----ESASHTETYRRIVKVDLKFPPF 226
                       250       260
                ....*....|....*....|.
gi 32528297 282 MSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14117 227 LSDGSRDLISKLLRYHPSERL 247
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
51-315 1.04e-44

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 159.19  E-value: 1.04e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFL--VRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRtERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd14076   5 LGRTLGEGEFGKVKLgwPLPKANHRSGVQVAIKLIRRDTQQENCQTSKIMR-EINILKGLTH-PNIVRLLDVLKTKKYIG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETE 208
Cdd:cd14076  83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNGD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEK---NSQAEISRRILKSEPPYPQEMSAL 285
Cdd:cd14076 163 LMSTSCGSPCYAAPELVVSDSMYAGRKADIWSCGVILYAMLAGYLPFDDDPHNpngDNVPRLYRYICNTPLIFPEYVTPK 242
                       250       260       270
                ....*....|....*....|....*....|
gi 32528297 286 AKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14076 243 ARDLLRRILVPNPRKRI-----RLSAIMRH 267
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
49-315 2.46e-44

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 157.73  E-value: 2.46e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGHDTGKLyAMKVLKKAtivqKAKTTEHTR---TERQVLEHIRQsPFLVTLHYAFQTET 125
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTKSGLKEKV-ACKIIDKK----KAPKDFLEKflpRELEILRKLRH-PNIIQVYSIFERGS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd14080  76 KVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYS-FCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRRILKSE--PPYPQEM 282
Cdd:cd14080 156 DGDVLSKtFCGSAAYAAPEILQ-GIPYDPKKYDIWSLGVILYIMLCGSMPF---DDSNIKKMLKDQQNRKVrfPSSVKKL 231
                       250       260       270
                ....*....|....*....|....*....|...
gi 32528297 283 SALAKDLIQRLLMKDPKKRLGcgprdADEIKEH 315
Cdd:cd14080 232 SPECKDLIDQLLEPDPTKRAT-----IEEILNH 259
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
48-304 2.50e-44

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 157.55  E-value: 2.50e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKttEHTRTERQVLEHIrQSPFLVTLHYAFQTETKL 127
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLS---DNQVYALKEVNLGSLSQKER--EDSVNEIRLLASV-NHPNIIRYKEAFLDGNRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRER----FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefv 203
Cdd:cd08530  75 CIVMEYAPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSE-PPYPQEM 282
Cdd:cd08530 152 VLKKNLAKTQIGTPLYAAPEVWK--GRPYDYKSDIWSLGCLLYEMATFRPPFEAR----TMQELRYKVCRGKfPPIPPVY 225
                       250       260
                ....*....|....*....|..
gi 32528297 283 SALAKDLIQRLLMKDPKKRLGC 304
Cdd:cd08530 226 SQDLQQIIRSLLQVNPKKRPSC 247
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
53-320 2.53e-44

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 159.39  E-value: 2.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGkvfLVRKISGHDTGKLYAMKvlkkatIVQKAKttEHTRtERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd14092  12 EALGDGSFS---VCRKCVHKKTGQEFAVK------IVSRRL--DTSR-EVQLLRLCQGHPNIVKLHEVFQDELHTYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL---DSNGHVVLTDFGLSKefVADETER 209
Cdd:cd14092  80 LLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFAR--LKPENQP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 AYSFCGTIEYMAPDIVRGGDS--GHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSE----PPYPQEMS 283
Cdd:cd14092 158 LKTPCFTLPYAAPEVLKQALStqGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRIKSGDfsfdGEEWKNVS 237
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 284 ALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQK 320
Cdd:cd14092 238 SEAKSLIQGLLTVDPSKRL-----TMSELRNHPWLQG 269
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
59-315 1.57e-43

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 155.97  E-value: 1.57e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  59 AYGKVFLVRKISGHDTGKLYAMKVLKKAtivQKAKTTEH-TRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYINGG 137
Cdd:cd14106  17 GRGKFAVVRKCIHKETGKEYAAKFLRKR---RRGQDCRNeILHEIAVLELCKDCPRVVNLHEVYETRSELILILELAAGG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 138 ELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS---NGHVVLTDFGLSKefVADETERAYSFC 214
Cdd:cd14106  94 ELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSefpLGDIKLCDFGISR--VIGEGEEIREIL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 215 GTIEYMAPDIVRggdsgHDK---AVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQ 291
Cdd:cd14106 172 GTPDYVAPEILS-----YEPislATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSPLAIDFIK 246
                       250       260
                ....*....|....*....|....
gi 32528297 292 RLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14106 247 RLLVKDPEKRL-----TAKECLEH 265
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
49-301 1.65e-43

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 155.71  E-value: 1.65e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVflvRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd14098   2 YQIIDRLGSGTFAEV---KKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQREINILKSLEH-PGIVRLIDWYEDDQHIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG--HVVLTDFGLSKefVADE 206
Cdd:cd14098  78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAK--VIHT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVRG----GDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKS----EPPY 278
Cdd:cd14098 156 GTFLVTFCGTMAYLAPEILMSkeqnLQGGYSNLVDMWSVGCLVYVMLTGALPFDGS----SQLPVEKRIRKGrytqPPLV 231
                       250       260
                ....*....|....*....|...
gi 32528297 279 PQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14098 232 DFNISEEAIDFILRLLDVDPEKR 254
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
47-302 1.94e-43

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 155.56  E-value: 1.94e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQV--LEHIRQsPFLVTLHYAFQTE 124
Cdd:cd14194   5 DYYDTGEELGSGQFA---VVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVsiLKEIQH-PNVITLHEVYENK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENI-LLDSNG---HVVLTDFGLSK 200
Cdd:cd14194  81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVpkpRIKIIDFGLAH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFvaDETERAYSFCGTIEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQ 280
Cdd:cd14194 161 KI--DFGNEFKNIFGTPEFVAPEIVNYEPLGLEA--DMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFS 236
                       250       260
                ....*....|....*....|..
gi 32528297 281 EMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14194 237 NTSALAKDFIRRLLVKDPKKRM 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
430-548 4.25e-43

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 154.22  E-value: 4.25e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR----MEANTQKEITALKLCeGHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIKKKkikkDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYCEGGD 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 32528297    506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:smart00220  84 LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPE 126
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
54-315 6.08e-43

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 154.88  E-value: 6.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEhtrtERQVLEHIRQSPFLVTLHYAFQTETKLHLILDY 133
Cdd:cd14090   9 LLGEGAYASVQTCINLY---TGKEYAVKIIEKHPGHSRSRVFR----EVETLHQCQGHPNILQLIEYFEDDERFYLVFEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV---LTDFGL-------SKEFV 203
Cdd:cd14090  82 MRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSpvkICDFDLgsgiklsSTSMT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCGTIEYMAPDIVR---GGDSGHDKAVDWWSLGVLMYELLTGASPFTVD---------GE--KNSQAEISR 269
Cdd:cd14090 162 PVTTPELLTPVGSAEYMAPEVVDafvGEALSYDKRCDLWSLGVILYIMLCGYPPFYGRcgedcgwdrGEacQDCQELLFH 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 270 RILKSEPPYPQE----MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14090 242 SIQEGEYEFPEKewshISAEAKDLISHLLVRDASQRY-----TAEQVLQH 286
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
49-301 6.62e-43

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 153.95  E-value: 6.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAygkvFLVRKISGH-DTGKLYAMKVLKKATIVQKAKTTEhtrTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd14185   2 YEIGRTIGDGN----FAVVKECRHwNENQEYAMKIIDKSKLKGKEDMIE---SEILIIKSLSH-PNIVKLFEVYETEKEI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL----DSNGHVVLTDFGLSKEFv 203
Cdd:cd14185  74 YLILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYV- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 adeTERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRILKSE----PPYP 279
Cdd:cd14185 153 ---TGPIFTVCGTPTYVAPEILSE--KGYGLEVDMWAAGVILYILLCGFPPFR--SPERDQEELFQIIQLGHyeflPPYW 225
                       250       260
                ....*....|....*....|..
gi 32528297 280 QEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14185 226 DNISEAAKDLISRLLVVDPEKR 247
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
49-302 1.49e-42

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 153.03  E-value: 1.49e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQV--LEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd14105   7 YDIGEELGSGQFA---VVKKCREKSTGLEYAAKFIKKRRSKASRRGVSREDIEREVsiLRQVLH-PNIITLHDVFENKTD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENI-LLDSN---GHVVLTDFGLSKEF 202
Cdd:cd14105  83 VVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENImLLDKNvpiPRIKLIDFGLAHKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETERaySFCGTIEYMAPDIVRGGDSGHDkaVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEM 282
Cdd:cd14105 163 EDGNEFK--NIFGTPEFVAPEIVNYEPLGLE--ADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNT 238
                       250       260
                ....*....|....*....|
gi 32528297 283 SALAKDLIQRLLMKDPKKRL 302
Cdd:cd14105 239 SELAKDFIRQLLVKDPRKRM 258
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
54-318 2.49e-42

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 152.82  E-value: 2.49e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGkvfLVRKISGHDTGKLYAMKVLK----KATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHL 129
Cdd:cd14181  17 VIGRGVSS---VVRRCVHRHTGQEFAVKIIEvtaeRLSPEQLEEVRSSTLKEIHILRQVSGHPSIITLIDSYESSTFIFL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETER 209
Cdd:cd14181  94 VFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLR 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 aySFCGTIEYMAPDIVRGG----DSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSE----PPYPQE 281
Cdd:cd14181 174 --ELCGTPGYLAPEILKCSmdetHPGYGKEVDLWACGVILFTLLAGSPPFW----HRRQMLMLRMIMEGRyqfsSPEWDD 247
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 282 MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14181 248 RSSTVKDLISRLLVVDPEIRL-----TAEQALQHPFF 279
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
48-301 4.39e-42

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 151.22  E-value: 4.39e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTehTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNL---NTGEFVAIKQISLEKIPKSDLKS--VMGEIDLLKKLNH-PNIVKYIGSVKTKDSL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVADET 207
Cdd:cd06627  75 YIILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATK-LNEVE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd06627 154 KDENSVVGTPYWMAPEVIEM--SGVTTASDIWSVGCTVIELLTGNPPY---YDLQPMAALFRIVQDDHPPLPENISPELR 228
                       250
                ....*....|....
gi 32528297 288 DLIQRLLMKDPKKR 301
Cdd:cd06627 229 DFLLQCFQKDPTLR 242
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
430-548 5.02e-42

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 151.13  E-value: 5.02e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd14003   6 KTLGEGSFGKVKLARHKLTGEKVAIKIIDKsklkeEIEEKIKREIEIMKLLN-HPNIIKLYEVIETENKIYLVMEYASGG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14003  85 ELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLE 128
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
48-301 1.01e-41

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 150.36  E-value: 1.01e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKaTIVQKAKTTEHTRTER--QVLEHirqsPFLVTLHYAFQTET 125
Cdd:cd14072   1 NYRLLKTIGKGNFAKVKLARHVL---TGREVAIKIIDK-TQLNPSSLQKLFREVRimKILNH----PNIVKLFEVIETEK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd14072  73 TLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 etERAYSFCGTIEYMAPDIVRGgdSGHD-KAVDWWSLGVLMYELLTGASPFtvDGekNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd14072 153 --NKLDTFCGSPPYAAPELFQG--KKYDgPEVDVWSLGVILYTLVSGSLPF--DG--QNLKELRERVLRGKYRIPFYMST 224
                       250
                ....*....|....*..
gi 32528297 285 LAKDLIQRLLMKDPKKR 301
Cdd:cd14072 225 DCENLLKKFLVLNPSKR 241
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-304 1.13e-41

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 151.20  E-value: 1.13e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTEHtrtERQVLEHIrQSPFLVTLHYAFQTETKLH 128
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQE---RGSQRLVALKCIPKKALRGKEAMVEN---EIAVLRRI-NHENIVSLEDIYESPTHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS---NGHVVLTDFGLSKefvAD 205
Cdd:cd14169  78 LAMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSK---IE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSE----PPYPQE 281
Cdd:cd14169 155 AQGMLSTACGTPGYVAPELLEQKPYG--KAVDVWAIGVISYILLCGYPPFYDE----NDSELFNQILKAEyefdSPYWDD 228
                       250       260
                ....*....|....*....|...
gi 32528297 282 MSALAKDLIQRLLMKDPKKRLGC 304
Cdd:cd14169 229 ISESAKDFIRHLLERDPEKRFTC 251
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
53-317 1.43e-41

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 150.25  E-value: 1.43e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLvrKISGhDTGKLYAMKVLKKATIVQKAK-TTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLIL 131
Cdd:cd06632   6 QLLGSGSFGSVYE--GFNG-DTGDFFAVKEVSLVDDDKKSReSVKQLEQEIALLSKLRH-PNIVQYYGTEREEDNLYIFL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETerAY 211
Cdd:cd06632  82 EYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSF--AK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSE--PPYPQEMSALAKDL 289
Cdd:cd06632 160 SFKGSPYWMAPEVIMQKNSGYGLAVDIWSLGCTVLEMATGKPPWS----QYEGVAAIFKIGNSGelPPIPDHLSPDAKDF 235
                       250       260
                ....*....|....*....|....*...
gi 32528297 290 IQRLLMKDPKKRlgcgPRdADEIKEHLF 317
Cdd:cd06632 236 IRLCLQRDPEDR----PT-ASQLLEHPF 258
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
46-318 1.78e-41

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 149.73  E-value: 1.78e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVflvrKISGHD-TGKLYAMKVLKKATIvQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTE 124
Cdd:cd14079   1 IGNYILGKTLGVGSFGKV----KLAEHElTGHKVAVKILNRQKI-KSLDMEEKIRREIQILKLFRH-PHIIRLYEVIETP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK---- 200
Cdd:cd14079  75 TDIFMVMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNimrd 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 -EFVadETEraysfCGTIEYMAPDIVrggdSGHDKA---VDWWSLGVLMYELLTGASPFtvDGEknSQAEISRRILKSEP 276
Cdd:cd14079 155 gEFL--KTS-----CGSPNYAAPEVI----SGKLYAgpeVDVWSCGVILYALLCGSLPF--DDE--HIPNLFKKIKSGIY 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 32528297 277 PYPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14079 220 TIPSHLSPGARDLIKRMLVVDPLKRI-----TIPEIRQHPWF 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
47-302 1.21e-40

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 147.53  E-value: 1.21e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIvqkAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd14078   3 KYYELHETIGSGGFAKVKLATHIL---TGEKVAIKIMDKKAL---GDDLPRVKTEIEALKNLSH-QHICRLYHVIETDNK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd14078  76 IFMVLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGM 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVRGGDSGHDKAvDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALA 286
Cdd:cd14078 156 DHHLETCCGSPAYAAPELIQGKPYIGSEA-DVWSMGVLLYALLCGFLPF----DDDNVMALYRKIQSGKYEEPEWLSPSS 230
                       250
                ....*....|....*.
gi 32528297 287 KDLIQRLLMKDPKKRL 302
Cdd:cd14078 231 KLLLDQMLQVDPKKRI 246
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
47-302 3.54e-40

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 147.57  E-value: 3.54e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKkatiVQKAKTTEHTRTERQV-----LEHirqsPFLVTLHYAF 121
Cdd:cd14086   1 DEYDLKEELGKGAFS---VVRRCVQKSTGQEFAAKIIN----TKKLSARDHQKLEREAricrlLKH----PNIVRLHDSI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS---NGHVVLTDFGL 198
Cdd:cd14086  70 SEEGFHYLVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASkskGAAVKLADFGL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKEfVADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPY 278
Cdd:cd14086 150 AIE-VQGDQQAWFGFAGTPGYLSPEVLR--KDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPE 226
                       250       260
                ....*....|....*....|....
gi 32528297 279 PQEMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14086 227 WDTVTPEAKDLINQMLTVNPAKRI 250
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
47-320 3.75e-40

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 146.54  E-value: 3.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   47 ENFELLKVLGT--GAYGKVFLVRKisgHDTGKLYAMKVLKkativqkakttEHTRTERQVLEHI--RQSPFLVTLHYAFQ 122
Cdd:PHA03390  14 KNCEIVKKLKLidGKFGKVSVLKH---KPTQKLFVQKIIK-----------AKNFNAIEPMVHQlmKDNPNFIKLYYSVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  123 TETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD-SNGHVVLTDFGLSK- 200
Cdd:PHA03390  80 TLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCKi 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  201 ---EFVADeteraysfcGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPP 277
Cdd:PHA03390 160 igtPSCYD---------GTLDYFSPEKIKGHN--YDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQQKKLP 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 32528297  278 YPQEMSALAKDLIQRLLMKDPKKRLgcgpRDADEIKEHLFFQK 320
Cdd:PHA03390 229 FIKNVSKNANDFVQSMLKYNINYRL----TNYNEIIKHPFLKI 267
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
47-315 4.14e-40

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 147.20  E-value: 4.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvRKISGHDTGKLYAMKVLKKATIVQKA-KTTEHTRTERQVLEHIRQS-PFLVTLHYAFQTE 124
Cdd:cd14096   1 ENYRLINKIGEGAFSNVY--KAVPLRNTGKPVAIKVVRKADLSSDNlKGSSRANILKEVQIMKRLShPNIVKLLDFQESD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSN---------------- 188
Cdd:cd14096  79 EYYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPIpfipsivklrkaddde 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 189 -----------------GHVVLTDFGLSKEFVADETERAysfCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14096 159 tkvdegefipgvggggiGIVKLADFGLSKQVWDSNTKTP---CGTVGYTAPEVVK--DERYSKKVDMWALGCVLYTLLCG 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 252 ASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14096 234 FPPFYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRY-----DIDEFLAH 292
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
49-302 4.89e-40

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 146.30  E-value: 4.89e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQV--LEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd14195   7 YEMGEELGSGQFA---IVRKCREKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVniLREIQH-PNIITLHDIFENKTD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENI-LLDSNG---HVVLTDFGLSKEF 202
Cdd:cd14195  83 VVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImLLDKNVpnpRIKLIDFGIAHKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETERaySFCGTIEYMAPDIVRGGDSGHDkaVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEM 282
Cdd:cd14195 163 EAGNEFK--NIFGTPEFVAPEIVNYEPLGLE--ADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNT 238
                       250       260
                ....*....|....*....|
gi 32528297 283 SALAKDLIQRLLMKDPKKRL 302
Cdd:cd14195 239 SELAKDFIRRLLVKDPKKRM 258
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
48-315 7.46e-40

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 145.76  E-value: 7.46e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKttEHTRTERQVLEHIRQsPFLVTLHYAF--QTET 125
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKS---DGKILVWKEIDYGKMSEKEK--QQLVSEVNILRELKH-PNIVRYYDRIvdRANT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFT----HLSQRERFTEHEVQIYVGEIVLALEHLHKLG-----IIYRDIKLENILLDSNGHVVLTDF 196
Cdd:cd08217  75 TLYIVMEYCEGGDLAQlikkCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 197 GLSKEfVADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSE- 275
Cdd:cd08217 155 GLARV-LSHDSSFAKTYVGTPYYMSPELLN--EQSYDEKSDIWSLGCLIYELCALHPPF----QAANQLELAKKIKEGKf 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 32528297 276 PPYPQEMSALAKDLIQRLLMKDPKKRlgcgPrDADEIKEH 315
Cdd:cd08217 228 PRIPSRYSSELNEVIKSMLNVDPDKR----P-SVEELLQL 262
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
48-301 2.41e-39

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 144.19  E-value: 2.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVflvRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd14070   3 SYLIGRKLGEGSFAKV---REGLHAVTGEKVAIKVIDKKKAKKDSYVTKNLRREGRIQQMIRH-PNITQLLDILETENSY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF-VADE 206
Cdd:cd14070  79 YLVMELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAgILGY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVrggdsGHDK---AVDWWSLGVLMYELLTGASPFTVDgEKNSQAEISRRILKSEPPYPQEMS 283
Cdd:cd14070 159 SDPFSTQCGSPAYAAPELL-----ARKKygpKVDVWSIGVNMYAMLTGTLPFTVE-PFSLRALHQKMVDKEMNPLPTDLS 232
                       250
                ....*....|....*...
gi 32528297 284 ALAKDLIQRLLMKDPKKR 301
Cdd:cd14070 233 PGAISFLRSLLEPDPLKR 250
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
49-302 2.71e-39

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 144.33  E-value: 2.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQV--LEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd14196   7 YDIGEELGSGQFA---IVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVsiLRQV-LHPNIITLHDVYENRTD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENI-LLDSNG---HVVLTDFGLSKEf 202
Cdd:cd14196  83 VVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHE- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETERAYSFcGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEM 282
Cdd:cd14196 162 IEDGVEFKNIF-GTPEFVAPEIVNYEPLG--LEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHT 238
                       250       260
                ....*....|....*....|
gi 32528297 283 SALAKDLIQRLLMKDPKKRL 302
Cdd:cd14196 239 SELAKDFIRKLLVKETRKRL 258
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
49-302 2.71e-39

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 144.97  E-value: 2.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKaTIVQKAkttehTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd14085   5 FEIESELGRGATSVVYRCRQ---KGTQKPYAVKKLKK-TVDKKI-----VRTEIGVLLRLSH-PNIIKLKEIFETPTEIS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH---VVLTDFGLSKefVAD 205
Cdd:cd14085  75 LVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSK--IVD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNsqaEISRRILKSE----PPYPQE 281
Cdd:cd14085 153 QQVTMKTVCGTPGYCAPEILRG--CAYGPEVDMWSVGVITYILLCGFEPFYDERGDQ---YMFKRILNCDydfvSPWWDD 227
                       250       260
                ....*....|....*....|.
gi 32528297 282 MSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14085 228 VSLNAKDLVKKLIVLDPKKRL 248
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
47-320 3.01e-39

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 144.29  E-value: 3.01e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLK-----KATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAF 121
Cdd:cd14182   3 EKYEPKEILGRGVSS---VVRRCIHKPTRQEYAVKIIDitgggSFSPEEVQELREATLKEIDILRKVSGHPNIIQLKDTY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd14182  80 ETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FvaDETERAYSFCGTIEYMAPDIVRGG----DSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSE-- 275
Cdd:cd14182 160 L--DPGEKLREVCGTPGYLAPEIIECSmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFW----HRKQMLMLRMIMSGNyq 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 276 --PPYPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQK 320
Cdd:cd14182 234 fgSPEWDDRSDTVKDLISRFLVVQPQKRY-----TAEEALAHPFFQQ 275
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
55-304 4.22e-39

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 143.14  E-value: 4.22e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd14103   1 LGRGKFGTVYRCVEKA---TGKELAAKFIK----CRKAKDREDVRNEIEIMNQLRH-PRLLQLYDAFETPREMVLVMEYV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFthlsqrER-------FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL-LDSNGHVV-LTDFGLSKEFvaD 205
Cdd:cd14103  73 AGGELF------ERvvdddfeLTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNQIkIIDFGLARKY--D 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSAL 285
Cdd:cd14103 145 PDKKLKVLFGTPEFVAPEVVNYEPISY--ATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDE 222
                       250
                ....*....|....*....
gi 32528297 286 AKDLIQRLLMKDPKKRLGC 304
Cdd:cd14103 223 AKDFISKLLVKDPRKRMSA 241
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
48-303 4.35e-39

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 143.74  E-value: 4.35e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKAT------IVQKAKTTEHTRTERQVLEHIRQS----PFLVTL 117
Cdd:cd14077   2 NWEFVKTIGAGSMGKVKLAKHIR---TGEKCAIKIIPRASnaglkkEREKRLEKEISRDIRTIREAALSSllnhPHICRL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 118 HYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd14077  79 RDFLRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEFvaDETERAYSFCGTIEYMAPDIVRGGD-SGHDkaVDWWSLGVLMYELLTGASPFTvdgEKNSQAeISRRILKSEP 276
Cdd:cd14077 159 LSNLY--DPRRLLRTFCGSLYFAAPELLQAQPyTGPE--VDVWSFGVVLYVLVCGKVPFD---DENMPA-LHAKIKKGKV 230
                       250       260
                ....*....|....*....|....*..
gi 32528297 277 PYPQEMSALAKDLIQRLLMKDPKKRLG 303
Cdd:cd14077 231 EYPSYLSSECKSLISRMLVVDPKKRAT 257
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
47-320 4.52e-39

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 143.64  E-value: 4.52e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRkisgH-DTGKLYAMKVLKKAtiVQKAKTTEHTRtERQVLeHIRQSPFLVTLHYAFQTET 125
Cdd:cd06605   1 DDLEYLGELGEGNGGVVSKVR----HrPSGQIMAVKVIRLE--IDEALQKQILR-ELDVL-HKCNSPYIVGFYGAFYSEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEV-QIYVGeIVLALEHLH-KLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV 203
Cdd:cd06605  73 DISICMEYMDGGSLDKILKEVGRIPERILgKIAVA-VVKGLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADeteRAYSFCGTIEYMAPDIVRGGdsGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQA--EISRRILKSEPP-YPQ 280
Cdd:cd06605 152 DS---LAKTFVGTRSYMAPERISGG--KYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMifELLSYIVDEPPPlLPS 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 32528297 281 EM-SALAKDLIQRLLMKDPKKRlgcgpRDADEIKEHLFFQK 320
Cdd:cd06605 227 GKfSPDFQDFVSQCLQKDPTER-----PSYKELMEHPFIKR 262
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
55-303 7.69e-39

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 142.36  E-value: 7.69e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVqkAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd14009   1 IGRGSFATVWKGRHK---QTGEVVAIKEISRKKLN--KKLQENLESEIAILKSIKH-PNIVRLYDVQKTEDFIYLVLEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH---VVLTDFGLSKeFVADETErAY 211
Cdd:cd14009  75 AGGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFAR-SLQPASM-AE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTVdgekNSQAEISRRILKSE----PPYPQEMSALAK 287
Cdd:cd14009 153 TLCGSPLYMAPEILQFQK--YDAKADLWSVGAILFEMLVGKPPFRG----SNHVQLLRNIERSDavipFPIAAQLSPDCK 226
                       250
                ....*....|....*.
gi 32528297 288 DLIQRLLMKDPKKRLG 303
Cdd:cd14009 227 DLLRRLLRRDPAERIS 242
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
49-301 1.17e-38

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 142.17  E-value: 1.17e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATI--VQKAKTTEHTRTERQVlehirQSPFLVTLHYAFQTETK 126
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVF---TGEKVAVKVIDKTKLddVSKAHLFQEVRCMKLV-----QHPNVVRLYEVIDTQTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL-DSNGHVVLTDFGLSKEFVA 204
Cdd:cd14074  77 LYLILELGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DEteRAYSFCGTIEYMAPDIVRGgDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSA 284
Cdd:cd14074 157 GE--KLETSCGSLAYSAPEILLG-DEYDAPAVDIWSLGVILYMLVCGQPPF----QEANDSETLTMIMDCKYTVPAHVSP 229
                       250
                ....*....|....*..
gi 32528297 285 LAKDLIQRLLMKDPKKR 301
Cdd:cd14074 230 ECKDLIRRMLIRDPKKR 246
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
47-304 2.26e-38

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 142.88  E-value: 2.26e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHtrtERQVLEHIRQSPfLVTLHYAFQTETK 126
Cdd:cd14168  10 KIFEFKEVLGTGAFSEVVLAEERA---TGKLFAVKCIPKKALKGKESSIEN---EIAVLRKIKHEN-IVALEDIYESPNH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL---DSNGHVVLTDFGLSK-EF 202
Cdd:cd14168  83 LYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKmEG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETERAysfCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEM 282
Cdd:cd14168 163 KGDVMSTA---CGTPGYVAPEVL--AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDI 237
                       250       260
                ....*....|....*....|..
gi 32528297 283 SALAKDLIQRLLMKDPKKRLGC 304
Cdd:cd14168 238 SDSAKDFIRNLMEKDPNKRYTC 259
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
53-302 2.59e-38

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 141.27  E-value: 2.59e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVflvRKISGHDTGKLYAMKVLKKatiVQKAkttehtrtERQVLEHIRQS--PFLVTLH--YA--FQTETK 126
Cdd:cd14089   7 QVLGLGINGKV---LECFHKKTGEKFALKVLRD---NPKA--------RREVELHWRASgcPHIVRIIdvYEntYQGRKC 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQR--ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH---VVLTDFGLSKe 201
Cdd:cd14089  73 LLVVMECMEGGELFSRIQERadSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAK- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fvadETERAYSF---CGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEIS----RRIL-- 272
Cdd:cd14089 152 ----ETTTKKSLqtpCYTPYYVAPEVL--GPEKYDKSCDMWSLGVIMYILLCGYPPFY----SNHGLAISpgmkKRIRng 221
                       250       260       270
                ....*....|....*....|....*....|..
gi 32528297 273 KSEPPYPQ--EMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14089 222 QYEFPNPEwsNVSEEAKDLIRGLLKTDPSERL 253
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
49-315 3.34e-38

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 140.99  E-value: 3.34e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAygkvFLVRKISGHDTGKL-YAMKVLKKATIvqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd14071   2 YDIERTIGKGN----FAVVKLARHRITKTeVAIKIIDKSQL--DEENLKKIYREVQIMKMLNH-PHIIKLYQVMETKDML 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd14071  75 YLVTEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGEL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERaySFCGTIEYMAPDIVRGGDSGHDKaVDWWSLGVLMYELLTGASPFtvDGekNSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd14071 155 LK--TWCGSPPYAAPEVFEGKEYEGPQ-LDIWSLGVVLYVLVCGALPF--DG--STLQTLRDRVLSGRFRIPFFMSTDCE 227
                       250       260
                ....*....|....*....|....*...
gi 32528297 288 DLIQRLLMKDPKKRLGcgprdADEIKEH 315
Cdd:cd14071 228 HLIRRMLVLDPSKRLT-----IEQIKKH 250
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
48-301 5.80e-38

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 140.24  E-value: 5.80e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKV--LKKATIVQKAKTTEHTRterqVLEHIRqSPFLVTLHYAFQTET 125
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVR---KVDGRVYALKQidISRMSRKMREEAIDEAR----VLSKLN-SPYVIKYYDSFVDKG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHL-SQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKeFV 203
Cdd:cd08529  73 KLNIVMEYAENGDLHSLIkSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAK-IL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSE-PPYPQEM 282
Cdd:cd08529 152 SDTTNFAQTIVGTPYYLSPELCE--DKPYNEKSDVWALGCVLYELCTGKHPF----EAQNQGALILKIVRGKyPPISASY 225
                       250
                ....*....|....*....
gi 32528297 283 SALAKDLIQRLLMKDPKKR 301
Cdd:cd08529 226 SQDLSQLIDSCLTKDYRQR 244
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
53-302 1.04e-37

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 141.33  E-value: 1.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKativqkaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd14179  13 KPLGEGSFS---ICRKCLHKKTNQEYAVKIVSK-------RMEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL---DSNGHVVLTDFGLSKeFVADETER 209
Cdd:cd14179  83 LLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFAR-LKPPDNQP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 AYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEK---NSQAEISRRILKSEPPYPQE----M 282
Cdd:cd14179 162 LKTPCFTLHYAAPELLN--YNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltcTSAEEIMKKIKQGDFSFEGEawknV 239
                       250       260
                ....*....|....*....|
gi 32528297 283 SALAKDLIQRLLMKDPKKRL 302
Cdd:cd14179 240 SQEAKDLIQGLLTVDPNKRI 259
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
47-302 1.12e-37

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 139.61  E-value: 1.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIvQKAKTTEHTRTERQVleHIR-QSPFLVTLHYAFQTET 125
Cdd:cd14186   1 EDFKVLNLLGKGSFACVYRARSL---HTGLEVAIKMIDKKAM-QKAGMVQRVRNEVEI--HCQlKHPSILELYNYFEDSN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd14186  75 YVYLVLEMCHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKM 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DEtERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQaeisRRILKSEPPYPQEMSA 284
Cdd:cd14186 155 PH-EKHFTMCGTPNYISPEIAT--RSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTL----NKVVLADYEMPAFLSR 227
                       250
                ....*....|....*...
gi 32528297 285 LAKDLIQRLLMKDPKKRL 302
Cdd:cd14186 228 EAQDLIHQLLRKNPADRL 245
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
49-337 2.02e-37

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 139.69  E-value: 2.02e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKAtivqKAKTTEhtrtERQVLEHIRQSPFLVTLHYAFQTETKLH 128
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIHKA---TGKEYAVKIIDKS----KRDPSE----EIEILLRYGQHPNIITLRDVYDDGNSVY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH----VVLTDFGLSKEFVA 204
Cdd:cd14091  71 LVTELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKQLRA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DE----TEraysfCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSQAEISRRI----LKSEP 276
Cdd:cd14091 151 ENgllmTP-----CYTANFVAPEVLK--KQGYDAACDIWSLGVLLYTMLAGYTPFA-SGPNDTPEVILARIgsgkIDLSG 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 277 PYPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQkiNWDDLAAKKVPAPFKP 337
Cdd:cd14091 223 GNWDHVSDSAKDLVRKMLHVDPSQRP-----TAAQVLQHPWIR--NRDSLPQRQLTDPQDA 276
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
55-301 4.37e-37

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 137.67  E-value: 4.37e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKIsghdtGKLYAMKVLKKATIVqkAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd13999   1 IGSGSFGEVYKGKWR-----GTDVAIKKLKVEDDN--DELLKEFRREVSILSKLRH-PNIVQFIGACLSPPPLCIVTEYM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvADETERAYSF 213
Cdd:cd13999  73 PGGSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIK-NSTTEKMTGV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 214 CGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRL 293
Cdd:cd13999 152 VGTPRWMAPEVLRG--EPYTEKADVYSFGIVLWELLTGEVPF--KELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKRC 227

                ....*...
gi 32528297 294 LMKDPKKR 301
Cdd:cd13999 228 WNEDPEKR 235
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
49-318 4.40e-37

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 137.75  E-value: 4.40e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAkttehTRTERQVLEHIR---QSPFLVTLHYAF--QT 123
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARD---KVTGEKVAIKKIKNDFRHPKA-----ALREIKLLKHLNdveGHPNIVKLLDVFehRG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYInGGELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD-SNGHVVLTDFGLSKE 201
Cdd:cd05118  73 GNHLCLVFELM-GMNLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADEterAYSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGaSPFTVDGEKNSQAEISRRILKSEppypqe 281
Cdd:cd05118 152 FTSPP---YTPYVATRWYRAPEVLL-GAKPYGSSIDIWSLGCILAELLTG-RPLFPGDSEVDQLAKIVRLLGTP------ 220
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 282 msaLAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd05118 221 ---EALDLLSKMLKYDPAKRI-----TASQALAHPYF 249
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
49-302 6.03e-37

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 137.66  E-value: 6.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKativqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRV---TRQPYAIKMIET-----KCRGREVCESELNVLRRVRH-TNIIQLIEVFETKERVY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH---VVLTDFGLSKEFVAD 205
Cdd:cd14087  74 MVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDI-VRggdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQE--- 281
Cdd:cd14087 154 PNCLMKTTCGTPEYIAPEIlLR---KPYTQSVDMWAVGVIAYILLSGTMPF----DDDNRTRLYRQILRAKYSYSGEpwp 226
                       250       260
                ....*....|....*....|..
gi 32528297 282 -MSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14087 227 sVSNLAKDFIDRLLTVNPGERL 248
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
49-315 8.67e-37

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 137.61  E-value: 8.67e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHtrtERQVLEHIRQSPF--LVTLHYAFQTETK 126
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVK---TGRVVALKVLNLDTDDDDVSDIQK---EVALLSQLKLGQPknIIKYYGSYLKGPS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFThLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd06917  77 LWIIMDYCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAySFCGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPY--PQEMSA 284
Cdd:cd06917 156 SKRS-TFVGTPYWMAPEVITEGKY-YDTKADIWSLGITTYEMATGNPPYS----DVDALRAVMLIPKSKPPRleGNGYSP 229
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 285 LAKDLIQRLLMKDPKKRLgcgprDADE------IKEH 315
Cdd:cd06917 230 LLKEFVAACLDEEPKDRL-----SADEllkskwIKQH 261
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
419-548 8.67e-37

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 137.49  E-value: 8.67e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 419 FYQHYDLdlKDKpLGEGSFSICRKCVHKKSNQAFAVKIIS-----------KRMEANTQKEITALKLCEGHPNIVKLHEV 487
Cdd:cd14093   1 FYAKYEP--KEI-LGRGVSSTVRRCIEKETGQEFAVKIIDitgeksseneaEELREATRREIEILRQVSGHPNIIELHDV 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 488 FHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14093  78 FESPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPE 138
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
49-320 1.91e-36

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 136.61  E-value: 1.91e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLvrkisGHD--TGKLYAMKV--LKKA-----TIVQkakttehtrtERQVLEHIRqSPFLVTLHY 119
Cdd:cd06609   3 FTLLERIGKGSFGEVYK-----GIDkrTNQVVAIKVidLEEAedeieDIQQ----------EIQFLSQCD-SPYITKYYG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 AFQTETKLHLILDYINGGELFtHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd06609  67 SFLKGSKLWIIMEYCGGGSVL-DLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVS 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KEfVADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgeknsqAEIS-----RRILKS 274
Cdd:cd06609 146 GQ-LTSTMSKRNTFVGTPFWMAPEVIKQ--SGYDEKADIWSLGITAIELAKGEPPL---------SDLHpmrvlFLIPKN 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 275 EPPY--PQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQK 320
Cdd:cd06609 214 NPPSleGNKFSKPFKDFVELCLNKDPKERP-----SAKELLKHKFIKK 256
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
53-317 1.93e-36

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 136.28  E-value: 1.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKIsghDTGKLYAMKVLkkATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILD 132
Cdd:cd06626   6 NKIGEGTFGKVYTAVNL---DTGELMAMKEI--RFQDNDPKTIKEIADEMKVLEGLDH-PNLVRYYGVEVHREEVYIFME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET----E 208
Cdd:cd06626  80 YCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTtmapG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSFCGTIEYMAPDIVRGGD-SGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISRRI-LKSEPPYPQ--EMSA 284
Cdd:cd06626 160 EVNSLVGTPAYMAPEVITGNKgEGHGRAADIWSLGCVVLEMATGKRPWS---ELDNEWAIMYHVgMGHKPPIPDslQLSP 236
                       250       260       270
                ....*....|....*....|....*....|...
gi 32528297 285 LAKDLIQRLLMKDPKKRLgcgprDADEIKEHLF 317
Cdd:cd06626 237 EGKDFLSRCLESDPKKRP-----TASELLDHPF 264
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
55-302 8.24e-36

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 134.34  E-value: 8.24e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISGHDTgkLYAMKVLKKATIvqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd14121   3 LGSGTYATVYKAYRKSGARE--VVAVKCVSKSSL--NKASTENLLTEIELLKKLKH-PHIVELKDFQWDEEHIYLIMEYC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVL--TDFGLSKEFvaDETERAYS 212
Cdd:cd14121  78 SGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLklADFGFAQHL--KPNDEAHS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEP---PYPQEMSALAKDL 289
Cdd:cd14121 156 LRGSPLYMAPEMILKKK--YDARVDLWSVGVILYECLFGRAPFA----SRSFEELEEKIRSSKPieiPTRPELSADCRDL 229
                       250
                ....*....|...
gi 32528297 290 IQRLLMKDPKKRL 302
Cdd:cd14121 230 LLRLLQRDPDRRI 242
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
49-318 9.50e-36

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 134.35  E-value: 9.50e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVflvRKISGHDTGKLYAMKvlkkatIVQKAKTTEHTRT-----ERQVLEHIRQsPFLVTLHYAFQT 123
Cdd:cd14162   2 YIVGKTLGHGSYAVV---KKAYSTKHKCKVAIK------IVSKKKAPEDYLQkflprEIEVIKGLKH-PNLICFYEAIET 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK-EF 202
Cdd:cd14162  72 TSRVYIIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgVM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETERAYS--FCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPypq 280
Cdd:cd14162 152 KTKDGKPKLSetYCGSYAYASPEILR-GIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRVVFPKNP--- 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 32528297 281 EMSALAKDLIQRLLMKdPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14162 228 TVSEECKDLILRMLSP-VKKRI-----TIEEIKRDPWF 259
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
426-548 1.48e-35

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 133.65  E-value: 1.48e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKDKpLGEGSFSICRKCVHKKSNQAFAVKIISKRM----EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd14083   6 EFKEV-LGTGAFSEVVLAEDKATGKLVAIKCIDKKAlkgkEDSLENEIAVLRKIK-HPNIVQLLDIYESKSHLYLVMELV 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14083  84 TGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPE 130
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
46-301 3.09e-35

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 133.12  E-value: 3.09e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTG--AYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTteHTRTERQVLEHIRQSPFLVTLHYAFQT 123
Cdd:cd14198   2 MDNFNNFYILTSKelGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRA--EILHEIAVLELAKSNPRVVNLHEVYET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGELFTHL--SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSN---GHVVLTDFGL 198
Cdd:cd14198  80 TSEIILILEYAAGGEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGM 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKEfVADETErAYSFCGTIEYMAPDIVrggdsGHD---KAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISR-RILKS 274
Cdd:cd14198 160 SRK-IGHACE-LREIMGTPEYLAPEIL-----NYDpitTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQvNVDYS 232
                       250       260
                ....*....|....*....|....*..
gi 32528297 275 EPPYpQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14198 233 EETF-SSVSQLATDFIQKLLVKNPEKR 258
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
48-301 4.35e-35

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 132.86  E-value: 4.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHTRTERQ---VLEHIRQSPFLVTLHYAFQTE 124
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLR---TGRKYAIKCLYKSGPNSKDGNDFQKLPQLReidLHRRVSRHPNIITLHDVFETE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERF---TEHEVQIYVgEIVLALEHLHKLGIIYRDIKLENILLDSN-GHVVLTDFGLsk 200
Cdd:cd13993  78 VAIYIVLEYCPNGDLFEAITENRIYvgkTELIKNVFL-QLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGL-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 efvADETERAYSF-CGTIEYMAP---DIVRGGDSGHD-KAVDWWSLGVLMYELLTGASPFTVDGEK----NSQAEISRRI 271
Cdd:cd13993 155 ---ATTEKISMDFgVGSEFYMAPecfDEVGRSLKGYPcAAGDIWSLGIILLNLTFGRNPWKIASESdpifYDYYLNSPNL 231
                       250       260       270
                ....*....|....*....|....*....|
gi 32528297 272 LKSEPPypqeMSALAKDLIQRLLMKDPKKR 301
Cdd:cd13993 232 FDVILP----MSDDFYNLLRQIFTVNPNNR 257
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
53-319 6.43e-35

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 132.85  E-value: 6.43e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVflvRKISGHDTGKLYAMKVLKK------ATIVQKAKTTEHTRTERQVLEHIRqspflvtlhyAFQTETK 126
Cdd:cd14174   8 ELLGEGAYAKV---QGCVSLQNGKEYAVKIIEKnaghsrSRVFREVETLYQCQGNKNILELIE----------FFEDDTR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV---LTDFGLSKEFV 203
Cdd:cd14174  75 FYLVFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSpvkICDFDLGSGVK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADE------TERAYSFCGTIEYMAPDIVR---GGDSGHDKAVDWWSLGVLMYELLTGASPFTVD---------GE--KNS 263
Cdd:cd14174 155 LNSactpitTPELTTPCGSAEYMAPEVVEvftDEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrGEvcRVC 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 264 QAEISRRILKSEPPYPQ----EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd14174 235 QNKLFESIQEGKYEFPDkdwsHISSEAKDLISKLLVRDAKERL-----SAAQVLQHPWVQ 289
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
52-301 1.13e-34

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 131.47  E-value: 1.13e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIvqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLIL 131
Cdd:cd08218   5 IKKIGEGSFGKALLVKS---KEDGKQYVIKEINISKM--SPKEREESRKEVAVLSKMKH-PNIVQYQESFEENGNLYIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQRE--RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADET-E 208
Cdd:cd08218  79 DYCDGGDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIAR--VLNSTvE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRrilKSEPPYPQEMSALAKD 288
Cdd:cd08218 157 LARTCIGTPYYLSPEICE--NKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIR---GSYPPVPSRYSYDLRS 231
                       250
                ....*....|...
gi 32528297 289 LIQRLLMKDPKKR 301
Cdd:cd08218 232 LVSQLFKRNPRDR 244
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
47-301 1.88e-34

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 136.15  E-value: 1.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQSPF-LVTLHYAF---- 121
Cdd:PTZ00283  32 KKYWISRVLGSGATGTVLCAKRVS---DGEPFAVKVVD----MEGMSEADKNRAQAEVCCLLNCDFFsIVKCHEDFakkd 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  122 ----QTETKLHLILDYINGGELFTHLSQRER----FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVL 193
Cdd:PTZ00283 105 prnpENVLMIALVLDYANAGDLRQEIKSRAKtnrtFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  194 TDFGLSKEF---VADETERaySFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvDGEknSQAEISRR 270
Cdd:PTZ00283 185 GDFGFSKMYaatVSDDVGR--TFCGTPYYVAPEIWR--RKPYSKKADMFSLGVLLYELLTLKRPF--DGE--NMEEVMHK 256
                        250       260       270
                 ....*....|....*....|....*....|..
gi 32528297  271 ILKSE-PPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:PTZ00283 257 TLAGRyDPLPPSISPEMQEIVTALLSSDPKRR 288
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
432-548 2.21e-34

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 129.31  E-value: 2.21e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT----QKEITALKLCeGHPNIVKLHEVFHDQLHTFLVMELLNGGELF 507
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLleelLREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 508 ERIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd00180  80 DLLKENKGpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPE 121
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
46-321 2.31e-34

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 131.02  E-value: 2.31e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLkkatIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTET 125
Cdd:cd06611   4 NDIWEIIGELGDGAFGKVYKAQH---KETGLFAAAKII----QIESEEELEDFMVEIDILSECKH-PNIVGLYEAYFYEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVA 204
Cdd:cd06611  76 KLWILIEFCDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAK-NK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPftvdgekNSQAEISR---RILKSEPP- 277
Cdd:cd06611 155 STLQKRDTFIGTPYWMAPEVVaceTFKDNPYDYKADIWSLGITLIELAQMEPP-------HHELNPMRvllKILKSEPPt 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 278 --YPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQKI 321
Cdd:cd06611 228 ldQPSKWSSSFNDFLKSCLVKDPDDRP-----TAAELLKHPFVSDQ 268
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
47-301 2.58e-34

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 130.54  E-value: 2.58e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKAtivqKAKTTEH-TRTERQVLEHIRQsPFLVTLHYAFQTET 125
Cdd:cd14184   1 EKYKIGKVIGDGNFA---VVKECVERSTGKEFALKIIDKA----KCCGKEHlIENEVSILRRVKH-PNIIMLIEEMDTPA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL----DSNGHVVLTDFGLSKe 201
Cdd:cd14184  73 ELYLVMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLAT- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fVADETerAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRILKSE----PP 277
Cdd:cd14184 152 -VVEGP--LYTVCGTPTYVAPEII--AETGYGLKVDIWAAGVITYILLCGFPPFR--SENNLQEDLFDQILLGKlefpSP 224
                       250       260
                ....*....|....*....|....
gi 32528297 278 YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14184 225 YWDNITDSAKELISHMLQVNVEAR 248
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
55-302 3.08e-34

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 131.53  E-value: 3.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGkvfLVRKISGHDTGKLYAMKVLKKativqkaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd14180  14 LGEGSFS---VCRKCRHRQSGQEYAVKIISR-------RMEANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL--DSNGHVV-LTDFGLSKEFVADeTERAY 211
Cdd:cd14180  84 RGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadESDGAVLkVIDFGFARLRPQG-SRPLQ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVD---GEKNSQAEISRRILKS----EPPYPQEMSA 284
Cdd:cd14180 163 TPCFTLQYAAPELFS--NQGYDESCDLWSLGVILYTMLSGQVPFQSKrgkMFHNHAADIMHKIKEGdfslEGEAWKGVSE 240
                       250
                ....*....|....*...
gi 32528297 285 LAKDLIQRLLMKDPKKRL 302
Cdd:cd14180 241 EAKDLVRGLLTVDPAKRL 258
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
48-304 3.47e-34

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 130.91  E-value: 3.47e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAmkvLKKATIVQK-AKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRE---TGETVA---LKKVALRKLeGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYInGGELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvAD 205
Cdd:cd07832  75 FVLVFEYM-LSSLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLF-SE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSF-CGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFtvDGEKN-SQAEISRRIL----------- 272
Cdd:cd07832 153 EDPRLYSHqVATRWYRAPELLYGSRK-YDEGVDLWAVGCIFAELLNGSPLF--PGENDiEQLAIVLRTLgtpnektwpel 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 273 KSEPPYPQ----------------EMSALAKDLIQRLLMKDPKKRLGC 304
Cdd:cd07832 230 TSLPDYNKitfpeskgirleeifpDCSPEAIDLLKGLLVYNPKKRLSA 277
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
53-301 5.55e-34

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 129.67  E-value: 5.55e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATIV---QKAKTTEHTRTERQvLEHirqsPFLVTLHYAFQTETKLHL 129
Cdd:cd14187  13 RFLGKGGFAKCY---EITDADTKEVFAGKIVPKSLLLkphQKEKMSMEIAIHRS-LAH----QHVVGFHGFFEDNDFVYV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVADETER 209
Cdd:cd14187  85 VLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATK-VEYDGER 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 AYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKDL 289
Cdd:cd14187 164 KKTLCGTPNYIAPEVL--SKKGHSFEVDIWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSIPKHINPVAASL 237
                       250
                ....*....|..
gi 32528297 290 IQRLLMKDPKKR 301
Cdd:cd14187 238 IQKMLQTDPTAR 249
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
421-548 7.20e-34

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 130.23  E-value: 7.20e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 421 QHYDLDLKdkpLGEGSFSICRKCVHKKSNQAFAVKII-SKRMEA-NTQKEITALKLCE--GHPNIVKLHEVFHDQLHTFL 496
Cdd:cd14086   1 DEYDLKEE---LGKGAFSVVRRCVQKSTGQEFAAKIInTKKLSArDHQKLEREARICRllKHPNIVRLHDSISEEGFHYL 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 497 VMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14086  78 VFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPE 129
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
48-301 7.39e-34

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 128.92  E-value: 7.39e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRkisghdtGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIR-QSPFLVTLHYAFQTETK 126
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLAK-------AKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKmKHPNIVTFFASFQENGR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLsQRER---FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV-LTDFGLSKEf 202
Cdd:cd08225  74 LFIVMEYCDGGDLMKRI-NRQRgvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAkLGDFGIARQ- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSE-PPYPQE 281
Cdd:cd08225 152 LNDSMELAYTCVGTPYYLSPEICQ--NRPYNNKTDIWSLGCVLYELCTLKHPF----EGNNLHQLVLKICQGYfAPISPN 225
                       250       260
                ....*....|....*....|
gi 32528297 282 MSALAKDLIQRLLMKDPKKR 301
Cdd:cd08225 226 FSRDLRSLISQLFKVSPRDR 245
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
47-302 8.59e-34

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 128.99  E-value: 8.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATivQKAKTTEHTRTERQvLEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd14069   1 EDWDLVQTLGEGAFGEVFLAVNRN---TEEAVAVKFVDMKR--APGDCPENIKKEVC-IQKMLSHKNVVRFYGHRREGEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd14069  75 QYLFLEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERA-YSFCGTIEYMAPDIVrGGDSGHDKAVDWWSLGVLMYELLTGASPFtvDGEKNSQAEISRRI---LKSEPPYPQeM 282
Cdd:cd14069 155 KERLlNKMCGTLPYVAPELL-AKKKYRAEPVDVWSCGIVLFAMLAGELPW--DQPSDSCQEYSDWKenkKTYLTPWKK-I 230
                       250       260
                ....*....|....*....|
gi 32528297 283 SALAKDLIQRLLMKDPKKRL 302
Cdd:cd14069 231 DTAALSLLRKILTENPNKRI 250
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
48-318 1.09e-33

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 128.63  E-value: 1.09e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVlkkatiVQKAKTTEHTRTERQVLEhiRQSPFLVTLHY-------- 119
Cdd:cd06625   1 NWKQGKLLGQGAFGQVYLCYDA---DTGRELAVKQ------VEIDPINTEASKEVKALE--CEIQLLKNLQHerivqyyg 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 AFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd06625  70 CLQDEKSLSIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGAS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KEFVADETERAY-SFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgeknSQAEISRRILK----- 273
Cdd:cd06625 150 KRLQTICSSTGMkSVTGTPYWMSPEVING--EGYGRKADIWSVGCTVVEMLTTKPPW-------AEFEPMAAIFKiatqp 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 32528297 274 SEPPYPQEMSALAKDLIQRLLMKDPKKRlgcgPrDADEIKEHLFF 318
Cdd:cd06625 221 TNPQLPPHVSEDARDFLSLIFVRNKKQR----P-SAEELLSHSFV 260
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
55-304 1.13e-33

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 128.58  E-value: 1.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVF-LVRKisghDTGKLYAMKVLKKATivqkAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDY 133
Cdd:cd14191  10 LGSGKFGQVFrLVEK----KTKKVWAGKFFKAYS----AKEKENIRQEISIMNCLHH-PKLVQCVDAFEEKANIVMVLEM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL--DSNGHVVLTDFGLSKEFvadetERA 210
Cdd:cd14191  81 VSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLARRL-----ENA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 YSF---CGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAK 287
Cdd:cd14191 156 GSLkvlFGTPEFVAPEVINYEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAK 233
                       250
                ....*....|....*..
gi 32528297 288 DLIQRLLMKDPKKRLGC 304
Cdd:cd14191 234 DFISNLLKKDMKARLTC 250
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
75-301 1.58e-33

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 133.22  E-value: 1.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   75 GKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQspFLVTLHYA-FQTETKLHLILDYINGGELFTHLSQR--ER--F 149
Cdd:PTZ00267  89 GSDPKEKVVAKFVMLNDERQAAYARSELHCLAACDH--FGIVKHFDdFKSDDKLLLIMEYGSGGDLNKQIKQRlkEHlpF 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  150 TEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET-ERAYSFCGTIEYMAPDIVRgg 228
Cdd:PTZ00267 167 QEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSlDVASSFCGTPYYLAPELWE-- 244
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297  229 DSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSE-PPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:PTZ00267 245 RKRYSKKADMWSLGVILYELLTLHRPF----KGPSQREIMQQVLYGKyDPFPCPVSSGMKALLDPLLSKNPALR 314
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
430-548 1.63e-33

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 127.98  E-value: 1.63e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR------MEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14007   6 KPLGKGKFGNVYLAREKKSGFIVALKVISKSqlqksgLEHQLRREIEIQSHLR-HPNILRLYGYFEDKKRIYLILEYAPN 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14007  85 GELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPE 129
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
47-302 1.67e-33

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 128.09  E-value: 1.67e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKakttEHTRTERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd14114   2 DHYDILEELGTGAFGVVHRCTERA---TGNNFAAKFIMTPHESDK----ETVRKEIQIMNQLHH-PKLINLHDAFEDDNE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD--SNGHVVLTDFGLSKEFV 203
Cdd:cd14114  74 MVLILEFLSGGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSfcGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMS 283
Cdd:cd14114 154 PKESVKVTT--GTAEFAAPEIVEREPVGF--YTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGIS 229
                       250
                ....*....|....*....
gi 32528297 284 ALAKDLIQRLLMKDPKKRL 302
Cdd:cd14114 230 EEAKDFIRKLLLADPNKRM 248
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
47-302 1.75e-33

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 128.18  E-value: 1.75e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLK-VLGTGAYGKVFlvrKISGHDTGKLYAMKVLkkativqkaktTEHTRTERQVLEHIRQS--PFLVTLHYAFQT 123
Cdd:cd14172   3 DDYKLSKqVLGLGVNGKVL---ECFHRRTGQKCALKLL-----------YDSPKARREVEHHWRASggPHIVHILDVYEN 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETK----LHLILDYINGGELFTHLSQR--ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS---NGHVVLT 194
Cdd:cd14172  69 MHHgkrcLLIIMECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSkekDAVLKLT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 195 DFGLSKEFVADETERaySFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKS 274
Cdd:cd14172 149 DFGFAKETTVQNALQ--TPCYTPYYVAPEVL--GPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRMG 224
                       250       260       270
                ....*....|....*....|....*....|..
gi 32528297 275 EPPYPQ----EMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14172 225 QYGFPNpewaEVSEEAKQLIRHLLKTDPTERM 256
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
55-302 2.12e-33

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 128.73  E-value: 2.12e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLkkativqkaktTEHTRTERQVLEHIRQS--PFLVTLHYAFQTE-------- 124
Cdd:cd14171  14 LGTGISGPVRVCVKKS---TGERFALKIL-----------LDRPKARTEVRLHMMCSghPNIVQIYDVYANSvqfpgess 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 --TKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH---VVLTDFGLS 199
Cdd:cd14171  80 prARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGFA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KEFVADETERAYsfcgTIEYMAPDIV------RGGDSG---------HDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQ 264
Cdd:cd14171 160 KVDQGDLMTPQF----TPYYVAPQVLeaqrrhRKERSGiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFY--SEHPSR 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 32528297 265 A---EISRRILKSEPPYPQE----MSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14171 234 TitkDMKRKIMTGSYEFPEEewsqISEMAKDIVRKLLCVDPEERM 278
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
48-301 2.13e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 127.78  E-value: 2.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVN---SDQKYAMKEIR---LPKSSSAVEDSRKEAVLLAKMKH-PNIVAFKESFEADGHL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLS-QRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGlSKEFVAD 205
Cdd:cd08219  74 YIVMEYCDGGDLMQKIKlQRGKlFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFG-SARLLTS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKsepPYPQEMSAL 285
Cdd:cd08219 153 PGAYACTYVGTPYYVPPEIWE--NMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYK---PLPSHYSYE 227
                       250
                ....*....|....*.
gi 32528297 286 AKDLIQRLLMKDPKKR 301
Cdd:cd08219 228 LRSLIKQMFKRNPRSR 243
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
426-548 2.47e-33

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 128.69  E-value: 2.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRmEANTQ----KEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd14090   4 KLTGELLGEGAYASVQTCINLYTGKEYAVKIIEKH-PGHSRsrvfREVETLHQCQGHPNILQLIEYFEDDERFYLVFEKM 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14090  83 RGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPE 129
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
55-302 3.01e-33

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 127.42  E-value: 3.01e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISgHDTGKLYAMKVLKKATIVQKAK-TTEHTRTERQVLEHIRqSPFLVTLHYAFQTET-KLHLILD 132
Cdd:cd13994   1 IGKGATSVVRIVTKKN-PRSGVLYAVKEYRRRDDESKRKdYVKRLTSEYIISSKLH-HPNIVKVLDLCQDLHgKWCLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF-VADETERAY 211
Cdd:cd13994  79 YCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFgMPAEKESPM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 S--FCGTIEYMAPDIVRGGdsGHD-KAVDWWSLGVLMYELLTGASPFTV--DGEKNSQAEISRRILKSEPPYPQEMS--A 284
Cdd:cd13994 159 SagLCGSEPYMAPEVFTSG--SYDgRAVDVWSCGIVLFALFTGRFPWRSakKSDSAYKAYEKSGDFTNGPYEPIENLlpS 236
                       250
                ....*....|....*...
gi 32528297 285 LAKDLIQRLLMKDPKKRL 302
Cdd:cd13994 237 ECRRLIYRMLHPDPEKRI 254
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
61-301 3.07e-33

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 127.74  E-value: 3.07e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  61 GKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTteHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYINGGELF 140
Cdd:cd14197  20 GKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRM--EIIHEIAVLELAQANPWVINLHEVYETASEMILVLEYAAGGEIF 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 141 TH-LSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSN---GHVVLTDFGLSKefVADETERAYSFCG 215
Cdd:cd14197  98 NQcVADREEaFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSR--ILKNSEELREIMG 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 216 TIEYMAPDIVrggdsGHDK---AVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQR 292
Cdd:cd14197 176 TPEYVAPEIL-----SYEPistATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEFEHLSESAIDFIKT 250

                ....*....
gi 32528297 293 LLMKDPKKR 301
Cdd:cd14197 251 LLIKKPENR 259
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
47-318 5.12e-33

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 126.89  E-value: 5.12e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTgaYGKVFLVRKISghdTGKLYAMKVLKKativqkakTTEHTRTERQVLEHirQSPFLVTLHYAFQTETK 126
Cdd:cd05576   1 EELKAFRVLGV--IDKVLLVMDTR---TQETFILKGLRK--------SSEYSRERKTIIPR--CVPNMVCLRKYIISEES 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQ----------------------RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL 184
Cdd:cd05576  66 VFLVLQHAEGGKLWSYLSKflndkeihqlfadlderlaaasRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNIL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 185 LDSNGHVVLTDFGLSKEfVADETERAysfcgTIE--YMAPDIvrGGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgeKN 262
Cdd:cd05576 146 LNDRGHIQLTYFSRWSE-VEDSCDSD-----AIEnmYCAPEV--GGISEETEACDWWSLGALLFELLTGKALV-----EC 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 263 SQAEISRRILKSEPPYpqeMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFF 318
Cdd:cd05576 213 HPAGINTHTTLNIPEW---VSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
53-302 5.49e-33

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 127.45  E-value: 5.49e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVflvRKISGHDTGKLYAMKVLKK------ATIVQKAKTTEHTRTERQVLEHIRqspflvtlhyAFQTETK 126
Cdd:cd14173   8 EVLGEGAYARV---QTCINLITNKEYAVKIIEKrpghsrSRVFREVEMLYQCQGHRNVLELIE----------FFEEEDK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV---LTDFGLSK--E 201
Cdd:cd14173  75 FYLVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSpvkICDFDLGSgiK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVAD----ETERAYSFCGTIEYMAPDIVRGGD---SGHDKAVDWWSLGVLMYELLTGASPFTVD---------GE--KNS 263
Cdd:cd14173 155 LNSDcspiSTPELLTPCGSAEYMAPEVVEAFNeeaSIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrGEacPAC 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 32528297 264 QAEISRRILKSEPPYPQE----MSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14173 235 QNMLFESIQEGKYEFPEKdwahISCAAKDLISKLLVRDAKQRL 277
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
49-301 5.61e-33

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 126.73  E-value: 5.61e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQ----KAKTTEHTRTERQVLEHIRQS--PFLVTLHYAFQ 122
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAIYKS---KGKEVVIKFIFKERILVdtwvRDRKLGTVPLEIHILDTLNKRshPNIVKLLDFFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILD-YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGlSKE 201
Cdd:cd14004  79 DDEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG-SAA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVadETERAYSFCGTIEYMAPDIVRGGDSGhDKAVDWWSLGVLMYELLTGASPFTvdgeknsqaEISrRILKSEPPYPQE 281
Cdd:cd14004 158 YI--KSGPFDTFVGTIDYAAPEVLRGNPYG-GKEQDIWALGVLLYTLVFKENPFY---------NIE-EILEADLRIPYA 224
                       250       260
                ....*....|....*....|
gi 32528297 282 MSALAKDLIQRLLMKDPKKR 301
Cdd:cd14004 225 VSEDLIDLISRMLNRDVGDR 244
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
55-318 7.31e-33

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 126.22  E-value: 7.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRqSPFLVTLHYAFQTET--KLHLILD 132
Cdd:cd14119   1 LGEGSYGKVKEVLDT---ETLCRRAVKILKKRKLRRIPNGEANVKREIQILRRLN-HRNVIKLVDVLYNEEkqKLYMVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGG-ELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE---FVADETE 208
Cdd:cd14119  77 YCVGGlQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEAldlFAEDDTC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSfcGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKD 288
Cdd:cd14119 157 TTSQ--GSPAFQPPEIANGQDSFSGFKVDIWSAGVTLYNMTTGKYPF----EGDNIYKLFENIGKGEYTIPDDVDPDLQD 230
                       250       260       270
                ....*....|....*....|....*....|
gi 32528297 289 LIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14119 231 LLRGMLEKDPEKRF-----TIEQIRQHPWF 255
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
47-318 7.63e-33

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 126.70  E-value: 7.63e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdtgklYAMKVLKKATIVQKAKTT-EHTRTERQVLEHIrQSPFLVTLHYAFQTET 125
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLP-------KKEKVAIKRIDLEKCQTSmDELRKEIQAMSQC-NHPNVVSYYTSFVVGD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRER---FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKeF 202
Cdd:cd06610  73 ELWLVMPLLSGGSLLDIMKSSYPrggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSA-S 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETERA----YSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPY 278
Cdd:cd06610 152 LATGGDRTrkvrKTFVGTPCWMAPEVME-QVRGYDFKADIWSFGITAIELATGAAPYS----KYPPMKVLMLTLQNDPPS 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 279 PQE------MSALAKDLIQRLLMKDPKKRlgcgPrDADEIKEHLFF 318
Cdd:cd06610 227 LETgadykkYSKSFRKMISLCLQKDPSKR----P-TAEELLKHKFF 267
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
55-315 1.44e-32

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 125.93  E-value: 1.44e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGkvfLVRKISGHDTGKLYAMKVLKKATIVQKA---------KTTEHTRTERQVLEHIRQS---------PFLVT 116
Cdd:cd14118   2 IGKGSYG---IVKLAYNEEDNTLYAMKILSKKKLLKQAgffrrppprRKPGALGKPLDPLDRVYREiailkkldhPNVVK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 117 LHYAFQ--TETKLHLILDYINGGELFTHLSQrERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLT 194
Cdd:cd14118  79 LVEVLDdpNEDNLYMVFELVDKGAVMEVPTD-NPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 195 DFGLSKEFVADETERAySFCGTIEYMAPDIVRGG-DSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILK 273
Cdd:cd14118 158 DFGVSNEFEGDDALLS-STAGTPAFMAPEALSESrKKFSGKALDIWAMGVTLYCFVFGRCPF----EDDHILGLHEKIKT 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 32528297 274 SEPPYPQE--MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14118 233 DPVVFPDDpvVSEQLKDLILRMLDKNPSERI-----TLPEIKEH 271
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
48-301 2.09e-32

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 125.31  E-value: 2.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGhdTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEH---IRQS---PFLVTLHYAF 121
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKVRKKSN--GQTLLALKEINMTNPAFGRTEQERDKSVGDIISEvniIKEQlrhPNIVRYYKTF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYING---GELFTHLSQR-ERFTEHEVQIYVGEIVLALEHLHK-LGIIYRDIKLENILLDSNGHVVLTDF 196
Cdd:cd08528  79 LENDRLYIVMELIEGaplGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 197 GLSKEFVADETeRAYSFCGTIEYMAPDIVRGGDSGhDKAvDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSE- 275
Cdd:cd08528 159 GLAKQKGPESS-KMTSVVGTILYSCPEIVQNEPYG-EKA-DIWALGCILYQMCTLQPPFYST----NMLTLATKIVEAEy 231
                       250       260
                ....*....|....*....|....*..
gi 32528297 276 PPYPQEM-SALAKDLIQRLLMKDPKKR 301
Cdd:cd08528 232 EPLPEGMySDDITFVIRSCLTPDPEAR 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
430-548 2.09e-32

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 124.82  E-value: 2.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK------RMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14663   6 RTLGEGTFAKVKFARNTKTGESVAIKIIDKeqvareGMVEQIKREIAIMKLLR-HPNIVELHEVMATKTKIFFVMELVTG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14663  85 GELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPE 129
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
47-302 2.40e-32

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 127.06  E-value: 2.40e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKativQKAKTTEhtrtERQVLEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd14176  19 DGYEVKEDIGVGSYS---VCKRCIHKATNMEFAVKIIDK----SKRDPTE----EIEILLRYGQHPNIITLKDVYDDGKY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL-LDSNGH---VVLTDFGLSKEF 202
Cdd:cd14176  88 VYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VAdETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSQAEISRRI----LKSEPPY 278
Cdd:cd14176 168 RA-ENGLLMTPCYTANFVAPEVLE--RQGYDAACDIWSLGVLLYTMLTGYTPFA-NGPDDTPEEILARIgsgkFSLSGGY 243
                       250       260
                ....*....|....*....|....
gi 32528297 279 PQEMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14176 244 WNSVSDTAKDLVSKMLHVDPHQRL 267
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
53-318 2.57e-32

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 124.74  E-value: 2.57e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIvqkAKTTEHTRTERQV-LEHIRQSPFLVTLHYAFQTETKLHLIL 131
Cdd:cd14188   7 KVLGKGGFAKCYEMTDLT---TNKVYAAKIIPHSRV---SKPHQREKIDKEIeLHRILHHKHVVQFYHYFEDKENIYILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAy 211
Cdd:cd14188  81 EYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRR- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKDLIQ 291
Cdd:cd14188 160 TICGTPNYLSPEVL--NKQGHGCESDIWALGCVMYTMLLGRPPF----ETTNLKETYRCIREARYSLPSSLLAPAKHLIA 233
                       250       260
                ....*....|....*....|....*..
gi 32528297 292 RLLMKDPKKRlgcgpRDADEIKEHLFF 318
Cdd:cd14188 234 SMLSKNPEDR-----PSLDEIIRHDFF 255
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
422-548 2.69e-32

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 124.75  E-value: 2.69e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKR----MEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd14095   1 KYDIG---RVIGDGNFAVVKECRDKATDKEYALKIIDKAkckgKEHMIENEVAILRRVK-HPNIVQLIEEYDTDTELYLV 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14095  77 MELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPE 127
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
55-302 4.32e-32

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 124.58  E-value: 4.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKIsghDTGKLYAMKVLKKativQKAKTTEHTRTERQV--LEHIRQSpFLVTLHYAFQTETKLHLILD 132
Cdd:cd14097   9 LGQGSFGVVIEATHK---ETQTKWAIKKINR----EKAGSSAVKLLEREVdiLKHVNHA-HIIHLEEVFETPKRMYLVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG-------HVVLTDFGLSKEFVAD 205
Cdd:cd14097  81 LCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSVQKYGL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGDSGHDkaVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSAL 285
Cdd:cd14097 161 GEDMLQETCGTPIYMAPEVISAHGYSQQ--CDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDA 238
                       250
                ....*....|....*..
gi 32528297 286 AKDLIQRLLMKDPKKRL 302
Cdd:cd14097 239 AKNVLQQLLKVDPAHRM 255
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
430-548 7.73e-32

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 123.86  E-value: 7.73e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR--MEANTQK----EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05581   7 KPLGEGSYSTVVLAKEKETGKEYAIKVLDKRhiIKEKKVKyvtiEKEVLSRLA-HPGIVKLYYTFQDESKLYFVLEYAPN 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05581  86 GDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPE 130
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
47-318 9.03e-32

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 123.97  E-value: 9.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKAtivqkaKTTEHTRT----ERQVLEHIRQsPFLVTLHYAFQ 122
Cdd:cd07833   1 NKYEVLGVVGEGAYGVVLKCRN---KATGEIVAIKKFKES------EDDEDVKKtalrEVKVLRQLRH-ENIVNLKEAFR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGgelfTHLSQRERF----TEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGL 198
Cdd:cd07833  71 RKGRLYLVFEYVER----TLLELLEASpgglPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKEFVADETERAYSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNsQAEISRRILKSEPP- 277
Cdd:cd07833 147 ARALTARPASPLTDYVATRWYRAPELLV-GDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDID-QLYLIQKCLGPLPPs 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 278 ----------------------------YPQEMSALAKDLIQRLLMKDPKKRLGCgprdaDEIKEHLFF 318
Cdd:cd07833 225 hqelfssnprfagvafpepsqpeslerrYPGKVSSPALDFLKACLRMDPKERLTC-----DELLQHPYF 288
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
432-547 9.08e-32

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 124.37  E-value: 9.08e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRmEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIK 511
Cdd:cd14175   9 IGVGSYSVCKRCVHKATNMEYAVKVIDKS-KRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKIL 87
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 32528297 512 KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14175  88 RQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKP 123
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
49-319 1.27e-31

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 122.70  E-value: 1.27e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKaKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRA---TGKEVAIKKMR----LRK-QNKELIINEILIMKECKH-PNIVDYYDSYLVGDELW 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET 207
Cdd:cd06614  73 VVMEYMDGGSLTDIITQNPvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 ERAySFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPP---YPQEMSA 284
Cdd:cd06614 153 KRN-SVVGTPYWMAPEVIKRKD--YGPKVDIWSLGIMCIEMAEGEPPYLEE----PPLRALFLITTKGIPplkNPEKWSP 225
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 285 LAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd06614 226 EFKDFLNKCLVKDPEKRP-----SAEELLQHPFLK 255
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
432-548 2.65e-31

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 121.86  E-value: 2.65e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR------MEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKeiikrkEVEHTLNERNILERVN-HPFIVKLHYAFQTEEKLYLVLDYVPGGE 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05123  80 LFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPE 122
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
47-301 2.96e-31

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 121.60  E-value: 2.96e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLK-KATIVQKAKttehtrtERQVLEHIRqSPFLVTLHYAFQTET 125
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHK---ETGQVVAIKVVPvEEDLQEIIK-------EISILKQCD-SPYIVKYYGSYFKNT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVa 204
Cdd:cd06612  72 DLWIVMEYCGAGSVSDIMKITNKtLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLT- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgeknsqAEI--SRRIL--KSEPP--- 277
Cdd:cd06612 151 DTMAKRNTVIGTPFWMAPEVI--QEIGYNNKADIWSLGITAIEMAEGKPPY---------SDIhpMRAIFmiPNKPPptl 219
                       250       260
                ....*....|....*....|....*
gi 32528297 278 -YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd06612 220 sDPEKWSPEFNDFVKKCLVKDPEER 244
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
47-322 6.29e-31

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 122.06  E-value: 6.29e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd06644  12 EVWEIIGELGDGAFGKVY---KAKNKETGALAAAKVIE----TKSEEELEDYMVEIEILATCNH-PYIVKLLGAFYWDGK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVaD 205
Cdd:cd06644  84 LWIMIEFCPGGAVDAIMLELDRgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNV-K 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQaEISRRILKSEPP---YP 279
Cdd:cd06644 163 TLQRRDSFIGTPYWMAPEVVmceTMKDTPYDYKADIWSLGITLIEMAQIEPPHH---ELNPM-RVLLKIAKSEPPtlsQP 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 32528297 280 QEMSALAKDLIQRLLMKDPKKRlgcgPrDADEIKEHLFFQKIN 322
Cdd:cd06644 239 SKWSMEFRDFLKTALDKHPETR----P-SAAQLLEHPFVSSVT 276
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
49-315 9.99e-31

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 120.26  E-value: 9.99e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRkisGHDTGKLYAMKVLKKATivqkaKTTEHTrtERQVLEH--IRQsPFLVTLHYAFQTETK 126
Cdd:cd14662   2 YELVKDIGSGNFGVARLMR---NKETKELVAVKYIERGL-----KIDENV--QREIINHrsLRH-PNIIRFKEVVLTPTH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSN--GHVVLTDFGLSKEFVA 204
Cdd:cd14662  71 LAIVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKSSVL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DetERAYSFCGTIEYMAPDIV-RGGDSGhdKAVDWWSLGVLMYELLTGASPFT-VDGEKNSQAEISrRILKSEPPYPQ-- 280
Cdd:cd14662 151 H--SQPKSTVGTPAYIAPEVLsRKEYDG--KVADVWSCGVTLYVMLVGAYPFEdPDDPKNFRKTIQ-RIMSVQYKIPDyv 225
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 281 EMSALAKDLIQRLLMKDPKKRLGCGprdadEIKEH 315
Cdd:cd14662 226 RVSQDCRHLLSRIFVANPAKRITIP-----EIKNH 255
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
432-547 1.03e-30

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 121.27  E-value: 1.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRmEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIK 511
Cdd:cd14178  11 IGIGSYSVCKRCVHKATSTEYAVKIIDKS-KRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELLDRIL 89
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 32528297 512 KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14178  90 RQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKP 125
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
48-301 1.66e-30

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 119.68  E-value: 1.66e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKIsghDTGKLYAmkvLKKATI--VQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTET 125
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCL---LDGRLVA---LKKVQIfeMMDAKARQDCLKEIDLLQQLNH-PNIIKYLASFIENN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGEL---FTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd08224  74 ELNIVLELADAGDLsrlIKHFKKQKRlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FvADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRILKSE-PPYPQ 280
Cdd:cd08224 154 F-SSKTTAAHSLVGTPYYMSPERIRE--QGYDFKSDIWSLGCLLYEMAALQSPFY--GEKMNLYSLCKKIEKCEyPPLPA 228
                       250       260
                ....*....|....*....|..
gi 32528297 281 EM-SALAKDLIQRLLMKDPKKR 301
Cdd:cd08224 229 DLySQELRDLVAACIQPDPEKR 250
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
49-317 1.96e-30

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 120.10  E-value: 1.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKkatIVQKAKttEHTRTERQVLEHIRQSPFLVTLHYAFQT----- 123
Cdd:cd06608   8 FELVEVIGEGTYGKVYKARHK---KTGQLAAIKIMD---IIEDEE--EEIKLEINILRKFSNHPNIATFYGAFIKkdppg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 -ETKLHLILDYINGGELfTHLSQR-----ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd06608  80 gDDQLWLVMEYCGGGSV-TDLVKGlrkkgKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEfVADETERAYSFCGTIEYMAPDIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgeknSQAEISR---RI 271
Cdd:cd06608 159 VSAQ-LDSTLGRRNTFIGTPYWMAPEVIacdQQPDASYDARCDVWSLGITAIELADGKPPL-------CDMHPMRalfKI 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 272 LKSEPP---YPQEMSALAKDLIQRLLMKDPKKRlgcgPrDADEIKEHLF 317
Cdd:cd06608 231 PRNPPPtlkSPEKWSKEFNDFISECLIKNYEQR----P-FTEELLEHPF 274
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
53-305 2.60e-30

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 119.44  E-value: 2.60e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVF--LVRKisghdTGKLYAMKVLKKATIvqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLI 130
Cdd:cd14082   9 EVLGSGQFGIVYggKHRK-----TGRDVAIKVIDKLRF--PTKQESQLRNEVAILQQLSH-PGVVNLECMFETPERVFVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG---HVVLTDFGLSKeFVADE 206
Cdd:cd14082  81 MEKLHGDMLEMILSSeKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFAR-IIGEK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAySFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgekNSQAEISRRILKSE---PPYP-QEM 282
Cdd:cd14082 160 SFRR-SVVGTPAYLAPEVLR--NKGYNRSLDMWSVGVIIYVSLSGTFPF------NEDEDINDQIQNAAfmyPPNPwKEI 230
                       250       260
                ....*....|....*....|...
gi 32528297 283 SALAKDLIQRLLMKDPKKRLGCG 305
Cdd:cd14082 231 SPDAIDLINNLLQVKMRKRYSVD 253
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
426-547 2.61e-30

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 120.12  E-value: 2.61e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKDKpLGEGSFSICRKCVHKKSNQAFAVKIISKRmEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd14177   7 ELKED-IGVGSYSVCKRCIHRATNMEFAVKIIDKS-KRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGE 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14177  85 LLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKP 126
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
47-302 2.79e-30

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 119.36  E-value: 2.79e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKK--ATIVQKAkttehTRTERQVLEHIRQsPFLVTLHYAFQTE 124
Cdd:cd14088   1 DRYDLGQVIKTEEFCEIFRAKDKT---TGKLYTCKKFLKrdGRKVRKA-----AKNEINILKMVKH-PNILQLVDVFETR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS---NGHVVLTDFGLSKE 201
Cdd:cd14088  72 KEYFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNrlkNSKIVISDFHLAKL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fvadETERAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGE----KNSQAEISRRILKS--- 274
Cdd:cd14088 152 ----ENGLIKEPCGTPEYLAPEVV--GRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEeddyENHDKNLFRKILAGdye 225
                       250       260
                ....*....|....*....|....*....
gi 32528297 275 -EPPYPQEMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14088 226 fDSPYWDDISQAAKDLVTRLMEVEQDQRI 254
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
53-318 5.12e-30

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 118.49  E-value: 5.12e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIV---QKAKTTEHTRTERQVlehirQSPFLVTLHYAFQTETKLHL 129
Cdd:cd14189   7 RLLGKGGFARCYEMTDLA---TNKTYAVKVIPHSRVAkphQREKIVNEIELHRDL-----HHKHVVKFSHHFEDAENIYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADEtER 209
Cdd:cd14189  79 FLELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPE-QR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 AYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKDL 289
Cdd:cd14189 158 KKTICGTPNYLAPEVLL--RQGHGPESDVWSLGCVMYTLLCGNPPF----ETLDLKETYRCIKQVKYTLPASLSLPARHL 231
                       250       260
                ....*....|....*....|....*....
gi 32528297 290 IQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14189 232 LAGILKRNPGDRL-----TLDQILEHEFF 255
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
49-318 6.09e-30

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 118.18  E-value: 6.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd06613   2 YELIQRIGSGTYGDVYKARNIA---TGELAAVKVIK----LEPGDDFEIIQQEISMLKECRH-PNIVAYFGSYLRRDKLW 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELfTHLSQRERFTEhEVQI-YVG-EIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd06613  74 IVMEYCGGGSL-QDIYQVTGPLS-ELQIaYVCrETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAySFCGTIEYMAPDIVRGGD-SGHDKAVDWWSLGVLMYELLTGASP-FTVDGEKNSQAeISRRILKsePPYPQEM-- 282
Cdd:cd06613 152 AKRK-SFIGTPYWMAPEVAAVERkGGYDGKCDIWALGITAIELAELQPPmFDLHPMRALFL-IPKSNFD--PPKLKDKek 227
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 283 -SALAKDLIQRLLMKDPKKRlgcgPrDADEIKEHLFF 318
Cdd:cd06613 228 wSPDFHDFIKKCLTKNPKKR----P-TATKLLQHPFV 259
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
47-301 6.66e-30

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 118.56  E-value: 6.66e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKAtivqKAKTTEHT-RTERQVLEHIRQsPFLVTLHYAFQTET 125
Cdd:cd14183   6 ERYKVGRTIGDGNFA---VVKECVERSTGREYALKIINKS----KCRGKEHMiQNEVSILRRVKH-PNIVLLIEEMDMPT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL----DSNGHVVLTDFGLSKe 201
Cdd:cd14183  78 ELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLAT- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fVADETerAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRILKSE----PP 277
Cdd:cd14183 157 -VVDGP--LYTVCGTPTYVAPEII--AETGYGLKVDIWAAGVITYILLCGFPPFR--GSGDDQEVLFDQILMGQvdfpSP 229
                       250       260
                ....*....|....*....|....
gi 32528297 278 YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14183 230 YWDNVSDSAKELITMMLQVDVDQR 253
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
49-315 1.09e-29

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 117.39  E-value: 1.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKakttehtRTERQVLEHIR-QSPFLVTLHYAFQTETKL 127
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRD---KQTKELVAVKYIERGEKIDE-------NVQREIINHRSlRHPNIVRFKEVILTPTHL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG--HVVLTDFGLSKEFVAD 205
Cdd:cd14665  72 AIVMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLH 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERaySFCGTIEYMAPDIVRGGDsgHD-KAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQ--EM 282
Cdd:cd14665 152 SQPK--STVGTPAYIAPEVLLKKE--YDgKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRILSVQYSIPDyvHI 227
                       250       260       270
                ....*....|....*....|....*....|...
gi 32528297 283 SALAKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14665 228 SPECRHLISRIFVADPATRI-----TIPEIRNH 255
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
55-302 1.16e-29

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 118.21  E-value: 1.16e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGkvfLVRKISGHDTGKLYAMKVLKKAtivqKAKTTEhtrtERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd14175   9 IGVGSYS---VCKRCVHKATNMEYAVKVIDKS----KRDPSE----EIEILLRYGQHPNIITLKDVYDDGKHVYLVTELM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL-LDSNGH---VVLTDFGLSKEFVADETeRA 210
Cdd:cd14175  78 RGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENG-LL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 YSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSQAEISRRILKSEPPYP----QEMSALA 286
Cdd:cd14175 157 MTPCYTANFVAPEVLK--RQGYDEGCDIWSLGILLYTMLAGYTPFA-NGPSDTPEEILTRIGSGKFTLSggnwNTVSDAA 233
                       250
                ....*....|....*.
gi 32528297 287 KDLIQRLLMKDPKKRL 302
Cdd:cd14175 234 KDLVSKMLHVDPHQRL 249
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
47-301 1.29e-29

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 117.93  E-value: 1.29e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatIVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTET- 125
Cdd:cd06620   5 QDLETLKDLGAGNGGSVSKVLHIP---TGTIMAKKVIH---IDAKSSVRKQILRELQILHEC-HSPYIVSFYGAFLNENn 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEhEVqiyVGEIVLA----LEHLH-KLGIIYRDIKLENILLDSNGHVVLTDFGLSK 200
Cdd:cd06620  78 NIIICMEYMDCGSLDKILKKKGPFPE-EV---LGKIAVAvlegLTYLYnVHRIIHRDIKPSNILVNSKGQIKLCDFGVSG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFVadeTERAYSFCGTIEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLTGASPFTV-DGEKNSQA------EISRRILK 273
Cdd:cd06620 154 ELI---NSIADTFVGTSTYMSPERIQGGKYSVKS--DVWSLGLSIIELALGEFPFAGsNDDDDGYNgpmgilDLLQRIVN 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 274 SEPP-------YPQEMsalaKDLIQRLLMKDPKKR 301
Cdd:cd06620 229 EPPPrlpkdriFPKDL----RDFVDRCLLKDPRER 259
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
52-301 1.29e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 117.14  E-value: 1.29e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKISGHdtgklyAMKVLKKatiVQKAKTTEhtRTERQVLEHIR-----QSPFLVTLHYAFQTETK 126
Cdd:cd08221   5 VRVLGRGAFGEAVLYRKTEDN------SLVVWKE---VNLSRLSE--KERRDALNEIDilsllNHDNIITYYNHFLDGES 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRER--FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVA 204
Cdd:cd08221  74 LFIEMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKV-LD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSE-PPYPQEMs 283
Cdd:cd08221 153 SESSMAESIVGTPYYMSPELVQG--VKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIdEQYSEEI- 229
                       250
                ....*....|....*...
gi 32528297 284 alaKDLIQRLLMKDPKKR 301
Cdd:cd08221 230 ---IQLVHDCLHQDPEDR 244
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
61-301 1.37e-29

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 116.98  E-value: 1.37e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  61 GKVFLVRKISGHDTGKLYAMKVLKKativqKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLHLILDYINGGELF 140
Cdd:cd14115   4 GRFSIVKKCLHKATRKDVAVKFVSK-----KMKKKEQAAHEAALLQHL-QHPQYITLHDTYESPTSYILVLELMDDGRLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 141 THLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD---SNGHVVLTDFGLSKEFVADetERAYSFCGTI 217
Cdd:cd14115  78 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGH--RHVHHLLGNP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 218 EYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKD 297
Cdd:cd14115 156 EFAAPEVIQG--TPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQED 233

                ....
gi 32528297 298 PKKR 301
Cdd:cd14115 234 PRRR 237
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
429-548 1.53e-29

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 116.97  E-value: 1.53e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSFSICRKCVHKKSNQAFAVKIISKR------MEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd14081   6 GKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEklskesVLMKVEREIAIMKLIE-HPNVLKLYDVYENKKYLYLVLEYVS 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14081  85 GGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPE 130
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
418-548 1.63e-29

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 117.07  E-value: 1.63e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 418 PFYQHYDLDlkDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK-----EITALKLCEGHPNIVKLHEVFHDQL 492
Cdd:cd14106   4 NINEVYTVE--STPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRneilhEIAVLELCKDCPRVVNLHEVYETRS 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 493 HTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14106  82 ELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQ 137
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
53-317 1.67e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 117.15  E-value: 1.67e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLK--KATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLI 130
Cdd:cd06630   6 PLLGTGAFSSCYQARDVK---TGTLMAVKQVSfcRNSSSEQEEVVEAIREEIRMMARLNH-PNIVRMLGATQHKSHFNIF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG-HVVLTDFGLSKEFVADET-- 207
Cdd:cd06630  82 VEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGTga 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 208 -ERAYSFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPP-YPQEMSAL 285
Cdd:cd06630 162 gEFQGQLLGTIAFMAPEVLRGEQYG--RSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPPpIPEHLSPG 239
                       250       260       270
                ....*....|....*....|....*....|..
gi 32528297 286 AKDLIQRLLMKDPKKRlgcgPRDADEIKEHLF 317
Cdd:cd06630 240 LRDVTLRCLELQPEDR----PPARELLKHPVF 267
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
48-302 2.90e-29

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 116.18  E-value: 2.90e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGhdtGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQS----PFLVTLHYAFQT 123
Cdd:cd14005   1 QYEVGDLLGKGGFGTVYSGVRIRD---GLPVAVKFVPKSRVTEWAMINGPVPVPLEIALLLKASkpgvPGVIRLLDWYER 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGE-LFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSN-GHVVLTDFGlSKE 201
Cdd:cd14005  78 PDGFLLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFG-CGA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVadeTERAYS-FCGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEknsqaeisrrILKSEPPYPQ 280
Cdd:cd14005 157 LL---KDSVYTdFDGTRVYSPPEWIRHG-RYHGRPATVWSLGILLYDMLCGDIPFENDEQ----------ILRGNVLFRP 222
                       250       260
                ....*....|....*....|..
gi 32528297 281 EMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14005 223 RLSKECCDLISRCLQFDPSKRP 244
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
49-318 2.96e-29

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 116.86  E-value: 2.96e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKkativQKAKTTEHTRTERQV--LEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARN---KETGELVAIKKMK-----KKFYSWEECMNLREVksLRKLNEHPNIVKLKEVFRENDE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGgELFTHLSQRER--FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd07830  73 LYFVFEYMEG-NLYQLMKDRKGkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYsfCGTIEYMAPDIV-RggDSGHDKAVDWWSLGVLMYELLT------GASP-------FTVDGEKNSQ------ 264
Cdd:cd07830 152 RPPYTDY--VSTRWYRAPEILlR--STSYSSPVDIWALGCIMAELYTlrplfpGSSEidqlykiCSVLGTPTKQdwpegy 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 265 ---AEISRRILKSEPPYPQEM----SALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07830 228 klaSKLGFRFPQFAPTSLHQLipnaSPEAIDLIKDMLRWDPKKRP-----TASQALQHPYF 283
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
49-315 3.55e-29

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 116.59  E-value: 3.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKATIVQ-------------KAKTTEHTRT----ER--------Q 103
Cdd:cd14200   2 YKLQSEIGKGSYG---VVKLAYNESDDKYYAMKVLSKKKLLKqygfprrppprgsKAAQGEQAKPlaplERvyqeiailK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 104 VLEHIRQSPFLVTLHYAfqTETKLHLILDYINGGELFTHLSQRErFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENI 183
Cdd:cd14200  79 KLDHVNIVKLIEVLDDP--AEDNLYMVFDLLRKGPVMEVPSDKP-FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 184 LLDSNGHVVLTDFGLSKEFVADETERAySFCGTIEYMAPD-IVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDgekn 262
Cdd:cd14200 156 LLGDDGHVKIADFGVSNQFEGNDALLS-STAGTPAFMAPEtLSDSGQSFSGKALDVWAMGVTLYCFVYGKCPFIDE---- 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 263 SQAEISRRIlKSEP---PYPQEMSALAKDLIQRLLMKDPKKRLGcgprdADEIKEH 315
Cdd:cd14200 231 FILALHNKI-KNKPvefPEEPEISEELKDLILKMLDKNPETRIT-----VPEIKVH 280
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
49-301 3.62e-29

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 116.14  E-value: 3.62e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVlkkatIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd14107   4 YEVKEEIGRGTFG---FVKRVTHKGNGECCAAKF-----IPLRSSTRARAFQERDILARLSH-RRLTCLLDQFETRKTLI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH--VVLTDFGLSKEFvaDE 206
Cdd:cd14107  75 LILELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQEI--TP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALA 286
Cdd:cd14107 153 SEHQFSKYGSPEFVAPEIVH--QEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSEDA 230
                       250
                ....*....|....*
gi 32528297 287 KDLIQRLLMKDPKKR 301
Cdd:cd14107 231 KDFIKRVLQPDPEKR 245
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
47-302 4.53e-29

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 116.65  E-value: 4.53e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKAtivqKAKTTEhtrtERQVLEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd14178   3 DGYEIKEDIGIGSYS---VCKRCVHKATSTEYAVKIIDKS----KRDPSE----EIEILLRYGQHPNIITLKDVYDDGKF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL-LDSNGH---VVLTDFGLSKEF 202
Cdd:cd14178  72 VYLVMELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VAdETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSQAEISRRILKSEPPYP--- 279
Cdd:cd14178 152 RA-ENGLLMTPCYTANFVAPEVLK--RQGYDAACDIWSLGILLYTMLAGFTPFA-NGPDDTPEEILARIGSGKYALSggn 227
                       250       260
                ....*....|....*....|....
gi 32528297 280 -QEMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14178 228 wDSISDAAKDIVSKMLHVDPHQRL 251
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
55-318 5.19e-29

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 115.65  E-value: 5.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVflvRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRtERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd14165   9 LGEGSYAKV---KSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPR-ELEILARLNHKSIIKTYEIFETSDGKVYIVMELG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETER---AY 211
Cdd:cd14165  85 VQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRivlSK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQE--MSALAKDL 289
Cdd:cd14165 165 TFCGSAAYAAPEVLQ-GIPYDPRIYDIWSLGVILYIMVCGSMPY----DDSNVKKMLKIQKEHRVRFPRSknLTSECKDL 239
                       250       260
                ....*....|....*....|....*....
gi 32528297 290 IQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14165 240 IYRLLQPDVSQRL-----CIDEVLSHPWL 263
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
53-302 5.59e-29

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 115.44  E-value: 5.59e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQSPfLVTLHYAFQTETKLHLILD 132
Cdd:cd14192  10 EVLGGGRFGQVHKCTELS---TGLTLAAKIIK----VKGAKEREEVKNEINIMNQLNHVN-LIQLYDAFESKTNLTLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLS-QRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL-LDSNGHVV-LTDFGLSKEFVADETER 209
Cdd:cd14192  82 YVDGGELFDRITdESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNQIkIIDFGLARRYKPREKLK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 AySFcGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPYPQE----MSAL 285
Cdd:cd14192 162 V-NF-GTPEFLAPEVVNYDFVSF--PTDMWSVGVITYMLLSGLSPFLGE----TDAETMNNIVNCKWDFDAEafenLSEE 233
                       250
                ....*....|....*..
gi 32528297 286 AKDLIQRLLMKDPKKRL 302
Cdd:cd14192 234 AKDFISRLLVKEKSCRM 250
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
47-301 5.70e-29

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 116.28  E-value: 5.70e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATivqkAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd06643   5 DFWEIVGELGDGAFGKVY---KAQNKETGILAAAKVIDTKS----EEELEDYMVEIDILASCDH-PNIVKLLDAFYYENN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSkefvAD 205
Cdd:cd06643  77 LWILIEFCAGGAVDAVMLELERpLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVS----AK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ET---ERAYSFCGTIEYMAPDIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPftvDGEKNSQaEISRRILKSEPP-- 277
Cdd:cd06643 153 NTrtlQRRDSFIGTPYWMAPEVVmceTSKDRPYDYKADVWSLGVTLIEMAQIEPP---HHELNPM-RVLLKIAKSEPPtl 228
                       250       260
                ....*....|....*....|....*
gi 32528297 278 -YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd06643 229 aQPSRWSPEFKDFLRKCLEKNVDAR 253
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
53-302 5.81e-29

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 116.67  E-value: 5.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATivqkakttehtRTERQVLEHIR--QSPFLVTL----HYAFQTETK 126
Cdd:cd14170   8 QVLGLGINGKVL---QIFNKRTQEKFALKMLQDCP-----------KARREVELHWRasQCPHIVRIvdvyENLYAGRKC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQR--ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS---NGHVVLTDFGLSKE 201
Cdd:cd14170  74 LLIVMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETerAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQ- 280
Cdd:cd14170 154 TTSHNS--LTTPCYTPYYVAPEVL--GPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNp 229
                       250       260
                ....*....|....*....|....*
gi 32528297 281 ---EMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14170 230 ewsEVSEEVKMLIRNLLKTEPTQRM 254
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
432-548 7.45e-29

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 114.67  E-value: 7.45e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRME--ANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFER 509
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKkkEAVLREISILNQLQ-HPRIIQLHEAYESPTELVLILELCSGGELLDR 79
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 510 IKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14006  80 LAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPE 118
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
49-318 9.19e-29

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 115.27  E-value: 9.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKativqkaktteHTRTE-------RQV-----LEHirqsPFLVT 116
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDK---KTGEIVALKKIRL-----------DNEEEgipstalREIsllkeLKH----PNIVK 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 117 LHYAFQTETKLHLILDYINGgELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTD 195
Cdd:cd07829  63 LLDVIHTENKLYLVFEYCDQ-DLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLAD 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 196 FGLSKEFVadETERAYsfcgTIE-----YMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISrR 270
Cdd:cd07829 142 FGLARAFG--IPLRTY----THEvvtlwYRAPEILL-GSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIF-Q 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 271 IL----------------------KSEPPYPQE----MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07829 214 ILgtpteeswpgvtklpdykptfpKWPKNDLEKvlprLDPEGIDLLSKMLQYNPAKRI-----SAKEALKHPYF 282
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
432-547 1.08e-28

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 116.66  E-value: 1.08e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQkEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIK 511
Cdd:cd14176  27 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKIL 105
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 32528297 512 KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14176 106 RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKP 141
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
53-305 1.24e-28

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 114.63  E-value: 1.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVflvRKISGHDTGKLYAMKVLKKativQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILD 132
Cdd:cd14190  10 EVLGGGKFGKV---HTCTEKRTGLKLAAKVINK----QNSKDKEMVLLEIQVMNQLNH-RNLIQLYEAIETPNEIVLFME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL-DSNGHVV-LTDFGLSKEFVADETER 209
Cdd:cd14190  82 YVEGGELFERIvDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHQVkIIDFGLARRYNPREKLK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 AySFcGTIEYMAPDIVrGGDSGHDKAvDWWSLGVLMYELLTGASPFTVDGEknsqAEISRRILKSEPPYPQE----MSAL 285
Cdd:cd14190 162 V-NF-GTPEFLSPEVV-NYDQVSFPT-DMWSMGVITYMLLSGLSPFLGDDD----TETLNNVLMGNWYFDEEtfehVSDE 233
                       250       260
                ....*....|....*....|
gi 32528297 286 AKDLIQRLLMKDPKKRLGCG 305
Cdd:cd14190 234 AKDFVSNLIIKERSARMSAT 253
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
47-302 1.86e-28

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 114.95  E-value: 1.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKATIVQKAK-TTEHTRTERQVLeHIRQSPFLVTLHYAFQTET 125
Cdd:cd14094   3 DVYELCEVIGKGPFS---VVRRCIHRETGQQFAVKIVDVAKFTSSPGlSTEDLKREASIC-HMLKHPHIVELLETYSSDG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRER----FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL---DSNGHVVLTDFGL 198
Cdd:cd14094  79 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKEfVADETERAYSFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAeISRRILKSEPPY 278
Cdd:cd14094 159 AIQ-LGESGLVAGGRVGTPHFMAPEVVKREPYG--KPVDVWGCGVILFILLSGCLPFYGTKERLFEG-IIKGKYKMNPRQ 234
                       250       260
                ....*....|....*....|....
gi 32528297 279 PQEMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14094 235 WSHISESAKDLVRRMLMLDPAERI 258
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
419-548 1.98e-28

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 114.68  E-value: 1.98e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 419 FYQHYDldlKDKPLGEGSFSICRKCVHKKSNQAFAVKIIS-----------KRMEANTQKEITALKLCEGHPNIVKLHEV 487
Cdd:cd14181   8 FYQKYD---PKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlspeqlEEVRSSTLKEIHILRQVSGHPSIITLIDS 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 488 FHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14181  85 YESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPE 145
Pkinase pfam00069
Protein kinase domain;
428-532 3.23e-28

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 111.95  E-value: 3.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIISKR-----MEANTQKEITALKLCeGHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:pfam00069   3 VLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEkikkkKDKNILREIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEYVE 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 32528297   503 GGELFERIKKKKHFSETEASYIMRKLVSAV 532
Cdd:pfam00069  82 GGSLFDLLSEKGAFSEREAKFIMKQILEGL 111
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
429-548 3.86e-28

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 114.15  E-value: 3.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd14085   8 ESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFD 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 509 RIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14085  88 RIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPE 127
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
47-301 3.93e-28

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 113.15  E-value: 3.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKV----LGTGAYGkvfLVRKISGHDTGKLYAMKVLKKAtiVQKAKTTEHTRTERQVLEHirqsPFLVTLHYAFQ 122
Cdd:cd14113   3 DNFDSFYSevaeLGRGRFS---VVKKCDQRGTKRAVATKFVNKK--LMKRDQVTHELGVLQSLQH----PQLVGLLDTFE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD---SNGHVVLTDFGLS 199
Cdd:cd14113  74 TPTSYILVLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDqslSKPTIKLADFGDA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KEFvaDETERAYSFCGTIEYMAPDIVRGGDSghDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYP 279
Cdd:cd14113 154 VQL--NTTYYIHQLLGSPEFAAPEIILGNPV--SLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYF 229
                       250       260
                ....*....|....*....|..
gi 32528297 280 QEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14113 230 KGVSQKAKDFVCFLLQMDPAKR 251
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
55-316 4.09e-28

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 113.19  E-value: 4.09e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVR-KISGHdtgkLYAMKVLKKATIVQKAKTTEHTRTErqvleHIRQSPFLV-TLHYAFQTETKLHLILD 132
Cdd:cd13987   1 LGEGTYGKVLLAVhKGSGT----KMALKFVPKPSTKLKDFLREYNISL-----ELSVHPHIIkTYDVAFETEDYYVFAQE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL-DSN-GHVVLTDFGLSkeFVADETERA 210
Cdd:cd13987  72 YAPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLT--RRVGSTVKR 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 YSfcGTIEYMAP---DIVRGGDSGHDKAVDWWSLGVLMYELLTGASPF-TVDGEKNSQAEISR---RILKSEPPYPQEMS 283
Cdd:cd13987 150 VS--GTIPYTAPevcEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWeKADSDDQFYEEFVRwqkRKNTAVPSQWRRFT 227
                       250       260       270
                ....*....|....*....|....*....|...
gi 32528297 284 ALAKDLIQRLLMKDPKKRlgCGPrdaDEIKEHL 316
Cdd:cd13987 228 PKALRMFKKLLAPEPERR--CSI---KEVFKYL 255
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
49-319 4.10e-28

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 113.18  E-value: 4.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGHDTGklYAMKVLKKATIvqkAKTTEHTRTERQVLEHIRQSPfLVTLhYAFQT-ETKL 127
Cdd:cd14202   4 FSRKDLIGHGAFAVVFKGRHKEKHDLE--VAVKCINKKNL---AKSQTLLGKEIKILKELKHEN-IVAL-YDFQEiANSV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG---------HVVLTDFGL 198
Cdd:cd14202  77 YLVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKEFVADETerAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQA--EISRRILkseP 276
Cdd:cd14202 157 ARYLQNNMM--AATLCGSPMYMAPEVIM--SQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLfyEKNKSLS---P 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 32528297 277 PYPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd14202 230 NIPRETSSHLRQLLLGLLQRNQKDRM-----DFDEFFHHPFLD 267
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
54-317 4.18e-28

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 113.40  E-value: 4.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATI-----VQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLH 128
Cdd:cd06628   7 LIGSGSFGSVYLGMNAS---SGELMAVKQVELPSVsaenkDRKKSMLDALQREIALLREL-QHENIVQYLGSSSDANHLN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETE 208
Cdd:cd06628  83 IFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAY-----SFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISRRILKSEPPYPQEMS 283
Cdd:cd06628 163 TKNngarpSLQGSVFWMAPEVVK--QTSYTRKADIWSLGCLVVEMLTGTHPFP---DCTQMQAIFKIGENASPTIPSNIS 237
                       250       260       270
                ....*....|....*....|....*....|....
gi 32528297 284 ALAKDLIQRLLMKDPKKRlgcgPrDADEIKEHLF 317
Cdd:cd06628 238 SEARDFLEKTFEIDHNKR----P-TADELLKHPF 266
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
430-546 5.11e-28

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 112.65  E-value: 5.11e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK------RMEANTQKEIT---ALKlcegHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd14099   7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKssltkpKQREKLKSEIKihrSLK----HPNIVKFHDCFEDEENVYILLEL 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd14099  83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLK 128
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
47-317 1.25e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 113.77  E-value: 1.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   47 ENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVL----KKATIVQKAKTTEHTRTerqvLEHirqsPFLVTLHYAFQ 122
Cdd:PLN00034  74 SELERVNRIGSGAGGTVYKVIH---RPTGRLYALKVIygnhEDTVRRQICREIEILRD----VNH----PNVVKCHDMFD 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  123 TETKLHLILDYINGGEL-FTHLSQRERFTEHEVQIYVGeivlaLEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKe 201
Cdd:PLN00034 143 HNGEIQVLLEFMDGGSLeGTHIADEQFLADVARQILSG-----IAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSR- 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  202 FVADETERAYSFCGTIEYMAP-----DIVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVdGEKNSQAEISRRILKSEP 276
Cdd:PLN00034 217 ILAQTMDPCNSSVGTIAYMSPerintDLNHGAYDGY--AGDIWSLGVSILEFYLGRFPFGV-GRQGDWASLMCAICMSQP 293
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 32528297  277 PY-PQEMSALAKDLIQRLLMKDPKKRlgcgpRDADEIKEHLF 317
Cdd:PLN00034 294 PEaPATASREFRHFISCCLQREPAKR-----WSAMQLLQHPF 330
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
427-548 1.31e-27

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 112.43  E-value: 1.31e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKR---MEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14173   5 LQEEVLGEGAYARVQTCINLITNKEYAVKIIEKRpghSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14173  85 GSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPE 129
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
48-301 2.06e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 110.98  E-value: 2.06e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKisghdtgklyamKVLKKATIVQKAKTTEHTRTERQ----------VLEHirqsPFLVTL 117
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRR------------KDDNKLVIIKQIPVEQMTKEERQaalnevkvlsMLHH----PNIIEY 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 118 HYAFQTETKLHLILDYINGGELFTHLSQR--ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV-LT 194
Cdd:cd08220  65 YESFLEDKALMIVMEYAPGGTLFEYIQQRkgSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVkIG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 195 DFGLSKEFVAdeTERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKS 274
Cdd:cd08220 145 DFGISKILSS--KSKAYTVVGTPCYISPELCEG--KPYNQKSDIWALGCVLYELASLKRAF----EAANLPALVLKIMRG 216
                       250       260
                ....*....|....*....|....*...
gi 32528297 275 E-PPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd08220 217 TfAPISDRYSEELRHLILSMLHLDPNKR 244
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
422-548 2.14e-27

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 110.82  E-value: 2.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKR------MEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTF 495
Cdd:cd14079   3 NYILG---KTLGVGSFGKVKLAEHELTGHKVAVKILNRQkiksldMEEKIRREIQILKLFR-HPHIIRLYEVIETPTDIF 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 496 LVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14079  79 MVMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPE 131
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
423-548 2.24e-27

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 111.78  E-value: 2.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 423 YDLDLKDKpLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTqkEITALKLCEGHPNIVKLHEVF----------HDQL 492
Cdd:cd14171   6 YEVNWTQK-LGTGISGPVRVCVKKSTGERFALKILLDRPKART--EVRLHMMCSGHPNIVQIYDVYansvqfpgesSPRA 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 493 HTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14171  83 RLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPE 138
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
53-317 2.49e-27

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 110.93  E-value: 2.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKIsghDTGKLYAMK-VLKKATIVQKAKTTEHT-----RTERQVLEHIRQSPFLVTLHYAfQTETK 126
Cdd:cd06629   7 ELIGKGTYGRVYLAMNA---TTGEMLAVKqVELPKTSSDRADSRQKTvvdalKSEIDTLKDLDHPNIVQYLGFE-ETEDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfvADE 206
Cdd:cd06629  83 FSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKK--SDD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 ---TERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRriLKSEPPYPQE-- 281
Cdd:cd06629 161 iygNNGATSMQGSVFWMAPEVIHSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGN--KRSAPPVPEDvn 238
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32528297 282 MSALAKDLIQRLLMKDPKKRlgcgPRdADEIKEHLF 317
Cdd:cd06629 239 LSPEALDFLNACFAIDPRDR----PT-AAELLSHPF 269
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
432-548 3.81e-27

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 110.34  E-value: 3.81e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR-----------------MEANTQKEITALKLCEgHPNIVKLHEVFHD--QL 492
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSrlrkrregkndrgkiknALDDVRREIAIMKKLD-HPNIVRLYEVIDDpeSD 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32528297 493 HTFLVMELLNGGELFERIKKKKH--FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14008  80 KLYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPE 137
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
47-301 4.45e-27

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 110.98  E-value: 4.45e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVflvRKISGHDTGKLYAMKVLKkativqkakTTEHTRTERQVLEHIR-----QSPFLVTLHYAF 121
Cdd:cd06621   1 DKIVELSSLGEGAGGSV---TKCRLRNTKTIFALKTIT---------TDPNPDVQKQILRELEinkscASPYIVKYYGAF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 --QTETKLHLILDYINGGELFT----HLSQRERFTEHeVQIYVGEIVL-ALEHLHKLGIIYRDIKLENILLDSNGHVVLT 194
Cdd:cd06621  69 ldEQDSSIGIAMEYCEGGSLDSiykkVKKKGGRIGEK-VLGKIAESVLkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLC 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 195 DFGLSKEFVadeTERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQ--------AE 266
Cdd:cd06621 148 DFGVSGELV---NSLAGTFTGTSYYMAPERIQGGP--YSITSDVWSLGLTLLEVAQNRFPFPPEGEPPLGpiellsyiVN 222
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 267 ISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd06621 223 MPNPELKDEPENGIKWSESFKDFIEKCLEKDGTRR 257
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
426-548 4.78e-27

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 110.37  E-value: 4.78e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKDKpLGEGSFSICRKCVHKKSNQAFAVKIISKRM----EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd14169   6 ELKEK-LGEGAFSEVVLAQERGSQRLVALKCIPKKAlrgkEAMVENEIAVLRRIN-HENIVSLEDIYESPTHLYLAMELV 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14169  84 TGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPE 130
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
47-318 5.21e-27

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 109.84  E-value: 5.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd06648   7 SDLDNFVKIGEGSTGIVCIATDKS---TGRQVAVKKMD----LRKQQRRELLFNEVVIMRDY-QHPNIVEMYSSYLVGDE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVADE 206
Cdd:cd06648  79 LWVVMEFLEGGAL-TDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQ-VSKE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPY---PQEMS 283
Cdd:cd06648 157 VPRRKSLVGTPYWMAPEVI--SRLPYGTEVDIWSLGIMVIEMVDGEPPYFNE----PPLQAMKRIRDNEPPKlknLHKVS 230
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 284 ALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd06648 231 PRLRSFLDRMLVRDPAQRA-----TAAELLNHPFL 260
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
430-548 6.48e-27

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 110.18  E-value: 6.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK-----------EITALKLCEgHPNIVKLHEVFHDQLHTFLVM 498
Cdd:cd14084  12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRreinkprnietEIEILKKLS-HPCIIKIEDFFDAEDDYYIVL 90
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 499 ELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14084  91 ELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPE 140
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
432-548 9.05e-27

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 110.08  E-value: 9.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR---MEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd14166  11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSplsRDSSLENEIAVLKRIK-HENIVTLEDIYESTTHYYLVMQLVSGGELFD 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 509 RIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14166  90 RILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPE 129
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
49-318 1.22e-26

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 109.58  E-value: 1.22e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKkativqkaktTEHTRT--------ERQVLEHIRQsPFLVTLH-- 118
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNK---KTGELVALKKIR----------MENEKEgfpitairEIKLLQKLDH-PNVVRLKei 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 119 ----YAFQTETKLHLILDYinggelFTH-----LSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSN 188
Cdd:cd07840  67 vtskGSAKYKGSIYMVFEY------MDHdltglLDNPEvKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINND 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 189 GHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEIS 268
Cdd:cd07840 141 GVLKLADFGLARPYTKENNADYTNRVITLWYRPPELLL-GATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIF 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 269 R-------------------RILKSEPPYP--------QEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07840 220 ElcgspteenwpgvsdlpwfENLKPKKPYKrrlrevfkNVIDPSALDLLDKLLTLDPKKRI-----SADQALQHEYF 291
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
50-301 1.31e-26

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 108.76  E-value: 1.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  50 ELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVL-----KKATIVQKAKTTEHTRTERqvlehirqspfLVTLHYAFQTE 124
Cdd:cd14111   3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVpyqaeEKQGVLQEYEILKSLHHER-----------IMALHEAYITP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd14111  72 RYLVLIAEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQeMSA 284
Cdd:cd14111 152 LSLRQLGRRTGTLEYMAPEMVKGEPVG--PPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAFKLYPN-VSQ 228
                       250
                ....*....|....*..
gi 32528297 285 LAKDLIQRLLMKDPKKR 301
Cdd:cd14111 229 SASLFLKKVLSSYPWSR 245
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
47-301 1.58e-26

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 109.33  E-value: 1.58e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATIVQkakttEHTRTERQVLEHIRQSPFLVTLHYAF----- 121
Cdd:cd06638  18 DTWEIIETIGKGTYGKVF---KVLNKKNGSKAAVKILDPIHDID-----EEIEAEYNILKALSDHPNVVKFYGMYykkdv 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFT----HLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd06638  90 KNGDQLWLVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEFVADETERAYSfCGTIEYMAPDIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRrilkS 274
Cdd:cd06638 170 VSAQLTSTRLRRNTS-VGTPFWMAPEVIaceQQLDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPR----N 244
                       250       260       270
                ....*....|....*....|....*....|
gi 32528297 275 EPP---YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd06638 245 PPPtlhQPELWSNEFNDFIRKCLTKDYEKR 274
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
432-548 1.98e-26

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 108.19  E-value: 1.98e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISK-RMEANTQK----EITALKlCEGHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd14075  10 LGSGNFSQVKLGIHQLTKEKVAIKILDKtKLDQKTQRllsrEISSME-KLHHPNIIRLYEVVETLSKLHLVMEYASGGEL 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14075  89 YTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAE 130
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
49-301 2.02e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 108.28  E-value: 2.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGHDTGKLyamKVLKKATI--VQKAKTTEHTRtERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSDLKATADEEL---KVLKEISVgeLQPDETVDANR-EAKLLSKL-DHPAIVKFHDSFVEKES 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQ----RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLdSNGHVVLTDFGLSKeF 202
Cdd:cd08222  77 FCIVTEYCEGGDLDDKISEykksGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISR-I 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSE-PPYPQE 281
Cdd:cd08222 155 LMGTSDLATTFTGTPYYMSPEVLKH--EGYNSKSDIWSLGCILYEMCCLKHAF----DGQNLLSVMYKIVEGEtPSLPDK 228
                       250       260
                ....*....|....*....|
gi 32528297 282 MSALAKDLIQRLLMKDPKKR 301
Cdd:cd08222 229 YSKELNAIYSRMLNKDPALR 248
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
432-548 2.44e-26

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 108.19  E-value: 2.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM----EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELF 507
Cdd:cd14167  11 LGTGAFSEVVLAEEKRTQKLVAIKCIAKKAlegkETSIENEIAVLHKIK-HPNIVALDDIYESGGHLYLIMQLVSGGELF 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 508 ERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14167  90 DRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPE 130
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
427-548 2.45e-26

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 108.96  E-value: 2.45e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRM---EANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14174   5 LTDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAghsRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14174  85 GSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPE 129
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
55-302 3.91e-26

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 107.45  E-value: 3.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISGHDtgKLYAMKVLKKATIvqkAKTTEHTRTERQVLEHIRQSPfLVTLHYAFQTETKLHLILDYI 134
Cdd:cd14120   1 IGHGAFAVVFKGRHRKKPD--LPVAIKCITKKNL---SKSQNLLGKEIKILKELSHEN-VVALLDCQETSSSVYLVMEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG---------HVVLTDFGLSKeFVAD 205
Cdd:cd14120  75 NGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFAR-FLQD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETeRAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSE---PPYPQEM 282
Cdd:cd14120 154 GM-MAATLCGSPMYMAPEVIMS--LQYDAKADLWSIGTIVYQCLTGKAPF----QAQTPQELKAFYEKNAnlrPNIPSGT 226
                       250       260
                ....*....|....*....|
gi 32528297 283 SALAKDLIQRLLMKDPKKRL 302
Cdd:cd14120 227 SPALKDLLLGLLKRNPKDRI 246
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
48-302 3.92e-26

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 107.31  E-value: 3.92e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVflvRKISGHDTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQSPfLVTLHYAFQTETKL 127
Cdd:cd14193   5 NVNKEEILGGGRFGQV---HKCEEKSSGLKLAAKIIK----ARSQKEKEEVKNEIEVMNQLNHAN-LIQLYDAFESRNDI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSN--GHVVLTDFGLSKEFVA 204
Cdd:cd14193  77 VLVMEYVDGGELFDRIiDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSReaNQVKIIDFGLARRYKP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSfcGTIEYMAPDIVrggdsGHDKA---VDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQE 281
Cdd:cd14193 157 REKLRVNF--GTPEFLAPEVV-----NYEFVsfpTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFAD 229
                       250       260
                ....*....|....*....|.
gi 32528297 282 MSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14193 230 ISEEAKDFISKLLIKEKSWRM 250
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
419-548 4.92e-26

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 107.69  E-value: 4.92e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 419 FYQHYDldlKDKPLGEGSFSICRKCVHKKSNQAFAVKIIS------------KRMEANTQKEITALKLCEGHPNIVKLHE 486
Cdd:cd14182   1 FYEKYE---PKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgggsfspeevQELREATLKEIDILRKVSGHPNIIQLKD 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 487 VFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14182  78 TYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPE 139
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
432-548 5.56e-26

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 107.74  E-value: 5.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR----MEANTQKEITALKLCEGHPNIVKLHEVFHDQLH--TFLVMELLNGgE 505
Cdd:cd07831   7 IGEGTFSEVLKAQSRKTGKYYAIKCMKKHfkslEQVNNLREIQALRRLSPHPNILRLIEVLFDRKTgrLALVFELMDM-N 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 506 LFERIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07831  86 LYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPE 129
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
151-301 6.40e-26

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 107.11  E-value: 6.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 151 EHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS-NGHVVLTDFGLSKEfVADETERAYSFCGTIEYMAPDIVRGGD 229
Cdd:cd06624 107 ENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKR-LAGINPCTETFTGTLQYMAPEVIDKGQ 185
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 230 SGHDKAVDWWSLGVLMYELLTGASPFTVDGEknSQAEISR-RILKSEPPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd06624 186 RGYGPPADIWSLGCTIIEMATGKPPFIELGE--PQAAMFKvGMFKIHPEIPESLSEEAKSFILRCFEPDPDKR 256
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
49-326 8.32e-26

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 107.20  E-value: 8.32e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRkisGHDTGKLYAmkvLKKATIVQKAKTtehtRtERQVLEHIRqSPFLVTLHYAFQT----- 123
Cdd:cd14137   6 YTIEKVIGSGSFGVVYQAK---LLETGEVVA---IKKVLQDKRYKN----R-ELQIMRRLK-HPNIVKLKYFFYSsgekk 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 -ETKLHLILDYI--NGGELFTHLS-QRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD-SNGHVVLTDFGL 198
Cdd:cd14137  74 dEVYLNLVMEYMpeTLYRVIRHYSkNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFGS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKEFVADETERAYsFCgTIEYMAPD-IVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQ--AEI-------S 268
Cdd:cd14137 154 AKRLVPGEPNVSY-IC-SRYYRAPElIF--GATDYTTAIDIWSAGCVLAELLLGQPLFP--GESSVDqlVEIikvlgtpT 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 269 RRILKS------EPPYPQ------------EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFqkinwDDL 326
Cdd:cd14137 228 REQIKAmnpnytEFKFPQikphpwekvfpkRTPPDAIDLLSKILVYNPSKRL-----TALEALAHPFF-----DEL 293
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
49-301 1.10e-25

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 105.98  E-value: 1.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGhdtGKLYAMKVLKkatiVQKAKTTEH--TRTERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd08223   2 YQFLRVIGKGSYGEVWLVRHKRD---RKQYVIKKLN----LKNASKRERkaAEQEAKLLSKLKH-PNIVSYKESFEGEDG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 -LHLILDYINGGELFTHLSQR--ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKeFV 203
Cdd:cd08223  74 fLYIVMGFCEGGDLYTRLKEQkgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIAR-VL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCGTIEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLTGASPFTVDgEKNSqaeISRRILKSE-PPYPQEM 282
Cdd:cd08223 153 ESSSDMATTLIGTPYYMSPELFSNKPYNHKS--DVWALGCCVYEMATLKHAFNAK-DMNS---LVYKILEGKlPPMPKQY 226
                       250
                ....*....|....*....
gi 32528297 283 SALAKDLIQRLLMKDPKKR 301
Cdd:cd08223 227 SPELGELIKAMLHQDPEKR 245
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
441-548 1.60e-25

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 105.83  E-value: 1.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 441 RKCVHKKSNQAFAVKIISKRMEANTQKEITALklCEGHPNIVKLHEVF----HDQLHTFLVMELLNGGELFERIKKK--K 514
Cdd:cd14089  18 LECFHKKTGEKFALKVLRDNPKARREVELHWR--ASGCPHIVRIIDVYentyQGRKCLLVVMECMEGGELFSRIQERadS 95
                        90       100       110
                ....*....|....*....|....*....|....
gi 32528297 515 HFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14089  96 AFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPE 129
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
47-304 1.83e-25

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 105.49  E-value: 1.83e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKATIVQK-AKTTEHTRTERQVLEHIRQSPfLVTLHYAFQ--T 123
Cdd:cd06653   2 VNWRLGKLLGRGAFGEVYLCYDA---DTGRELAVKQVPFDPDSQEtSKEVNALECEIQLLKNLRHDR-IVQYYGCLRdpE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK--E 201
Cdd:cd06653  78 EKKLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKriQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISRRILK-SEPPYPQ 280
Cdd:cd06653 158 TICMSGTGIKSVTGTPYWMSPEVISG--EGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKIATQpTKPQLPD 232
                       250       260
                ....*....|....*....|....
gi 32528297 281 EMSALAKDLIQRLLMKDPKKRLGC 304
Cdd:cd06653 233 GVSDACRDFLRQIFVEEKRRPTAE 256
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
55-306 1.95e-25

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 106.38  E-value: 1.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATiVQKAKTTEHTRTERQVLEHIRQ----SPFLVTLHYAFQTETKLHLI 130
Cdd:cd13989   1 LGSGGFGYVTLWKH---QDTGEYVAIKKCRQEL-SPSDKNRERWCLEVQIMKKLNHpnvvSARDVPPELEKLSPNDLPLL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 -LDYINGGELFTHLSQRERFT---EHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL-DSNGHVV--LTDFGLSKEFv 203
Cdd:cd13989  77 aMEYCSGGDLRKVLNQPENCCglkESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqQGGGRVIykLIDLGYAKEL- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 aDETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFT-----------VDGEKNSQ---AEISR 269
Cdd:cd13989 156 -DQGSLCTSFVGTLQYLAPELFE--SKKYTCTVDYWSFGTLAFECITGYRPFLpnwqpvqwhgkVKQKKPEHicaYEDLT 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 32528297 270 RILK--SEPPYPQEMSALAKDLIQR----LLMKDPKKRLGCGP 306
Cdd:cd13989 233 GEVKfsSELPSPNHLSSILKEYLESwlqlMLRWDPRQRGGGPQ 275
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
430-548 2.05e-25

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 106.08  E-value: 2.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRM----EANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGgE 505
Cdd:cd07830   5 KQLGDGTFGSVYLARNKETGELVAIKKMKKKFysweECMNLREVKSLRKLNEHPNIVKLKEVFRENDELYFVFEYMEG-N 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 506 LFERIK--KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07830  84 LYQLMKdrKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPE 128
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
422-548 2.60e-25

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 105.03  E-value: 2.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRM----EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd14185   1 HYEIG---RTIGDGNFAVVKECRHWNENQEYAMKIIDKSKlkgkEDMIESEILIIKSLS-HPNIVKLFEVYETEKEIYLI 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14185  77 LEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPE 127
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
47-301 2.66e-25

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 105.87  E-value: 2.66e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKAtivqKAKTTEhtrtERQVLEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd14177   4 DVYELKEDIGVGSYS---VCKRCIHRATNMEFAVKIIDKS----KRDPSE----EIEILMRYGQHPNIITLKDVYDDGRY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL-LDSNGH---VVLTDFGLSKEF 202
Cdd:cd14177  73 VYLVTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETeRAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSQAEISRRILKSEPPYP--- 279
Cdd:cd14177 153 RGENG-LLLTPCYTANFVAPEVLM--RQGYDAACDIWSLGVLLYTMLAGYTPFA-NGPNDTPEEILLRIGSGKFSLSggn 228
                       250       260
                ....*....|....*....|...
gi 32528297 280 -QEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14177 229 wDTVSDAAKDLLSHMLHVDPHQR 251
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
46-301 2.76e-25

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 105.11  E-value: 2.76e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAmkvLKKATIVQ--KAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQT 123
Cdd:cd08228   1 LANFQIEKKIGRGQFSEVY---RATCLLDRKPVA---LKKVQIFEmmDAKARQDCVKEIDLLKQLNH-PNVIKYLDSFIE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGEL---FTHLSQRERFT-EHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd08228  74 DNELNIVLELADAGDLsqmIKYFKKQKRLIpERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KeFVADETERAYSFCGTIEYMAPDivRGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRILKSE-PPY 278
Cdd:cd08228 154 R-FFSSKTTAAHSLVGTPYYMSPE--RIHENGYNFKSDIWSLGCLLYEMAALQSPFY--GDKMNLFSLCQKIEQCDyPPL 228
                       250       260
                ....*....|....*....|....
gi 32528297 279 PQE-MSALAKDLIQRLLMKDPKKR 301
Cdd:cd08228 229 PTEhYSEKLRELVSMCIYPDPDQR 252
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
47-301 3.34e-25

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 105.46  E-value: 3.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATIVQkakttEHTRTERQVLEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd06639  22 DTWDIIETIGKGTYGKVY---KVTNKKDGSLAAVKILDPISDVD-----EEIEAEYNILRSLPNHPNVVKFYGMFYKADQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 -----LHLILDYINGG---ELFTHLSQR-ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd06639  94 yvggqLWLVLELCNGGsvtELVKGLLKCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEFVADETERAYSfCGTIEYMAPDIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRrilkS 274
Cdd:cd06639 174 VSAQLTSARLRRNTS-VGTPFWMAPEVIaceQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPR----N 248
                       250       260       270
                ....*....|....*....|....*....|
gi 32528297 275 EPP---YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd06639 249 PPPtllNPEKWCRGFSHFISQCLIKDFEKR 278
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
421-548 3.37e-25

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 105.10  E-value: 3.37e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 421 QHYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT---------QKEITALKLCEgHPNIVKLHEVFHDQ 491
Cdd:cd14194   5 DYYDTG---EELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSrrgvsrediEREVSILKEIQ-HPNVITLHEVYENK 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 492 LHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14194  81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPE 137
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
46-301 4.35e-25

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 104.68  E-value: 4.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKkativQKAKTTEHTRTERQVLEHIR-QSPFLVTLHYAFQTE 124
Cdd:cd13996   5 LNDFEEIELLGSGGFGSVYKVRN---KVDGVTYAIKKIR-----LTEKSSASEKVLREVKALAKlNHPNIVRYYTAWVEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERFT---EHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV-LTDFGLSK 200
Cdd:cd13996  77 PPLYIQMELCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVkIGDFGLAT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFVADETERAY-------------SFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLtgaSPFTVDGEKnsqAEI 267
Cdd:cd13996 157 SIGNQKRELNNlnnnnngntsnnsVGIGTPLYASPEQLDGEN--YNEKADIYSLGIILFEML---HPFKTAMER---STI 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 32528297 268 SRRILKSEPP------YPQEmsalaKDLIQRLLMKDPKKR 301
Cdd:cd13996 229 LTDLRNGILPesfkakHPKE-----ADLIQSLLSKNPEER 263
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
432-548 4.67e-25

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 105.21  E-value: 4.67e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAF-AVKIISK----------RMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd14096   9 IGEGAFSNVYKAVPLRNTGKPvAIKVVRKadlssdnlkgSSRANILKEVQIMKRLS-HPNIVKLLDFQESDEYYYIVLEL 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14096  88 ADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPE 135
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
48-301 5.08e-25

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 104.00  E-value: 5.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKativQKAKTTEHTRTERQVLEH--IRQSPFLVTLHYAFQTET 125
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRS---KVDGCLYAVKKSKK----PFRGPKERARALREVEAHaaLGQHPNIVRYYSSWEEGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGEL---FTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLskef 202
Cdd:cd13997  74 HLYIQMELCENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGL---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 vADETERAYSFC-GTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGaSPFTVDGEKNSQAEISRRILKSEPPYPQE 281
Cdd:cd13997 150 -ATRLETSGDVEeGDSRYLAPELLN-ENYTHLPKADIFSLGVTVYEAATG-EPLPRNGQQWQQLRQGKLPLPPGLVLSQE 226
                       250       260
                ....*....|....*....|
gi 32528297 282 MSALAKDLIQRllmkDPKKR 301
Cdd:cd13997 227 LTRLLKVMLDP----DPTRR 242
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
432-548 5.62e-25

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 103.84  E-value: 5.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIS-----KRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISrkklnKKLQENLESEIAILKSIK-HPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14009  80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQ 121
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
52-319 6.72e-25

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 104.34  E-value: 6.72e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLkkatIVQKAKTTEHTRTERQVLEHIRQSPFLVTL--HYAFQTETKLH- 128
Cdd:cd13985   5 TKQLGEGGFSYVYLAHD---VNTGRRYALKRM----YFNDEEQLRVAIKEIEIMKRLCGHPNIVQYydSAILSSEGRKEv 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 -LILDYInGGELFTHLSQRE--RFTEHEVQIYVGEIVLALEHLHKLG--IIYRDIKLENILLDSNGHVVLTDFG-LSKEF 202
Cdd:cd13985  78 lLLMEYC-PGSLVDILEKSPpsPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsATTEH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETEraySFCGTIE----------YMAPDI--VRGGDSGHDKAvDWWSLGVLMYELLTGASPFtvdgEKNSQAEIS-- 268
Cdd:cd13985 157 YPLERA---EEVNIIEeeiqknttpmYRAPEMidLYSKKPIGEKA-DIWALGCLLYKLCFFKLPF----DESSKLAIVag 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 269 RRILKSEPPYPQEMsalaKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd13985 229 KYSIPEQPRYSPEL----HDLIRHMLTPDPAERP-----DIFQVINIITKD 270
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
104-318 7.03e-25

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 103.75  E-value: 7.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 104 VLEHirqsPFLVTLHYAFQTETK-LHLILDYINGGELFTH--LSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKL 180
Cdd:cd14109  52 SLDH----PNIVQMHDAYDDEKLaVTVIDNLASTIELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRP 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 181 ENILLdSNGHVVLTDFGLSKEFVADETerAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGE 260
Cdd:cd14109 128 EDILL-QDDKLKLADFGQSRRLLRGKL--TTLIYGSPEFVSPEIVNS--YPVTLATDMWSVGVLTYVLLGGISPFLGDND 202
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 261 KNSQAEI--SRRILKSEPPYPqeMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14109 203 RETLTNVrsGKWSFDSSPLGN--ISDDARDFIKKLLVYIPESRL-----TVDEALNHPWF 255
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
54-317 7.77e-25

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 104.06  E-value: 7.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVF--LVrkisghDTGKLYAMKVLKKATIVQKAKTTEHTRTERQV-----LEHIRQSPFLVTLhyafQTETK 126
Cdd:cd06631   8 VLGKGAYGTVYcgLT------STGQLIAVKQVELDTSDKEKAEKEYEKLQEEVdllktLKHVNIVGYLGTC----LEDNV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF---- 202
Cdd:cd06631  78 VSIFMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLcinl 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 -VADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEI----SRRilKSEPP 277
Cdd:cd06631 158 sSGSQSQLLKSMRGTPYWMAPEVIN--ETGHGRKSDIWSIGCTVFEMATGKPPWA---DMNPMAAIfaigSGR--KPVPR 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 32528297 278 YPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLF 317
Cdd:cd06631 231 LPDKFSPEARDFVHACLTRDQDERP-----SAEQLLKHPF 265
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
429-548 7.91e-25

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 103.82  E-value: 7.91e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN------TQKEITALKLCeGHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd14014   5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDeefrerFLREARALARL-SHPNIVRVYDVGEDDGRPYIVMEYVE 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14014  84 GGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPA 129
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
55-318 9.11e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 104.30  E-value: 9.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisgHDTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd06659  29 IGEGSTGVVCIARE---KHSGRQVAVKMMD----LRKQQRRELLFNEVVIMRDY-QHPNVVEMYKSYLVGEELWVLMEYL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAySFC 214
Cdd:cd06659 101 QGGAL-TDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRK-SLV 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 215 GTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILKSEPPY---PQEMSALAKDLIQ 291
Cdd:cd06659 179 GTPYWMAPEVI--SRCPYGTEVDIWSLGIMVIEMVDGEPPYFSD----SPVQAMKRLRDSPPPKlknSHKASPVLRDFLE 252
                       250       260
                ....*....|....*....|....*..
gi 32528297 292 RLLMKDPKKRlgcgpRDADEIKEHLFF 318
Cdd:cd06659 253 RMLVRDPQER-----ATAQELLDHPFL 274
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
430-548 1.01e-24

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 107.41  E-value: 1.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT------QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:COG0515  13 RLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPearerfRREARALARLN-HPNIVRVYDVGEEDGRPYLVMEYVEG 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:COG0515  92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPA 136
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
49-301 1.40e-24

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 103.60  E-value: 1.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVR-KISGhdtgKLYAMKvlkkaTIVQKAKTTEHTRTERQV-----LEHirqsPFLVTLHYAFQ 122
Cdd:cd14046   8 FEELQVLGKGAFGQVVKVRnKLDG----RYYAIK-----KIKLRSESKNNSRILREVmllsrLNH----QHVVRYYQAWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE- 201
Cdd:cd14046  75 ERANLYIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSn 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 ----------------FVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELltgASPFTVDGEKNSQA 265
Cdd:cd14046 155 klnvelatqdinkstsAALGSSGDLTGNVGTALYVAPEVQSGTKSTYNEKVDMYSLGIIFFEM---CYPFSTGMERVQIL 231
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 266 EISRRILKSEPP-YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14046 232 TALRSVSIEFPPdFDDNKHSKQAKLIRWLLNHDPAKR 268
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
48-317 1.53e-24

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 103.20  E-value: 1.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLK-KATIVQKAKTTEHTRTERQVLEHIRQSPflVTLHYAF---QT 123
Cdd:cd06652   3 NWRLGKLLGQGAFGRVYLCYDA---DTGRELAVKQVQfDPESPETSKEVNALECEIQLLKNLLHER--IVQYYGClrdPQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF- 202
Cdd:cd06652  78 ERTLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLq 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 -VADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRRILK-SEPPYPQ 280
Cdd:cd06652 158 tICLSGTGMKSVTGTPYWMSPEVISG--EGYGRKADIWSVGCTVVEMLTEKPPW---AEFEAMAAIFKIATQpTNPQLPA 232
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 281 EMSALAKDLIQRLLMkDPKKRlgcgpRDADEIKEHLF 317
Cdd:cd06652 233 HVSDHCRDFLKRIFV-EAKLR-----PSADELLRHTF 263
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
50-301 1.83e-24

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 103.39  E-value: 1.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  50 ELLKVLGTGAYGKVFLVRKisgHDTGKLYAMK----VLKKATIVQKAKttehtrtERQVLeHIRQSPFLVTLHYAFQTET 125
Cdd:cd06622   4 EVLDELGKGNYGSVYKVLH---RPTGVTMAMKeirlELDESKFNQIIM-------ELDIL-HKAVSPYIVDFYGAFFIEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGG---ELFTHLSQRERFTEHEVQIYVGEIVLALEHL-HKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd06622  73 AVYMCMEYMDAGsldKLYAGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVAdetERAYSFCGTIEYMAPDIVRGGDSG----HDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISrRILKSEPP 277
Cdd:cd06622 153 LVA---SLAKTNIGCQSYMAPERIKSGGPNqnptYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLS-AIVDGDPP 228
                       250       260
                ....*....|....*....|....*
gi 32528297 278 -YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd06622 229 tLPSGYSDDAQDFVAKCLNKIPNRR 253
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
50-301 2.96e-24

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 101.84  E-value: 2.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297     50 ELLKVLGTGAYGKVFLVR-KISGHDTGKLYAMKVLKK-ATIVQKAKTTEHTRTERQvLEHirqsPFLVTLHYAFQTETKL 127
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlKGKGGKKKVEVAVKTLKEdASEQQIEEFLREARIMRK-LDH----PNVVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    128 HLILDYINGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:smart00219  77 YIVMEYMEGGDLLSYLrKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    207 TERAYSFCGTIEYMAPDIVRGGDSGHdkAVDWWSLGVLMYELLT-GASPFtvDGEKNSQAE---ISRRILKSEPPYPQEM 282
Cdd:smart00219 157 YYRKRGGKLPIRWMAPESLKEGKFTS--KSDVWSFGVLLWEIFTlGEQPY--PGMSNEEVLeylKNGYRLPQPPNCPPEL 232
                          250
                   ....*....|....*....
gi 32528297    283 salaKDLIQRLLMKDPKKR 301
Cdd:smart00219 233 ----YDLMLQCWAEDPEDR 247
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
42-319 3.01e-24

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 102.39  E-value: 3.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  42 EKVGIENFELLKVLGTGAYGKVFLVRKISGHDTGklYAMKVLKKATIvqkAKTTEHTRTERQVLEHIrQSPFLVTLHYAF 121
Cdd:cd14201   1 EVVGDFEYSRKDLVGHGAFAVVFKGRHRKKTDWE--VAIKSINKKNL---SKSQILLGKEIKILKEL-QHENIVALYDVQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD---------SNGHVV 192
Cdd:cd14201  75 EMPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 193 LTDFGLSKEFVADETerAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQA--EISRR 270
Cdd:cd14201 155 IADFGFARYLQSNMM--AATLCGSPMYMAPEVIM--SQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMfyEKNKN 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 271 ILksePPYPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd14201 231 LQ---PSIPRETSPYLADLLLGLLQRNQKDRM-----DFEAFFSHPFLE 271
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
55-301 3.25e-24

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 102.15  E-value: 3.25e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKttEHTRTERQVLEHIRqSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd13978   1 LGSGGFGTVSKARHVS---WFGMVAIKCLHSSPNCIEER--KALLKEAEKMERAR-HSYVLPLLGVCVERRSLGLVMEYM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELfTHLSQRE--------RFTehevqiYVGEIVLALEHLHKL--GIIYRDIKLENILLDSNGHVVLTDFGLSK---- 200
Cdd:cd13978  75 ENGSL-KSLLEREiqdvpwslRFR------IIHEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLSKlgmk 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFtvDGEKNSQAEISRRILKSEP---- 276
Cdd:cd13978 148 SISANRRRGTENLGGTPIYMAPEAFDDFNKKPTSKSDVYSFAIVIWAVLTRKEPF--ENAINPLLIMQIVSKGDRPsldd 225
                       250       260
                ....*....|....*....|....*...
gi 32528297 277 ---PYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd13978 226 igrLKQIENVQELISLMIRCWDGNPDAR 253
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
432-547 3.92e-24

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 101.77  E-value: 3.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIS-KRMEA----NTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd08215   8 IGKGSFGSAYLVRRKSDGKLYVLKEIDlSNMSEkereEALNEVKLLSKLK-HPNIVKYYESFEENGKLCIVMEYADGGDL 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 507 FERIKKKK----HFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd08215  87 AQKIKKQKkkgqPFPEEQILDWFVQICLALKYLHSRKILHRDLKT 131
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
432-548 4.68e-24

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 101.46  E-value: 4.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT--QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFER 509
Cdd:cd14087   9 IGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREvcESELNVLRRVR-HTNIIQLIEVFETKERVYMVMELATGGELFDR 87
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 510 IKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14087  88 IIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPE 126
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
49-345 4.91e-24

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 102.99  E-value: 4.91e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvrkiSGHD--TGKLYAMKVLkkativqkAKTTEHTRTERQVLEHIR-----QSPFLVTLH--- 118
Cdd:cd07834   2 YELLKPIGSGAYGVVC-----SAYDkrTGRKVAIKKI--------SNVFDDLIDAKRILREIKilrhlKHENIIGLLdil 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 119 YAFQTET--KLHLILDYInGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDF 196
Cdd:cd07834  69 RPPSPEEfnDVYIVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 197 GLSKEFVADETERAYS-FCGTIEYMAPDIVrGGDSGHDKAVDWWSLGVLMYELLTGASPF-------------------- 255
Cdd:cd07834 148 GLARGVDPDEDKGFLTeYVVTRWYRAPELL-LSSKKYTKAIDIWSVGCIFAELLTRKPLFpgrdyidqlnlivevlgtps 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 256 --TVDGEKNSQAeisRRILKSEPPYPQ--------EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQKI-NWD 324
Cdd:cd07834 227 eeDLKFISSEKA---RNYLKSLPKKPKkplsevfpGASPEAIDLLEKMLVFNPKKRI-----TADEALAHPYLAQLhDPE 298
                       330       340
                ....*....|....*....|.
gi 32528297 325 DLAAKKVPAPFKPVIRDELDV 345
Cdd:cd07834 299 DEPVAKPPFDFPFFDDEELTI 319
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
49-301 6.03e-24

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 101.03  E-value: 6.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    49 FELLKVLGTGAYGKVFL-VRKISGHDTGKLYAMKVLKK-ATIVQKAKTTEHTRTERQvLEHirqsPFLVTLHYAFQTETK 126
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKgTLKGEGENTKIKVAVKTLKEgADEEEREDFLEEASIMKK-LDH----PNIVKLLGVCTQGEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   127 LHLILDYINGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:pfam07714  76 LYIVTEYMPGGDLLDFLrKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   206 ETERAYSFCGT-IEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPFtvdgEKNSQAEISRRILKSE----PPY- 278
Cdd:pfam07714 156 DYYRKRGGGKLpIKWMAPESLK--DGKFTSKSDVWSFGVLLWEIFTlGEQPY----PGMSNEEVLEFLEDGYrlpqPENc 229
                         250       260
                  ....*....|....*....|...
gi 32528297   279 PQEMsalaKDLIQRLLMKDPKKR 301
Cdd:pfam07714 230 PDEL----YDLMKQCWAYDPEDR 248
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
50-301 7.19e-24

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 100.70  E-value: 7.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297     50 ELLKVLGTGAYGKVFLVR-KISGHDTGKLYAMKVLKKATivqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlKGKGDGKEVEVAVKTLKEDA---SEQQIEEFLREARIMRKLDH-PNIVKLLGVCTEEEPLM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    129 LILDYINGGELFTHL--SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:smart00221  78 IVMEYMPGGDLLDYLrkNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    207 TERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPFtvDGEKNsqAEISRRILKSE-PPYPQEMSA 284
Cdd:smart00221 158 YYKVKGGKLPIRWMAPESLK--EGKFTSKSDVWSFGVLLWEIFTlGEEPY--PGMSN--AEVLEYLKKGYrLPKPPNCPP 231
                          250
                   ....*....|....*..
gi 32528297    285 LAKDLIQRLLMKDPKKR 301
Cdd:smart00221 232 ELYKLMLQCWAEDPEDR 248
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
46-315 7.60e-24

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 101.58  E-value: 7.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKA------------KTTEHTRTERQVLEHIRQS-- 111
Cdd:cd14199   1 LNQYKLKDEIGKGSYGVVKLAYN---EDDNTYYAMKVLSKKKLMRQAgfprrppprgarAAPEGCTQPRGPIERVYQEia 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 112 -------PFLVTLHYAFQ--TETKLHLILDYINGGELFtHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLEN 182
Cdd:cd14199  78 ilkkldhPNVVKLVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 183 ILLDSNGHVVLTDFGLSKEFVADETERAySFCGTIEYMAPDIV---RGGDSGhdKAVDWWSLGVLMYELLTGASPFtvdg 259
Cdd:cd14199 157 LLVGEDGHIKIADFGVSNEFEGSDALLT-NTVGTPAFMAPETLsetRKIFSG--KALDVWAMGVTLYCFVFGQCPF---- 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 260 eknsqaeISRRIL------KSEP---PYPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEH 315
Cdd:cd14199 230 -------MDERILslhskiKTQPlefPDQPDISDDLKDLLFRMLDKNPESRI-----SVPEIKLH 282
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
432-548 8.01e-24

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 100.38  E-value: 8.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEA---NTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKdreDVRNEIEIMNQLR-HPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 509 R-IKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14103  80 RvVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPE 120
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
430-548 1.42e-23

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 100.23  E-value: 1.42e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK--RMEANTQKEIT---ALKlcegHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd14662   6 KDIGSGNFGVARLMRNKETKELVAVKYIERglKIDENVQREIInhrSLR----HPNIIRFKEVVLTPTHLAIVMEYAAGG 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14662  82 ELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLE 125
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
430-547 1.70e-23

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 99.97  E-value: 1.70e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK----EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd06623   7 KVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKqllrELKTLRSCE-SPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMH-DVGVVHRDLKP 547
Cdd:cd06623  86 LADLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKP 128
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
53-319 2.18e-23

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 99.77  E-value: 2.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKIsghDTGK-LYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPflVTLHYAF---QTETKLH 128
Cdd:cd06651  13 KLLGQGAFGRVYLCYDV---DTGReLAAKQVQFDPESPETSKEVSALECEIQLLKNLQHER--IVQYYGClrdRAEKTLT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF--VADE 206
Cdd:cd06651  88 IFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqtICMS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRRILK-SEPPYPQEMSAL 285
Cdd:cd06651 168 GTGIRSVTGTPYWMSPEVISG--EGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIATQpTNPQLPSHISEH 242
                       250       260       270
                ....*....|....*....|....*....|....
gi 32528297 286 AKDLIQRLLMkDPKKRlgcgpRDADEIKEHLFFQ 319
Cdd:cd06651 243 ARDFLGCIFV-EARHR-----PSAEELLRHPFAQ 270
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
53-301 2.18e-23

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 99.54  E-value: 2.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISGHDTGKLYAMKVLK-KATIVQKAKTTEhtrtERQVLEHIRQsPFLVTLhYAFQTE-TKLHLI 130
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKeDASESERKDFLK----EARVMKKLGH-PNVVRL-LGVCTEeEPLYLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHL-SQRERFTEHEVQI--------YVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd00192  75 MEYMEGGDLLDFLrKSRPVFPSPEPSTlslkdllsFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fvADETERAYSFCGT---IEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFtvDGEKNSqaEISRRILK-SEP 276
Cdd:cd00192 155 --IYDDDYYRKKTGGklpIRWMAPESLKDGI--FTSKSDVWSFGVLLWEIFTlGATPY--PGLSNE--EVLEYLRKgYRL 226
                       250       260
                ....*....|....*....|....*
gi 32528297 277 PYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd00192 227 PKPENCPDELYELMLSCWQLDPEDR 251
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
430-548 2.31e-23

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 99.38  E-value: 2.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK-RMEANT-----QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14073   7 ETLGKGTYGKVKLAIERATGREVAIKSIKKdKIEDEQdmvriRREIEIMSSLN-HPHIIRIYEVFENKDKIVIVMEYASG 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14073  86 GELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLE 130
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
47-320 2.68e-23

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 99.76  E-value: 2.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkatIVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd06641   4 ELFTKLEKIGKGSFGEVF---KGIDNRTQKVVAIKIID---LEEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLKDTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFThLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd06641  77 LWIIMEYLGGGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAySFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQ-EMSAL 285
Cdd:cd06641 156 IKRN-*FVGTPFWMAPEVIK--QSAYDSKADIWSLGITAIELARGEPPHS----ELHPMKVLFLIPKNNPPTLEgNYSKP 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 286 AKDLIQRLLMKDPKKRlgcgpRDADEIKEHLFFQK 320
Cdd:cd06641 229 LKEFVEACLNKEPSFR-----PTAKELLKHKFILR 258
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
55-319 2.76e-23

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 99.23  E-value: 2.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd06647  15 IGQGASGTVYTAIDVA---TGQEVAIKQMN----LQQQPKKELIINEILVMRENKN-PNIVNYLDSYLVGDELWVVMEYL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAySFC 214
Cdd:cd06647  87 AGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TMV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 215 GTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRiLKSEPPYPQEMSALAKDLIQRLL 294
Cdd:cd06647 165 GTPYWMAPEVVTRKAYG--PKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN-GTPELQNPEKLSAIFRDFLNRCL 241
                       250       260
                ....*....|....*....|....*
gi 32528297 295 MKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd06647 242 EMDVEKRG-----SAKELLQHPFLK 261
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
49-255 2.86e-23

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 99.70  E-value: 2.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATivqkaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTET--- 125
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHVK---TGQLAAIKVMDVTE-----DEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSppg 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 ---KLHLILDYINGGELfTHLSQRER---FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd06636  90 hddQLWLVMEFCGAGSV-TDLVKNTKgnaLKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KEFvaDET-ERAYSFCGTIEYMAPDIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd06636 169 AQL--DRTvGRRNTFIGTPYWMAPEVIacdENPDATYDYRSDIWSLGITAIEMAEGAPPL 226
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
48-337 2.99e-23

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 99.95  E-value: 2.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKkatiVQKAKTTEH--TRT---ERQVLEHIRQsPFLVTLHYAFQ 122
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKARD---KETGRIVAIKKIK----LGERKEAKDgiNFTalrEIKLLQELKH-PNIIGLLDVFG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYinggeLFTHLSQ-----RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd07841  73 HKSNINLVFEF-----METDLEKvikdkSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEFVADETERAYSFCgTIEYMAPDIVRGGDSGHdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRI------ 271
Cdd:cd07841 148 LARSFGSPNRKMTHQVV-TRWYRAPELLFGARHYG-VGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALgtptee 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 272 -------------LKSEPPYP--QEMSAL---AKDLIQRLLMKDPKKRLGCgpRDAdeiKEHLFFqkinwddlaaKKVPA 333
Cdd:cd07841 226 nwpgvtslpdyveFKPFPPTPlkQIFPAAsddALDLLQRLLTLNPNKRITA--RQA---LEHPYF----------SNDPA 290

                ....
gi 32528297 334 PFKP 337
Cdd:cd07841 291 PTPP 294
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
432-548 3.12e-23

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 99.09  E-value: 3.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT-------QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd14098   8 LGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNdknlqlfQREINILKSLE-HPGIVRLIDWYEDDQHIYLVMEYVEGG 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14098  87 DLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPE 130
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
49-297 3.57e-23

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 98.91  E-value: 3.57e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVflvRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRtERQVLEHIRQSPFLVTLHYAFQTETKLH 128
Cdd:cd14163   2 YQLGKTIGEGTYSKV---KEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPR-ELQIVERLDHKNIIHVYEMLESADGKIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNgHVVLTDFGLSKEFVADETE 208
Cdd:cd14163  78 LVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQLPKGGRE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSFCGTIEYMAPDIVRGgdSGHD-KAVDWWSLGVLMYELLTGASPFtvdgeknSQAEISRRILKSEP----PYPQEMS 283
Cdd:cd14163 157 LSQTFCGSTAYAAPEVLQG--VPHDsRKGDIWSMGVVLYVMLCAQLPF-------DDTDIPKMLCQQQKgvslPGHLGVS 227
                       250
                ....*....|....
gi 32528297 284 ALAKDLIQRLLMKD 297
Cdd:cd14163 228 RTCQDLLKRLLEPD 241
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
47-320 4.83e-23

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 99.04  E-value: 4.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKkATIvqkaKTTEHTRTERQVLEHIRQS--PFLVTLHYAFQTE 124
Cdd:cd06617   1 DDLEVIEELGRGAYG---VVDKMRHVPTGTIMAVKRIR-ATV----NSQEQKRLLMDLDISMRSVdcPYTVTFYGALFRE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGG--ELFTHLSQRERFTEHEV--QIYVGeIVLALEHLH-KLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd06617  73 GDVWICMEVMDTSldKFYKKVYDKGLTIPEDIlgKIAVS-IVKALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCDFGIS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KEFVAD--ETERAysfcGTIEYMAPDIV--RGGDSGHDKAVDWWSLGVLMYELLTGASPFtvDGEKNSQAEISRRILKSE 275
Cdd:cd06617 152 GYLVDSvaKTIDA----GCKPYMAPERInpELNQKGYDVKSDVWSLGITMIELATGRFPY--DSWKTPFQQLKQVVEEPS 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 276 PPYPQE-MSALAKDLIQRLLMKDPKKRlgcgPRDAdEIKEHLFFQK 320
Cdd:cd06617 226 PQLPAEkFSPEFQDFVNKCLKKNYKER----PNYP-ELLQHPFFEL 266
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
55-255 5.15e-23

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 97.95  E-value: 5.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLvrkisghdtGKLYAMKV-LKKatiVQKAKTTEhtrterqvLEHIR--QSPFLVTLHYAFQTETKLHLIL 131
Cdd:cd14059   1 LGSGAQGAVFL---------GKFRGEEVaVKK---VRDEKETD--------IKHLRklNHPNIIKFKGVCTQAPCYCILM 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETEraY 211
Cdd:cd14059  61 EYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTK--M 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 32528297 212 SFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd14059 139 SFAGTVAWMAPEVIR--NEPCSEKVDIWSFGVVLWELLTGEIPY 180
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
46-301 5.76e-23

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 99.34  E-value: 5.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKISGHdtgklyAMKVLKKATI--VQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQT 123
Cdd:cd08229  23 LANFRIEKKIGRGQFSEVYRATCLLDG------VPVALKKVQIfdLMDAKARADCIKEIDLLKQLNH-PNVIKYYASFIE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGEL---FTHLSQRERFT-EHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd08229  96 DNELNIVLELADAGDLsrmIKHFKKQKRLIpEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLG 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KeFVADETERAYSFCGTIEYMAPDivRGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRILKSE-PPY 278
Cdd:cd08229 176 R-FFSSKTTAAHSLVGTPYYMSPE--RIHENGYNFKSDIWSLGCLLYEMAALQSPFY--GDKMNLYSLCKKIEQCDyPPL 250
                       250       260
                ....*....|....*....|....
gi 32528297 279 PQE-MSALAKDLIQRLLMKDPKKR 301
Cdd:cd08229 251 PSDhYSEELRQLVNMCINPDPEKR 274
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
423-548 7.03e-23

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 98.13  E-value: 7.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 423 YDLdLKDkpLGEGSFSICRKCVHKKSNQAFAVKIISK--RMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd14665   2 YEL-VKD--IGSGNFGVARLMRDKQTKELVAVKYIERgeKIDENVQREIINHRSLR-HPNIVRFKEVILTPTHLAIVMEY 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14665  78 AAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLE 125
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
55-319 7.16e-23

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 99.03  E-value: 7.16e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHiRQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd06654  28 IGQGASGTVYTAMDVA---TGQEVAIRQMN----LQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEYL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAySFC 214
Cdd:cd06654 100 AGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TMV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 215 GTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRiLKSEPPYPQEMSALAKDLIQRLL 294
Cdd:cd06654 178 GTPYWMAPEVVT--RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATN-GTPELQNPEKLSAIFRDFLNRCL 254
                       250       260
                ....*....|....*....|....*
gi 32528297 295 MKDPKKRlgcgpRDADEIKEHLFFQ 319
Cdd:cd06654 255 EMDVEKR-----GSAKELLQHQFLK 274
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
432-547 7.33e-23

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 98.56  E-value: 7.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVK-IISKRMEANTQ----KEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLnGGEL 506
Cdd:cd07832   8 IGEGAHGIVFKAKDRETGETVALKkVALRKLEGGIPnqalREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYM-LSSL 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07832  87 SEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKP 128
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
422-548 7.78e-23

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 98.33  E-value: 7.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDLKdkpLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT---------QKEITALKLCEgHPNIVKLHEVFHDQL 492
Cdd:cd14105   6 FYDIGEE---LGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASrrgvsrediEREVSILRQVL-HPNIITLHDVFENKT 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 493 HTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14105  82 DVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPE 137
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
430-547 9.10e-23

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 97.66  E-value: 9.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKII---SKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd05122   6 EKIGKGGFGVVYKARHKKTGQIVAIKKInleSKEKKESILNEIAILKKCK-HPNIVKYYGSYLKKDELWIVMEFCSGGSL 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd05122  85 KDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKA 126
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
430-548 1.14e-22

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 97.37  E-value: 1.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT--QK----EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14162   6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDylQKflprEIEVIKGLK-HPNLICFYEAIETTSRVYIIMELAEN 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14162  85 GDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCE 129
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
49-318 1.25e-22

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 97.34  E-value: 1.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLK--KATIVQKAKttehtrtERQVLEHIRQSP-----FLVTLHYAF 121
Cdd:cd14133   1 YEVLEVLGKGTFGQVV---KCYDLLTGEEVALKIIKnnKDYLDQSLD-------EIRLLELLNKKDkadkyHIVRLKDVF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTetKLHLILDY-INGGELFTHLSQ-RER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG--HVVLTDF 196
Cdd:cd14133  71 YF--KNHLCIVFeLLSQNLYEFLKQnKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 197 GLSKEfvadETERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEP 276
Cdd:cd14133 149 GSSCF----LTQRLYSYIQSRYYRAPEVILGLP--YDEKIDMWSLGCILAELYTGEPLFP----GASEVDQLARIIGTIG 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 277 PYPQEMSALAK-------DLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14133 219 IPPAHMLDQGKaddelfvDFLKKLLEIDPKERP-----TASQALSHPWL 262
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
28-319 1.32e-22

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 98.26  E-value: 1.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  28 VKHELRTANLTGHAEKvgieNFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEH 107
Cdd:cd06655   4 IMEKLRTIVSIGDPKK----KYTRYEKIGQGASGTVFTAIDVA---TGQEVAIKQIN----LQKQPKKELIINEILVMKE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 108 IRqSPFLVTLHYAFQTETKLHLILDYINGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS 187
Cdd:cd06655  73 LK-NPNIVNFLDSFLVGDELFVVMEYLAGGSL-TDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGM 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 188 NGHVVLTDFGLSKEFVADETERAySFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEI 267
Cdd:cd06655 151 DGSVKLTDFGFCAQITPEQSKRS-TMVGTPYWMAPEVVT--RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 268 SRRiLKSEPPYPQEMSALAKDLIQRLLMKDPKKRlgcgpRDADEIKEHLFFQ 319
Cdd:cd06655 228 ATN-GTPELQNPEKLSPIFRDFLNRCLEMDVEKR-----GSAKELLQHPFLK 273
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
422-548 1.33e-22

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 97.07  E-value: 1.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN----TQKEITALK-LCegHPNIVKLHEVFHDQLHTFL 496
Cdd:cd14078   4 YYELH---ETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDdlprVKTEIEALKnLS--HQHICRLYHVIETDNKIFM 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 497 VMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14078  79 VLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPE 130
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
432-548 1.38e-22

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 97.25  E-value: 1.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQA--FAVKIISKRMEANTQKE---------ITALKlcegHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd14080   8 IGEGSYSKVKLAEYTKSGLKekVACKIIDKKKAPKDFLEkflpreleiLRKLR----HPNIIQVYSIFERGSKVFIFMEY 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14080  84 AEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCE 131
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
432-548 1.86e-22

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 96.81  E-value: 1.86e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR-------MEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd14070  10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKkakkdsyVTKNLRREGRIQQMIR-HPNITQLLDILETENSYYLVMELCPGG 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14070  89 NLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIE 132
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
65-316 2.28e-22

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 97.48  E-value: 2.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  65 LVRKisgHDTGKLYAMKVLkkaTIVQKAKTTEHTR-------TERQVLEHIRQSPFLVTLHYAFQTET------------ 125
Cdd:cd13974  16 LARK---EGTDDFYTLKIL---TLEEKGEETQEDRqgkmllhTEYSLLSLLHDQDGVVHHHGLFQDRAceikedkssnvy 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 ------KLHLILD-------------YINggeLFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD 186
Cdd:cd13974  90 tgrvrkRLCLVLDclcahdfsdktadLIN---LQHYVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 187 SNGH-VVLTDFGLSKEFVAdETERAYSFCGTIEYMAPDIVRGGD-SGhdKAVDWWSLGVLMYELLTGASPFTvdgeKNSQ 264
Cdd:cd13974 167 KRTRkITITNFCLGKHLVS-EDDLLKDQRGSPAYISPDVLSGKPyLG--KPSDMWALGVVLFTMLYGQFPFY----DSIP 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 265 AEISRRILKSEPPYPQE--MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHL 316
Cdd:cd13974 240 QELFRKIKAAEYTIPEDgrVSENTVCLIRKLLVLNPQKRL-----TASEVLDSL 288
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
415-548 2.67e-22

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 96.54  E-value: 2.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 415 KDSPFYQHYDLdLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK-----EITALKLCEGHPNIVKLHEVFH 489
Cdd:cd14197   1 RSEPFQERYSL-SPGRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRmeiihEIAVLELAQANPWVINLHEVYE 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 490 DQLHTFLVMELLNGGELFERI--KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14197  80 TASEMILVLEYAAGGEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQ 140
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
47-320 2.78e-22

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 96.66  E-value: 2.78e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkatIVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd06640   4 ELFTKLERIGKGSFGEVF---KGIDNRTQQVVAIKIID---LEEAEDEIEDIQQEITVLSQC-DSPYVTKYYGSYLKGTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFThLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd06640  77 LWIIMEYLGGGSALD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAySFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPftvdgekNSQAEISR---RILKSEPP-YPQEM 282
Cdd:cd06640 156 IKRN-TFVGTPFWMAPEVIQ--QSAYDSKADIWSLGITAIELAKGEPP-------NSDMHPMRvlfLIPKNNPPtLVGDF 225
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 32528297 283 SALAKDLIQRLLMKDPKKRlgcgpRDADEIKEHLFFQK 320
Cdd:cd06640 226 SKPFKEFIDACLNKDPSFR-----PTAKELLKHKFIVK 258
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
47-322 2.98e-22

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 97.05  E-value: 2.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVflvRKISGHDTGKLYAMKVLKkATIVQKakttEHTRTeRQVLEHIRQS---PFLVTLHYAFQT 123
Cdd:cd06616   6 EDLKDLGEIGRGAFGTV---NKMLHKPSGTIMAVKRIR-STVDEK----EQKRL-LMDLDVVMRSsdcPYIVKFYGALFR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 E-----------TKLHLILDYInggelftHLSQRERFTEHEVQIYVGEIVLALEHLHK-LGIIYRDIKLENILLDSNGHV 191
Cdd:cd06616  77 EgdcwicmelmdISLDKFYKYV-------YEVLDSVIPEEILGKIAVATVKALNYLKEeLKIIHRDVKPSNILLDRNGNI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 192 VLTDFGLSKEFVAdeteraySFCGTIE-----YMAPDIV--RGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQ 264
Cdd:cd06616 150 KLCDFGISGQLVD-------SIAKTRDagcrpYMAPERIdpSASRDGYDVRSDVWSLGITLYEVATGKFPYP---KWNSV 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 265 AEISRRILKSEPP-----YPQEMSALAKDLIQRLLMKDPKKRlgcgPRdADEIKEHLFFQKIN 322
Cdd:cd06616 220 FDQLTQVVKGDPPilsnsEEREFSPSFVNFVNLCLIKDESKR----PK-YKELLKHPFIKMYE 277
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
430-548 3.42e-22

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 96.25  E-value: 3.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRM----EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd14184   7 KVIGDGNFAVVKECVERSTGKEFALKIIDKAKccgkEHLIENEVSILRRVK-HPNIIMLIEEMDTPAELYLVMELVKGGD 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14184  86 LFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPE 128
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
36-340 3.45e-22

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 97.06  E-value: 3.45e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  36 NLTGHAEKVGIENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKvlkkaTIVQKAKTTEHTRTER--QVLEHIRQSPF 113
Cdd:cd06618   4 TIDGKKYKADLNDLENLGEIGSGTCGQVYKMRHKK---TGHVMAVK-----QMRRSGNKEENKRILMdlDVVLKSHDCPY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 114 LVTLHYAFQTETKLHLILDYIngGELFTHLSQRER--FTEHEVQIYVGEIVLALEHL-HKLGIIYRDIKLENILLDSNGH 190
Cdd:cd06618  76 IVKCYGYFITDSDVFICMELM--STCLDKLLKRIQgpIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 191 VVLTDFGLSKEFVaDETERAYSfCGTIEYMAPDIVRGGDSG-HDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISR 269
Cdd:cd06618 154 VKLCDFGISGRLV-DSKAKTRS-AGCAAYMAPERIDPPDNPkYDIRADVWSLGISLVELATGQFPYR---NCKTEFEVLT 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 270 RILKSEPPYP---QEMSALAKDLIQRLLMKDPKKRlgcgPRdADEIKEHLFFQKInwdDLAAKKVPAPFKPVIR 340
Cdd:cd06618 229 KILNEEPPSLppnEGFSPDFCSFVDLCLTKDHRYR----PK-YRELLQHPFIRRY---ETAEVDVASWFQDVMA 294
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
49-301 4.84e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 96.22  E-value: 4.84e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTehTRTERQVLEHIRQSPfLVTLHYAFQTETKLH 128
Cdd:cd07848   3 FEVLGVVGEGAYGVVLKCRH---KETKEIVAIKKFKDSEENEEVKET--TLRELKMLRTLKQEN-IVELKEAFRRRGKLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELfthlsqrERFTEH-------EVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd07848  77 LVFEYVEKNML-------ELLEEMpngvppeKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETERAYSFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEIsRRILKSEPP---- 277
Cdd:cd07848 150 LSEGSNANYTEYVATRWYRSPELLLGAPYG--KAVDMWSVGCILGELSDGQPLFPGESEIDQLFTI-QKVLGPLPAeqmk 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 278 -----------------YPQEM--------SALAKDLIQRLLMKDPKKR 301
Cdd:cd07848 227 lfysnprfhglrfpavnHPQSLerrylgilSGVLLDLMKNLLKLNPTDR 275
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
432-548 5.14e-22

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 95.79  E-value: 5.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR---------MEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd14196  13 LGSGQFAIVKKCREKSTGLEYAAKFIKKRqsrasrrgvSREEIEREVSILRQVL-HPNIITLHDVYENRTDVVLILELVS 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14196  92 GGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPE 137
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
91-301 6.07e-22

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 95.85  E-value: 6.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  91 KAKTTEHTRTERQV---LEHIRqspfLVTLHYAFQTET-KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALE 166
Cdd:cd13990  44 KQNYIKHALREYEIhksLDHPR----IVKLYDVFEIDTdSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALK 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 167 HL--HKLGIIYRDIKLENILLDSN---GHVVLTDFGLSK-----EFVADETERAYSFCGTIEYMAPDI-VRGGDSGH-DK 234
Cdd:cd13990 120 YLneIKPPIIHYDLKPGNILLHSGnvsGEIKITDFGLSKimddeSYNSDGMELTSQGAGTYWYLPPECfVVGKTPPKiSS 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 235 AVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRR--ILKSE----PPYPQeMSALAKDLIQRLLMKDPKKR 301
Cdd:cd13990 200 KVDVWSVGVIFYQMLYGRKPF---GHNQSQEAILEEntILKATevefPSKPV-VSSEAKDFIRRCLTYRKEDR 268
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
55-319 6.38e-22

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 96.33  E-value: 6.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHiRQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd06656  27 IGQGASGTVYTAIDIA---TGQEVAIKQMN----LQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEYL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAySFC 214
Cdd:cd06656  99 AGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TMV 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 215 GTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRiLKSEPPYPQEMSALAKDLIQRLL 294
Cdd:cd06656 177 GTPYWMAPEVVT--RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN-GTPELQNPERLSAVFRDFLNRCL 253
                       250       260
                ....*....|....*....|....*
gi 32528297 295 MKDPKKRlgcgpRDADEIKEHLFFQ 319
Cdd:cd06656 254 EMDVDRR-----GSAKELLQHPFLK 273
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
428-548 7.84e-22

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 94.61  E-value: 7.84e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIIS--KRMEANTQKEITALKL---CEGHPNIVKLHEVFHDQL--HTFLVMEL 500
Cdd:cd05118   3 VLRKIGEGAFGTVWLARDKVTGEKVAIKKIKndFRHPKAALREIKLLKHlndVEGHPNIVKLLDVFEHRGgnHLCLVFEL 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 501 LnGGELFERIKK-KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05118  83 M-GMNLYELIKDyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPE 130
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
431-548 8.26e-22

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 95.11  E-value: 8.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 431 PLGEGSFSICRKCVHKKSNQAFAVKIISKRmEANTQ-----------KEITALKLCEGHPNIVKLHEVFHDQLHTFLVME 499
Cdd:cd13993   7 PIGEGAYGVVYLAVDLRTGRKYAIKCLYKS-GPNSKdgndfqklpqlREIDLHRRVSRHPNIITLHDVFETEVAIYIVLE 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 500 LLNGGELFERIKKKKHF--SETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd13993  86 YCPNGDLFEAITENRIYvgKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPE 136
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
432-548 8.61e-22

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 95.09  E-value: 8.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEA-----NTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd14069   9 LGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPgdcpeNIKKEVCIQKMLS-HKNVVRFYGHRREGEFQYLFLEYASGGEL 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14069  88 FDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPE 129
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
47-320 1.06e-21

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 95.12  E-value: 1.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvRKISGHdTGKLYAMKVLKkatIVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETK 126
Cdd:cd06642   4 ELFTKLERIGKGSFGEVY--KGIDNR-TKEVVAIKIID---LEEAEDEIEDIQQEITVLSQC-DSPYITRYYGSYLKGTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFThLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd06642  77 LWIIMEYLGGGSALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAySFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQ-EMSAL 285
Cdd:cd06642 156 IKRN-TFVGTPFWMAPEVIK--QSAYDFKADIWSLGITAIELAKGEPPNS----DLHPMRVLFLIPKNSPPTLEgQHSKP 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 286 AKDLIQRLLMKDPKKRlgcgpRDADEIKEHLFFQK 320
Cdd:cd06642 229 FKEFVEACLNKDPRFR-----PTAKELLKHKFITR 258
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
54-255 1.12e-21

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 94.77  E-value: 1.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLeHIRQSPFLVTLHYAFQTETKLHLILDY 133
Cdd:cd14061   1 VIGVGGFGKVY-----RGIWRGEEVAVKAARQDPDEDISVTLENVRQEARLF-WMLRHPNIIALRGVCLQPPNLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHLSQR----ERFTEHEVQIYVGeivlaLEHLHKLG---IIYRDIKLENILLD--------SNGHVVLTDFGL 198
Cdd:cd14061  75 ARGGALNRVLAGRkippHVLVDWAIQIARG-----MNYLHNEApvpIIHRDLKSSNILILeaienedlENKTLKITDFGL 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 199 SKEfvADETERAySFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd14061 150 ARE--WHKTTRM-SAAGTYAWMAPEVIK--SSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
432-548 1.73e-21

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 95.11  E-value: 1.73e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM----EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELF 507
Cdd:cd14168  18 LGTGAFSEVVLAEERATGKLFAVKCIPKKAlkgkESSIENEIAVLRKIK-HENIVALEDIYESPNHLYLVMQLVSGGELF 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 508 ERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14168  97 DRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPE 137
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
49-318 2.68e-21

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 94.26  E-value: 2.68e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAmkvLKKATIvqkaKTTEH-----TRTERQVLEHIRQS--PFLVTLH--- 118
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQ---DGRFVA---LKKVRV----PLSEEgiplsTIREIALLKQLESFehPNVVRLLdvc 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 119 --YAFQTETKLHLILDYINGgELFTHLSQ--RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLT 194
Cdd:cd07838  71 hgPRTDRELKLTLVFEHVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 195 DFGLSKefVADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRI-LK 273
Cdd:cd07838 150 DFGLAR--IYSFEMALTSVVVTLWYRAPEVLLQ--SSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIgLP 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 274 SE--------------PPYP--------QEMSALAKDLIQRLLMKDPKKRLGcgprdADEIKEHLFF 318
Cdd:cd07838 226 SEeewprnsalprssfPSYTprpfksfvPEIDEEGLDLLKKMLTFNPHKRIS-----AFEALQHPYF 287
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
430-548 2.71e-21

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 93.61  E-value: 2.71e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK-RMEANTQK----------EITALKLCE--GHPNIVKLHEVFHDQLHTFL 496
Cdd:cd14004   6 KEMGEGAYGQVNLAIYKSKGKEVVIKFIFKeRILVDTWVrdrklgtvplEIHILDTLNkrSHPNIVKLLDFFEDDEFYYL 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 497 VMELL-NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14004  86 VMEKHgSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDE 138
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
47-248 2.90e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 93.57  E-value: 2.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd06645  11 EDFELIQRIGSGTYGDVYKARNVN---TGELAAIKVIK----LEPGEDFAVVQQEIIMMKDCKH-SNIVAYFGSYLRRDK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd06645  83 LWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATI 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 32528297 207 TERAySFCGTIEYMAPDIV---RGGdsGHDKAVDWWSLGVLMYEL 248
Cdd:cd06645 163 AKRK-SFIGTPYWMAPEVAaveRKG--GYNQLCDIWAVGITAIEL 204
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
423-548 3.28e-21

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 93.25  E-value: 3.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 423 YDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISK-RMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd14074   5 YDLE---ETLGRGHFAVVKLARHVFTGEKVAVKVIDKtKLDDVSKahlfQEVRCMKLVQ-HPNVVRLYEVIDTQTKLYLI 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 498 MELLNGGELFERI-KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14074  81 LELGDGGDMYDYImKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPE 132
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
47-320 3.30e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 94.42  E-value: 3.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKAtiVQKAKTTEHTRtERQVLeHIRQSPFLVTLHYAFQTETK 126
Cdd:cd06615   1 DDFEKLGELGAGNGGVVTKVLHRP---SGLIMARKLIHLE--IKPAIRNQIIR-ELKVL-HECNSPYIVGFYGAFYSDGE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEhevqIYVGEIVLA----LEHLH-KLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd06615  74 ISICMEHMDGGSLDQVLKKAGRIPE----NILGKISIAvlrgLTYLReKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQ 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVadeTERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASP------------FTVDGEKNSQAEISR 269
Cdd:cd06615 150 LI---DSMANSFVGTRSYMSPERLQG--THYTVQSDIWSLGLSLVEMAIGRYPipppdakeleamFGRPVSEGEAKESHR 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 270 R--------------------ILKSEPP-YPQE-MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQK 320
Cdd:cd06615 225 PvsghppdsprpmaifelldyIVNEPPPkLPSGaFSDEFQDFVDKCLKKNPKERA-----DLKELTKHPFIKR 292
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
154-292 3.57e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 97.17  E-value: 3.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  154 VQIyVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERAY--SFCGTIEYMAPDIVRGGDSg 231
Cdd:NF033483 110 VEI-MIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIAR--ALSSTTMTQtnSVLGTVHYLSPEQARGGTV- 185
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297  232 hDKAVDWWSLGVLMYELLTGASPFtvDGEknSQAEISRRILKSEPPYPQE-------------MSALAKDLIQR 292
Cdd:NF033483 186 -DARSDIYSLGIVLYEMLTGRPPF--DGD--SPVSVAYKHVQEDPPPPSElnpgipqsldavvLKATAKDPDDR 254
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
55-302 3.82e-21

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 93.39  E-value: 3.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAkttehTRTERQVLEHIRQSPFLVtLHYAFQTETKLHLILDYI 134
Cdd:cd14104   8 LGRGQFGIVHRCVETS---SKKTYMAKFVKVKGADQVL-----VKKEISILNIARHRNILR-LHESFESHEELVMIFEFI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLS-QRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS--NGHVVLTDFGLSKEFV-ADETERA 210
Cdd:cd14104  79 SGVDIFERITtARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTrrGSYIKIIEFGQSRQLKpGDKFRLQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 YSfcgTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFtvDGEKNSQAEisRRILKSEPPYPQE----MSALA 286
Cdd:cd14104 159 YT---SAEFYAPEVHQHESVS--TATDMWSLGCLVYVLLSGINPF--EAETNQQTI--ENIRNAEYAFDDEafknISIEA 229
                       250
                ....*....|....*.
gi 32528297 287 KDLIQRLLMKDPKKRL 302
Cdd:cd14104 230 LDFVDRLLVKERKSRM 245
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
430-548 4.41e-21

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 93.14  E-value: 4.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRM----EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd14183  12 RTIGDGNFAVVKECVERSTGREYALKIINKSKcrgkEHMIQNEVSILRRVK-HPNIVLLIEEMDMPTELYLVMELVKGGD 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14183  91 LFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPE 133
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
55-277 5.00e-21

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 94.10  E-value: 5.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAkttEHTRTERQVLEHIRQSPfLVTLhYAFQTETKLH---LIL 131
Cdd:cd13988   1 LGQGATANVFRGRH---KKTGDLYAVKVFNNLSFMRPL---DVQMREFEVLKKLNHKN-IVKL-FAIEEELTTRhkvLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQRER---FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL--LDSNGHVV--LTDFGLSKEFva 204
Cdd:cd13988  73 ELCPCGSLYTVLEEPSNaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSVykLTDFGAAREL-- 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGG--DSGHDKA----VDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPP 277
Cdd:cd13988 151 EDDEQFVSLYGTEEYLHPDMYERAvlRKDHQKKygatVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPS 229
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
61-301 5.18e-21

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 92.67  E-value: 5.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  61 GKVFLVRKISGHDTGKLYAMKVlkkatIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDYINGGELF 140
Cdd:cd14110  14 GRFSVVRQCEEKRSGQMLAAKI-----IPYKPEDKQLVLREYQVLRRLSH-PRIAQLHSAYLSPRHLVLIEELCSGPELL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 141 THLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYM 220
Cdd:cd14110  88 YNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYVETM 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 221 APDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQeMSALAKDLIQRLLMKDPKK 300
Cdd:cd14110 168 APELLEG--QGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCYAG-LSGGAVNFLKSTLCAKPWG 244

                .
gi 32528297 301 R 301
Cdd:cd14110 245 R 245
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
432-548 5.72e-21

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 92.93  E-value: 5.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIskRME-------ANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGg 504
Cdd:cd07829   7 LGEGTYGVVYKAKDKKTGEIVALKKI--RLDneeegipSTALREISLLKELK-HPNIVKLLDVIHTENKLYLVFEYCDQ- 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 505 ELFERIKKK-KHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07829  83 DLKKYLDKRpGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQ 127
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
49-301 5.93e-21

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 92.62  E-value: 5.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVrkISGHDTGKLyAMKVLKK----ATIVQKaktteHTRTERQVLEHIRQsPFLVTLHYAFQTE 124
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLA--TSQKYCCKV-AIKIVDRrrasPDFVQK-----FLPRELSILRRVNH-PNIVQMFECIEVA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG-HVVLTDFGLSKeFV 203
Cdd:cd14164  73 NGRLYIVMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFAR-FV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCGTIEYMAPDIVRGgdSGHD-KAVDWWSLGVLMYELLTGASPFTVDgeknsqaeISRRILKSEPP--YPQ 280
Cdd:cd14164 152 EDYPELSTTFCGSRAYTPPEVILG--TPYDpKKYDVWSLGVVLYVMVTGTMPFDET--------NVRRLRLQQRGvlYPS 221
                       250       260
                ....*....|....*....|...
gi 32528297 281 EMSAL--AKDLIQRLLMKDPKKR 301
Cdd:cd14164 222 GVALEepCRALIRTLLQFNPSTR 244
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
48-302 6.41e-21

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 92.95  E-value: 6.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATIVQKAKTTehTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd07860   1 NFQKVEKIGEGTYGVVY---KARNKLTGEVVALKKIRLDTETEGVPST--AIREISLLKELNH-PNIVKLLDVIHTENKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGG-ELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAde 206
Cdd:cd07860  75 YLVFEFLHQDlKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGV-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSF-CGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRI----------LKSE 275
Cdd:cd07860 153 PVRTYTHeVVTLWYRAPEILLGCKY-YSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLgtpdevvwpgVTSM 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 32528297 276 PPY--------PQEMSAL-------AKDLIQRLLMKDPKKRL 302
Cdd:cd07860 232 PDYkpsfpkwaRQDFSKVvppldedGRDLLSQMLHYDPNKRI 273
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
49-255 7.11e-21

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 93.24  E-value: 7.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKAtivqkAKTTEHTRTERQVLEHIRQSPFLVTLHYAF------Q 122
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVK---TGQLAAIKVMDVT-----GDEEEEIKQEINMLKKYSHHRNIATYYGAFikknppG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGGELfTHLSQRER---FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd06637  80 MDDQLWLVMEFCGAGSV-TDLIKNTKgntLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVS 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KEFvaDET-ERAYSFCGTIEYMAPDIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd06637 159 AQL--DRTvGRRNTFIGTPYWMAPEVIacdENPDATYDFKSDLWSLGITAIEMAEGAPPL 216
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
432-548 7.97e-21

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 92.23  E-value: 7.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT-----QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd14097   9 LGQGSFGVVIEATHKETQTKWAIKKINREKAGSSavkllEREVDILKHVN-HAHIIHLEEVFETPKRMYLVMELCEDGEL 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14097  88 KELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLE 129
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
46-319 9.08e-21

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 92.99  E-value: 9.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKatiVQKAKTtehtRTERQVLEHIRQSPFLVTLHYAFQTET 125
Cdd:cd14132  17 QDDYEIIRKIGRGKYSEVFEGINI---GNNEKVVIKVLKP---VKKKKI----KREIKILQNLRGGPNIVKLLDVVKDPQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLH--LILDYINGgELFTHLsqRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH-VVLTDFGLSkEF 202
Cdd:cd14132  87 SKTpsLIFEYVNN-TDFKTL--YPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLA-EF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETEraYSF-CGTIEYMAPDI-VRGGDsgHDKAVDWWSLGVLMYELLTGASPFtVDGEKNS----------------- 263
Cdd:cd14132 163 YHPGQE--YNVrVASRYYKGPELlVDYQY--YDYSLDMWSLGCMLASMIFRKEPF-FHGHDNYdqlvkiakvlgtddlya 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 264 -----QAEISRRILKSEPPYPQEM-------------SALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd14132 238 yldkyGIELPPRLNDILGRHSKKPwerfvnsenqhlvTPEALDLLDKLLRYDHQERI-----TAKEAMQHPYFD 306
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
432-548 1.09e-20

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 91.99  E-value: 1.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT---------QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd14195  13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSrrgvsreeiEREVNILREIQ-HPNIITLHDIFENKTDVVLILELVS 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14195  92 GGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPE 137
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
47-318 1.31e-20

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 92.10  E-value: 1.31e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVL---KKATIVQKAKTTEhTRTERQvLEHIRqspfLVTLHYAFQT 123
Cdd:cd07846   1 EKYENLGLVGEGSYG---MVMKCRHKETGQIVAIKKFlesEDDKMVKKIAMRE-IKMLKQ-LRHEN----LVNLIEVFRR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINggelFTHLSQRERF----TEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd07846  72 KKRWYLVFEFVD----HTVLDDLEKYpnglDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KeFVADETERAYSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISR---------- 269
Cdd:cd07846 148 R-TLAAPGEVYTDYVATRWYRAPELLV-GDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKclgnliprhq 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 270 RILKSEPP------------------YPQeMSALAKDLIQRLLMKDPKKRLGCGprdadEIKEHLFF 318
Cdd:cd07846 226 ELFQKNPLfagvrlpevkeveplerrYPK-LSGVVIDLAKKCLHIDPDKRPSCS-----ELLHHEFF 286
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
47-318 1.50e-20

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 93.19  E-value: 1.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVflvrkISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFL-----VTLHYAF 121
Cdd:cd07878  15 ERYQNLTPVGSGAYGSV-----CSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIglldvFTPATSI 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYInGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd07878  90 ENFNEVYLVTNLM-GADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fvADETERAYsfCGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPF-------------TVDGEKNSQ---- 264
Cdd:cd07878 168 --ADDEMTGY--VATRWYRAPEIMLNW-MHYNQTVDIWSVGCIMAELLKGKALFpgndyidqlkrimEVVGTPSPEvlkk 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 265 --AEISRRILKSEPPYPQE--------MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07878 243 isSEHARKYIQSLPHMPQQdlkkifrgANPLAIDLLEKMLVLDSDKRI-----SASEALAHPYF 301
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
47-259 1.57e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 91.63  E-value: 1.57e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd14147   3 QELRLEEVIGIGGFGKVY-----RGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAH-PNIIALKAVCLEEPN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQReRFTEHEVQIYVGEIVLALEHLHK---LGIIYRDIKLENILLDSNG------HVVL--TD 195
Cdd:cd14147  77 LCLVMEYAAGGPLSRALAGR-RVPPHVLVNWAVQIARGMHYLHCealVPVIHRDLKSNNILLLQPIenddmeHKTLkiTD 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 196 FGLSKEFvadETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFT-VDG 259
Cdd:cd14147 156 FGLAREW---HKTTQMSAAGTYAWMAPEVIKA--STFSKGSDVWSFGVLLWELLTGEVPYRgIDC 215
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
42-259 1.63e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 91.64  E-value: 1.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  42 EKVGIENFELLKVLGTGAYGKVFlvRKISGhdtGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAF 121
Cdd:cd14145   1 LEIDFSELVLEEIIGIGGFGKVY--RAIWI---GDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKH-PNIIALRGVC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQReRFTEHEVQIYVGEIVLALEHLHKLGI---IYRDIKLENILLD--------SNGH 190
Cdd:cd14145  75 LKEPNLCLVMEFARGGPLNRVLSGK-RIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILekvengdlSNKI 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 191 VVLTDFGLSKEFvadETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFT-VDG 259
Cdd:cd14145 154 LKITDFGLAREW---HRTTKMSAAGTYAWMAPEVIRS--SMFSKGSDVWSYGVLLWELLTGEVPFRgIDG 218
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
114-319 1.86e-20

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 92.02  E-value: 1.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 114 LVTLHYAFQTETKLHLILDYINGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVL 193
Cdd:cd06658  81 VVDMYNSYLVGDELWVVMEFLEGGAL-TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKL 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 194 TDFGLSKEfVADETERAYSFCGTIEYMAPDIVRGGDSGHDkaVDWWSLGVLMYELLTGASPFTvdGEKNSQAeiSRRILK 273
Cdd:cd06658 160 SDFGFCAQ-VSKEVPKRKSLVGTPYWMAPEVISRLPYGTE--VDIWSLGIMVIEMIDGEPPYF--NEPPLQA--MRRIRD 232
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 274 SEPPYPQEM---SALAKDLIQRLLMKDPKKRlgcgpRDADEIKEHLFFQ 319
Cdd:cd06658 233 NLPPRVKDShkvSSVLRGFLDLMLVREPSQR-----ATAQELLQHPFLK 276
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
55-301 2.22e-20

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 91.03  E-value: 2.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKkativqkaktTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd13991  14 IGRGSFGEVHRMEDKQ---TGFQCAVKKVR----------LEVFRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG-HVVLTDFGLSKEF----VADETER 209
Cdd:cd13991  81 EGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLdpdgLGKSLFT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 AYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTvdgeknsQAEISRRILK--SEPP----YPQEMS 283
Cdd:cd13991 161 GDYIPGTETHMAPEVVLG--KPCDAKVDVWSSCCMMLHMLNGCHPWT-------QYYSGPLCLKiaNEPPplreIPPSCA 231
                       250
                ....*....|....*...
gi 32528297 284 ALAKDLIQRLLMKDPKKR 301
Cdd:cd13991 232 PLTAQAIQAGLRKEPVHR 249
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
432-548 2.59e-20

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 90.75  E-value: 2.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR--MEANTQKEI----TALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhiVQTRQQEHIfsekEILEECN-SPFIVKLYRTFKDKKYLYMLMEYCLGGE 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05572  80 LWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPE 122
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
55-301 2.60e-20

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 91.18  E-value: 2.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVqkaKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH------ 128
Cdd:cd14038   2 LGTGGFGNVLRWIN---QETGEQVAIKQCRQELSP---KNRERWCLEIQIMKRLNH-PNVVAARDVPEGLQKLApndlpl 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRER---FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV---LTDFGLSKEF 202
Cdd:cd14038  75 LAMEYCQGGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLihkIIDLGYAKEL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 vaDETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPF-----TVDGEKNSQAEISRRILKSEP- 276
Cdd:cd14038 155 --DQGSLCTSFVGTLQYLAPELLE--QQKYTVTVDYWSFGTLAFECITGFRPFlpnwqPVQWHGKVRQKSNEDIVVYEDl 230
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 32528297 277 ----------PYPQEMSA-LAKDL---IQRLLMKDPKKR 301
Cdd:cd14038 231 tgavkfssvlPTPNNLNGiLAGKLerwLQCMLMWHPRQR 269
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
55-320 2.65e-20

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 91.24  E-value: 2.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd06657  28 IGEGSTGIVCIATVKS---SGKLVAVKKMD----LRKQQRRELLFNEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVADETERAYSFC 214
Cdd:cd06657 100 EGGAL-TDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQ-VSKEVPRRKSLV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 215 GTIEYMAPDIVRGGDSGHDkaVDWWSLGVLMYELLTGASPFTVDGEKNSQAEIsRRILKSEPPYPQEMSALAKDLIQRLL 294
Cdd:cd06657 178 GTPYWMAPELISRLPYGPE--VDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI-RDNLPPKLKNLHKVSPSLKGFLDRLL 254
                       250       260
                ....*....|....*....|....*.
gi 32528297 295 MKDPKKRlgcgpRDADEIKEHLFFQK 320
Cdd:cd06657 255 VRDPAQR-----ATAAELLKHPFLAK 275
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
47-318 2.77e-20

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 91.28  E-value: 2.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKKAT---IVQKAKTTEhTRTERQvLEHirqsPFLVTLHYAFQT 123
Cdd:cd07847   1 EKYEKLSKIGEGSYGVVFKCRNR---ETGQIVAIKKFVESEddpVIKKIALRE-IRMLKQ-LKH----PNLVNLIEVFRR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINggelFTHLSQRERFT----EHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd07847  72 KRKLHLVFEYCD----HTVLNELEKNPrgvpEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KefVADETERAYS-FCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEP-- 276
Cdd:cd07847 148 R--ILTGPGDDYTdYVATRWYRAPELLV-GDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIPrh 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 277 ---------------PYPQEM----------SALAKDLIQRLLMKDPKKRLGCgprdaDEIKEHLFF 318
Cdd:cd07847 225 qqifstnqffkglsiPEPETRepleskfpniSSPALSFLKGCLQMDPTERLSC-----EELLEHPYF 286
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
53-301 3.83e-20

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 90.42  E-value: 3.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRkisGHDTGKLYAMKVLkkatIVQKAKTTEHTRTERQVLEHIRQSPFLVTL--HYAFQTETKLH-- 128
Cdd:cd14037   9 KYLAEGGFAHVYLVK---TSNGGNRAALKRV----YVNDEHDLNVCKREIEIMKRLSGHKNIVGYidSSANRSGNGVYev 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 -LILDYINGGELFTHLSQR--ERFTEHEV-QIY--VGEIVLALEHLhKLGIIYRDIKLENILLDSNGHVVLTDFG----- 197
Cdd:cd14037  82 lLLMEYCKGGGVIDLMNQRlqTGLTESEIlKIFcdVCEAVAAMHYL-KPPLIHRDLKVENVLISDSGNYKLCDFGsattk 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 -------LSKEFVADETERaYSfcgTIEYMAPDIVR--GGDSGHDKAvDWWSLGVLMYELLTGASPFtvdGEKNSQAeis 268
Cdd:cd14037 161 ilppqtkQGVTYVEEDIKK-YT---TLQYRAPEMIDlyRGKPITEKS-DIWALGCLLYKLCFYTTPF---EESGQLA--- 229
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32528297 269 rrILKSE---PPYPQEMSALaKDLIQRLLMKDPKKR 301
Cdd:cd14037 230 --ILNGNftfPDNSRYSKRL-HKLIRYMLEEDPEKR 262
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
420-548 4.46e-20

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 89.95  E-value: 4.46e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 420 YQHYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN---TQKEITALKLCEgHPNIVKLHEVFHDQLHTFL 496
Cdd:cd14114   1 YDHYDIL---EELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDketVRKEIQIMNQLH-HPKLINLHDAFEDDNEMVL 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 497 VMELLNGGELFERIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14114  77 ILEFLSGGELFERIAAEHYkMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPE 129
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
433-548 9.27e-20

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 88.85  E-value: 9.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 433 GEGSFSICRKCVHKKSNQAFAVKIISKRM------EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd05578   9 GKGSFGKVCIVQKKDTKKMFAMKYMNKQKciekdsVRNVLNELEILQELE-HPFLVNLWYSFQDEEDMYMVVDLLLGGDL 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05578  88 RYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPD 129
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
49-247 1.03e-19

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 89.40  E-value: 1.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKIsgHDTGKLYAMKVLKKATivQKAKTTEHTRTERQVLEHIRQ--SPFLVTLHYAFQTETK 126
Cdd:cd14052   2 FANVELIGSGEFSQVYKVSER--VPTGKVYAVKKLKPNY--AGAKDRLRRLEEVSILRELTLdgHDNIVQLIDSWEYHGH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGEL---FTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV 203
Cdd:cd14052  78 LYIQTELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWP 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 32528297 204 ADET-ERAysfcGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYE 247
Cdd:cd14052 158 LIRGiERE----GDREYIAPEILSEHM--YDKPADIFSLGLILLE 196
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
47-254 1.08e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 90.11  E-value: 1.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKAtiVQKAKTTEHTRtERQVLeHIRQSPFLVTLHYAFQTETK 126
Cdd:cd06650   5 DDFEKISELGAGNGGVVF---KVSHKPSGLVMARKLIHLE--IKPAIRNQIIR-ELQVL-HECNSPYIVGFYGAFYSDGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEH---EVQIYVGEIVLALEHLHKlgIIYRDIKLENILLDSNGHVVLTDFGLSKEFV 203
Cdd:cd06650  78 ISICMEHMDGGSLDQVLKKAGRIPEQilgKVSIAVIKGLTYLREKHK--IMHRDVKPSNILVNSRGEIKLCDFGVSGQLI 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 204 adeTERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASP 254
Cdd:cd06650 156 ---DSMANSFVGTRSYMSPERLQG--THYSVQSDIWSMGLSLVEMAVGRYP 201
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
47-317 1.10e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 88.93  E-value: 1.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLK-----KATIVQK----AKTTEHTRterqvlehirqspfLVTL 117
Cdd:cd06646   9 HDYELIQRVGSGTYGDVYKARNLH---TGELAAVKIIKlepgdDFSLIQQeifmVKECKHCN--------------IVAY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 118 HYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd06646  72 FGSYLSREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEFVADETERAySFCGTIEYMAPDIVR-GGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILksEP 276
Cdd:cd06646 152 VAAKITATIAKRK-SFIGTPYWMAPEVAAvEKNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNF--QP 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 32528297 277 PYPQEM---SALAKDLIQRLLMKDPKKRlgcgpRDADEIKEHLF 317
Cdd:cd06646 229 PKLKDKtkwSSTFHNFVKISLTKNPKKR-----PTAERLLTHLF 267
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
418-548 1.12e-19

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 89.21  E-value: 1.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 418 PFYQHYDLDLKDkpLGEGSFSICRKCVHKKSNQAFAVKIISKRM-----EANTQKEITALKLCEGHPNIVKLHEVFHDQL 492
Cdd:cd14198   4 NFNNFYILTSKE--LGRGKFAVVRQCISKSTGQEYAAKFLKKRRrgqdcRAEILHEIAVLELAKSNPRVVNLHEVYETTS 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32528297 493 HTFLVMELLNGGELFERI--KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14198  82 EIILILEYAAGGEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQ 139
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
46-319 1.38e-19

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 89.73  E-value: 1.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMK--------------VLKKATIVQKAKTTEHTRTERQVLEHIRQS 111
Cdd:cd07845   6 VTEFEKLNRIGEGTYGIVYRARDT---TSGEIVALKkvrmdnerdgipisSLREITLLLNLRHPNIVELKEVVVGKHLDS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 112 PFLVtLHYAfqtETKLHLILDyinggelfthlSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHV 191
Cdd:cd07845  83 IFLV-MEYC---EQDLASLLD-----------NMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 192 VLTDFGLSKEF---VADETERAYsfcgTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTVDGEKN------ 262
Cdd:cd07845 148 KIADFGLARTYglpAKPMTPKVV----TLWYRAPELLLGCTT-YTTAIDMWAVGCILAELLAHKPLLPGKSEIEqldlii 222
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 263 --------------SQAEISRRILKSEPPY---PQEMSALAK---DLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd07845 223 qllgtpnesiwpgfSDLPLVGKFTLPKQPYnnlKHKFPWLSEaglRLLNFLLMYDPKKRA-----TAEEALESSYFK 294
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
49-301 1.54e-19

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 88.89  E-value: 1.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAmkvLKKATIVQKAKTTEhtrTERQVLEHIR-QSPFLVTL-HYAFQTETK 126
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLS---TGRLYA---LKKILCHSKEDVKE---AMREIENYRLfNHPNILRLlDSQIVKEAG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 ----LHLILDYINGGELFTHLSQR----ERFTEHEVQIYVGEIVLALEHLHKL---GIIYRDIKLENILLDSNGHVVLTD 195
Cdd:cd13986  73 gkkeVYLLLPYYKRGSLQDEIERRlvkgTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 196 FG---LSKEFV-----ADETERAYSFCGTIEYMAPDI--VRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKN--- 262
Cdd:cd13986 153 LGsmnPARIEIegrreALALQDWAAEHCTMPYRAPELfdVKSH-CTIDEKTDIWSLGCTLYALMYGESPFERIFQKGdsl 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 32528297 263 SQAEISRRI-LKSEPPYPQEMsalaKDLIQRLLMKDPKKR 301
Cdd:cd13986 232 ALAVLSGNYsFPDNSRYSEEL----HQLVKSMLVVNPAER 267
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
47-318 1.55e-19

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 88.05  E-value: 1.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISGHDT----GKLYAMKVLkkativqkAKTTEHTR--TERQVLEHIRQSPFLVTLHYA 120
Cdd:cd14019   1 NKYRIIEKIGEGTFSSVYKAEDKLHDLYdrnkGRLVALKHI--------YPTSSPSRilNELECLERLGGSNNVSGLITA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 121 FQTETKLHLILDYinggelFTHLSQRERFTE---HEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS-NGHVVLTDF 196
Cdd:cd14019  73 FRNEDQVVAVLPY------IEHDDFRDFYRKmslTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNReTGKGVLVDF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 197 GLSkEFVADETERAYSFCGTIEYMAPDIV-RGGDSGhdKAVDWWSLGVLMYELLTGA-SPFTVDGEKNSQAEIsrrilks 274
Cdd:cd14019 147 GLA-QREEDRPEQRAPRAGTRGFRAPEVLfKCPHQT--TAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEI------- 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 275 eppypqeMS----ALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14019 217 -------ATifgsDEAYDLLDKLLELDPSKRI-----TAEEALKHPFF 252
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
55-263 1.70e-19

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 88.48  E-value: 1.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisghDTGKLYAMKVLKkativQKAKTTEHT--RTERQVLEHIRQSPFLVTLHYAFQTETKLhLILD 132
Cdd:cd14066   1 IGSGGFGTVYKGVL----ENGTVVAVKRLN-----EMNCAASKKefLTELEMLGRLRHPNLVRLLGYCLESDEKL-LVYE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRERFTEHEVQ----IYVGeIVLALEHLH---KLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV-A 204
Cdd:cd14066  71 YMPNGSLEDRLHCHKGSPPLPWPqrlkIAKG-IARGLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPpS 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGGDSghDKAVDWWSLGVLMYELLTGASPFTVDGEKNS 263
Cdd:cd14066 150 ESVSKTSAVKGTIGYLAPEYIRTGRV--STKSDVYSFGVVLLELLTGKPAVDENRENAS 206
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
49-318 2.03e-19

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 88.04  E-value: 2.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVlkkatIVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLh 128
Cdd:cd14108   4 YDIHKEIGRGAFS---YLRRVKEKSSDLSFAAKF-----IPVRAKKKTSARRELALLAEL-DHKSIVRFHDAFEKRRVV- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG--HVVLTDFGLSKEFVADE 206
Cdd:cd14108  74 IIVTELCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TEraYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALA 286
Cdd:cd14108 154 PQ--YCKYGTPEFVAPEIV--NQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREA 229
                       250       260       270
                ....*....|....*....|....*....|..
gi 32528297 287 KDLIQRLLMKDPKKrlgcgpRDADEIKEHLFF 318
Cdd:cd14108 230 KGFIIKVLVSDRLR------PDAEETLEHPWF 255
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
49-355 2.53e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 89.15  E-value: 2.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvrKISGHDTGKLYAmkvLKK-------ATIVQkakttehtRTERQV--LEHIRQSPFLVTLHY 119
Cdd:cd07852   9 YEILKKLGKGAYGIVW---KAIDKKTGEVVA---LKKifdafrnATDAQ--------RTFREImfLQELNDHPNIIKLLN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 AFQTETK--LHLILDYINggelfTHLSQ--RERFTEhEVQ----IYvgEIVLALEHLHKLGIIYRDIKLENILLDSNGHV 191
Cdd:cd07852  75 VIRAENDkdIYLVFEYME-----TDLHAviRANILE-DIHkqyiMY--QLLKALKYLHSGGVIHRDLKPSNILLNSDCRV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 192 VLTDFGLSKEFVADETERAYS----FCGTIEYMAPDIVRGgdSGH-DKAVDWWSLGVLMYELLTGASPF----TVDG--- 259
Cdd:cd07852 147 KLADFGLARSLSQLEEDDENPvltdYVATRWYRAPEILLG--STRyTKGVDMWSVGCILGEMLLGKPLFpgtsTLNQlek 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 260 -----EKNSQAEIS-----------RRILKSEPPYPQEM----SALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd07852 225 iieviGRPSAEDIEsiqspfaatmlESLPPSRPKSLDELfpkaSPDALDLLKKLLVFNPNKRL-----TAEEALRHPYVA 299
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 32528297 320 KI-NWDDLAAKkvPAPFKPVIRDE--LDVSNFAEEFTEM 355
Cdd:cd07852 300 QFhNPADEPSL--PGPIVIPLDDNkkLTVDEYRNRLYEE 336
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
49-301 2.53e-19

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 87.36  E-value: 2.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTTEHTRTERqvLEHIRQSPFLVTLHYAFQTETKLH 128
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRS---REDGKLYAVKRSRSRFRGEKDRKRKLEEVER--HEKLGEHPNCVRFIKAWEEKGILY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYInGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGL----SKEFVA 204
Cdd:cd14050  78 IQTELC-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLvvelDKEDIH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETEraysfcGTIEYMAPDIVRGGDSghdKAVDWWSLGVLMYELLTgaspftvDGEKNSQAEISRRILKSEPPYP--QEM 282
Cdd:cd14050 157 DAQE------GDPRYMAPELLQGSFT---KAADIFSLGITILELAC-------NLELPSGGDGWHQLRQGYLPEEftAGL 220
                       250
                ....*....|....*....
gi 32528297 283 SALAKDLIQRLLMKDPKKR 301
Cdd:cd14050 221 SPELRSIIKLMMDPDPERR 239
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
423-548 2.70e-19

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 87.45  E-value: 2.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 423 YDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRM--EANTQK---EITALKLCEgHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd14071   2 YDIE---RTIGKGNFAVVKLARHRITKTEVAIKIIDKSQldEENLKKiyrEVQIMKMLN-HPHIIKLYQVMETKDMLYLV 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14071  78 TEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAE 128
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
430-548 2.74e-19

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 87.58  E-value: 2.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRM--EANTQK---EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd14072   6 KTIGKGNFAKVKLARHVLTGREVAIKIIDKTQlnPSSLQKlfrEVRIMKILN-HPNIVKLFEVIETEKTLYLVMEYASGG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14072  85 EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAE 128
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
54-259 2.85e-19

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 87.79  E-value: 2.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDY 133
Cdd:cd14146   1 IIGVGGFGKVY-----RATWKGQEVAVKAARQDPDEDIKATAESVRQEAKLFSMLRH-PNIIKLEGVCLEEPNLCLVMEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHLS---------QRERFTEHEVQIYVGEIVLALEHLHK---LGIIYRDIKLENILL------DSNGHVVL-- 193
Cdd:cd14146  75 ARGGTLNRALAaanaapgprRARRIPPHILVNWAVQIARGMLYLHEeavVPILHRDLKSSNILLlekiehDDICNKTLki 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 194 TDFGLSKEFvadETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFT-VDG 259
Cdd:cd14146 155 TDFGLAREW---HRTTKMSAAGTYAWMAPEVIK--SSLFSKGSDIWSYGVLLWELLTGEVPYRgIDG 216
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
432-548 3.16e-19

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 87.42  E-value: 3.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKK-SNQAFAVKIISKRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd14120   1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQnllgKEIKILKELS-HENVVALLDCQETSSSVYLVMEYCNGGDL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14120  80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQ 121
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
47-283 3.17e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 88.95  E-value: 3.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKkatIVQKAKTTEHTRTERQVLeHIRQSPFLVTLHYAFQTETK 126
Cdd:cd06649   5 DDFERISELGAGNGG---VVTKVQHKPSGLIMARKLIH---LEIKPAIRNQIIRELQVL-HECNSPYIVGFYGAFYSDGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEH---EVQIYVGEIVLALEHLHKlgIIYRDIKLENILLDSNGHVVLTDFGLSKEFV 203
Cdd:cd06649  78 ISICMEHMDGGSLDQVLKEAKRIPEEilgKVSIAVLRGLAYLREKHQ--IMHRDVKPSNILVNSRGEIKLCDFGVSGQLI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 adeTERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMS 283
Cdd:cd06649 156 ---DSMANSFVGTRSYMSPERLQG--THYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSIS 230
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
430-546 3.20e-19

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 87.27  E-value: 3.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKII---SKRMEANTqKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd06614   6 EKIGEGASGEVYKATDRATGKEVAIKKMrlrKQNKELII-NEILIMKECK-HPNIVDYYDSYLVGDELWVVMEYMDGGSL 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 507 FERI-KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06614  84 TDIItQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIK 124
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
160-318 3.36e-19

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 87.71  E-value: 3.36e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 160 EIVLALEHLHKLGIIYRDIKLENILLD-----SNGHVVLTDFGLSKEFVADETE--RAYSFCGTIEYMAPDIVRGGDSGH 232
Cdd:cd13982 107 QIASGLAHLHSLNIVHRDLKPQNILIStpnahGNVRAMISDFGLCKKLDVGRSSfsRRSGVAGTSGWIAPEMLSGSTKRR 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 233 -DKAVDWWSLGVLMYELLTGAS-PF--TVDGEKNsqaeisrrILKSEPPYPQ-----EMSALAKDLIQRLLMKDPKKRlg 303
Cdd:cd13982 187 qTRAVDIFSLGCVFYYVLSGGShPFgdKLEREAN--------ILKGKYSLDKllslgEHGPEAQDLIERMIDFDPEKR-- 256
                       170
                ....*....|....*
gi 32528297 304 cgPrDADEIKEHLFF 318
Cdd:cd13982 257 --P-SAEEVLNHPFF 268
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
432-548 3.88e-19

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 86.94  E-value: 3.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ-KEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERI 510
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQaAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 32528297 511 KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14115  81 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPE 118
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
49-255 4.16e-19

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 87.99  E-value: 4.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVlkkatIVQKAKTTEHTRTERQVLEHIRQ-----SPFLVTLHYAFQ- 122
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLD---HKTGQLVAIKI-----IRNKKRFHQQALVEVKILKHLNDndpddKHNIVRYKDSFIf 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 -------TEtklhlILDyINggeLFTHLSQR--ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH--V 191
Cdd:cd14210  87 rghlcivFE-----LLS-IN---LYELLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssI 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 192 VLTDFGLSkefvADETERAYSFcgtIE---YMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd14210 158 KVIDFGSS----CFEGEKVYTY---IQsrfYRAPEVILG--LPYDTAIDMWSLGCILAELYTGYPLF 215
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
47-322 4.41e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 87.63  E-value: 4.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATIVQkakttehtrTERQVLEHIR-----QSPFLVTLHYAF 121
Cdd:cd06619   1 QDIQYQEILGHGNGGTVY---KAYHLLTRRILAVKVIPLDITVE---------LQKQIMSELEilykcDSPYIIGFYGAF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHlsqrERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd06619  69 FVENRISICTEFMDGGSLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVadeTERAYSFCGTIEYMAPDIVRGGDSGHDKAVdwWSLGVLMYELLTGASPF-TVDGEKNS--QAEISRRILKSEPPY 278
Cdd:cd06619 145 LV---NSIAKTYVGTNAYMAPERISGEQYGIHSDV--WSLGISFMELALGRFPYpQIQKNQGSlmPLQLLQCIVDEDPPV 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 279 --PQEMSALAKDLIQRLLMKDPKKRLGcgprdADEIKEHLFFQKIN 322
Cdd:cd06619 220 lpVGQFSEKFVHFITQCMRKQPKERPA-----PENLMDHPFIVQYN 260
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
47-357 6.38e-19

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 88.17  E-value: 6.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVflvrkISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPfLVTLHYAFQTETK 126
Cdd:cd07877  17 ERYQNLSPVGSGAYGSV-----CAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHEN-VIGLLDVFTPARS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LH-----LILDYINGGELfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd07877  91 LEefndvYLVTHLMGADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARH 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fVADETEraySFCGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPF-----------------TVDGE--KN 262
Cdd:cd07877 170 -TDDEMT---GYVATRWYRAPEIMLNW-MHYNQTVDIWSVGCIMAELLTGRTLFpgtdhidqlklilrlvgTPGAEllKK 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 263 SQAEISRRILKSEPPYPQEMSA--------LAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQKinWDDLAAKKVPAP 334
Cdd:cd07877 245 ISSESARNYIQSLTQMPKMNFAnvfiganpLAVDLLEKMLVLDSDKRI-----TAAQALAHAYFAQ--YHDPDDEPVADP 317
                       330       340
                ....*....|....*....|....*...
gi 32528297 335 FKPVIRD-ELDVSNFA----EEFTEMDP 357
Cdd:cd07877 318 YDQSFESrDLLIDEWKsltyDEVISFVP 345
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
54-255 7.71e-19

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 86.19  E-value: 7.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDY 133
Cdd:cd14148   1 IIGVGGFGKVY-----KGLWRGEEVAVKAARQDPDEDIAVTAENVRQEARLFWMLQH-PNIIALRGVCLNPPHLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHLSQReRFTEHEVQIYVGEIVLALEHLHK---LGIIYRDIKLENILLD--------SNGHVVLTDFGLSKEF 202
Cdd:cd14148  75 ARGGALNRALAGK-KVPPHVLVNWAVQIARGMNYLHNeaiVPIIHRDLKSSNILILepienddlSGKTLKITDFGLAREW 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 203 vadETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd14148 154 ---HKTTKMSAAGTYAWMAPEVIR--LSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
55-303 8.47e-19

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 86.89  E-value: 8.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisgHDTGKLYAMKVLKkatIVQKAKTTEHTRTERQVLEHIRQSPFL----VTLHYAFQTETKLHLI 130
Cdd:cd14039   1 LGTGGFGNVCLYQN---QETGEKIAIKSCR---LELSVKNKDRWCHEIQIMKKLNHPNVVkacdVPEEMNFLVNDVPLLA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQRER---FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL-DSNGHVV--LTDFGLSKEFva 204
Cdd:cd14039  75 MEYCSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIVhkIIDLGYAKDL-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEisrRILKSEP-------- 276
Cdd:cd14039 153 DQGSLCTSFVGTLQYLAPELFEN--KSYTVTVDYWSFGTMVFECIAGFRPFLHNLQPFTWHE---KIKKKDPkhifavee 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 32528297 277 -----------PYPQEMSALAKD----LIQRLLMKDPKKRLG 303
Cdd:cd14039 228 mngevrfsthlPQPNNLCSLIVEpmegWLQLMLNWDPVQRGG 269
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
54-301 1.22e-18

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 85.67  E-value: 1.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHTRTERQV-----LEHIRQSPFLVTLHYAFQTETKLH 128
Cdd:cd14101   7 LLGKGGFGTVYAGHRIS---DGLQVAIKQISRNRVQQWSKLPGVNPVPNEVallqsVGGGPGHRGVIRLLDWFEIPEGFL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDY-INGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS-NGHVVLTDFGlSKEFVADE 206
Cdd:cd14101  84 LVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLrTGDIKLIDFG-SGATLKDS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TeraYS-FCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEknsqaeisrrILKSEPPYPQEMSAL 285
Cdd:cd14101 163 M---YTdFDGTRVYSPPEWIL-YHQYHALPATVWSLGILLYDMVCGDIPFERDTD----------ILKAKPSFNKRVSND 228
                       250
                ....*....|....*.
gi 32528297 286 AKDLIQRLLMKDPKKR 301
Cdd:cd14101 229 CRSLIRSCLAYNPSDR 244
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
54-301 1.36e-18

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 86.13  E-value: 1.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFLVRKisghdTGKLYAMKVLKKATIVQKAKTTEHT-----------------RTERQVLEHIrQSPFLVT 116
Cdd:cd14000   1 LLGDGGFGSVYRASY-----KGEPVAVKIFNKHTSSNFANVPADTmlrhlratdamknfrllRQELTVLSHL-HHPSIVY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 117 LHYAfqTETKLHLILDYINGGELFTHLSQRER----FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL---LDSNG 189
Cdd:cd14000  75 LLGI--GIHPLMLVLELAPLGSLDHLLQQDSRsfasLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 190 HVV--LTDFGLSKEFVadeTERAYSFCGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEI 267
Cdd:cd14000 153 AIIikIADYGISRQCC---RMGAKGSEGTPGFRAPEIARGNVI-YNEKVDVFSFGMLLYEILSGGAPM----VGHLKFPN 224
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 32528297 268 SRRILKSEPP----YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14000 225 EFDIHGGLRPplkqYECAPWPEVEVLMKKCWKENPQQR 262
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
424-548 1.76e-18

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 85.43  E-value: 1.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAntQKEITALKLCEGHPNIVKLHEVFHDQLHT----FLVME 499
Cdd:cd14172   4 DYKLSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKA--RREVEHHWRASGGPHIVHILDVYENMHHGkrclLIIME 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 500 LLNGGELFERIKKK--KHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14172  82 CMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPE 132
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
430-548 1.92e-18

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 86.60  E-value: 1.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR--MEANTQKEITA--------LKlcegHPNIVKLHEVFHDQLHTFLVME 499
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKaiLKRNEVKHIMAernvllknVK----HPFLVGLHYSFQTKDKLYFVLD 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05575  77 YVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPE 125
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
47-318 2.28e-18

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 85.66  E-value: 2.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKvlKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTL----HYAFQ 122
Cdd:cd07837   1 DAYEKLEKIGEGTYGKVYKARDKN---TGKLVALK--KTRLEMEEEGVPSTALREVSLLQMLSQSIYIVRLldveHVEEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGgELFTHLSQRERFTEHE-----VQIYVGEIVLALEHLHKLGIIYRDIKLENILLD-SNGHVVLTDF 196
Cdd:cd07837  76 GKPLLYLVFEYLDT-DLKKFIDSYGRGPHNPlpaktIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQKGLLKIADL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 197 GLSKEFVADETERAYSFCgTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRI----- 271
Cdd:cd07837 155 GLGRAFTIPIKSYTHEIV-TLWYRAPEVLLGS-THYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLgtpne 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 272 --------LKSEPPYPQ-----------EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07837 233 evwpgvskLRDWHEYPQwkpqdlsravpDLEPEGVDLLTKMLAYDPAKRI-----SAKAALQHPYF 293
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
430-548 2.60e-18

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 85.92  E-value: 2.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFS---ICRKCVHKKSNQAFAVKIISK-----------RMEANTQKEItalklceGHPNIVKLHEVFHDQLHTF 495
Cdd:cd05582   1 KVLGQGSFGkvfLVRKITGPDAGTLYAMKVLKKatlkvrdrvrtKMERDILADV-------NHPFIVKLHYAFQTEGKLY 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 496 LVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05582  74 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPE 126
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
430-548 2.80e-18

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 85.32  E-value: 2.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK------RMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05580   7 KTLGTGSFGRVRLVKHKDSGKYYALKILKKakiiklKQVEHVLNEKRILSEVR-HPFIVNLLGSFQDDRNLYMVMEYVPG 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05580  86 GELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPE 130
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
432-548 3.39e-18

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 84.26  E-value: 3.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSN-QAFAVKIISKR------MEaNTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd14121   3 LGSGTYATVYKAYRKSGArEVVAVKCVSKSslnkasTE-NLLTEIELLKKLK-HPHIVELKDFQWDEEHIYLIMEYCSGG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14121  81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQ 124
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
53-319 3.61e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 85.97  E-value: 3.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEH----------TRTERQVLEHIRQsPFLVTLHYAFQ 122
Cdd:PTZ00024  15 AHLGEGTYGKVEKAYDTL---TGKIVAIKKVKIIEISNDVTKDRQlvgmcgihftTLRELKIMNEIKH-ENIMGLVDVYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  123 TETKLHLILDYINGgELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF 202
Cdd:PTZ00024  91 EGDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRY 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  203 VADETERAYSFCG-------------TIEYMAPDIVRGGDSGHDkAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEI-- 267
Cdd:PTZ00024 170 GYPPYSDTLSKDEtmqrreemtskvvTLWYRAPELLMGAEKYHF-AVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIfe 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297  268 -----------SRRILKSEPPY----PQEMSALAK-------DLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:PTZ00024 249 llgtpnednwpQAKKLPLYTEFtprkPKDLKTIFPnasddaiDLLQSLLKLNPLERI-----SAKEALKHEYFK 317
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
47-336 3.89e-18

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 85.88  E-value: 3.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKA-TIVQKAKttehtRTERQ--VLEHIRQsPFLVTLHYAFQT 123
Cdd:cd07855   5 DRYEPIETIGSGAYGVVCSAIDTK---SGQKVAIKKIPNAfDVVTTAK-----RTLRElkILRHFKH-DNIIAIRDILRP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKL------HLILDYINGgELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd07855  76 KVPYadfkdvYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEFVADETERAY---SFCGTIEYMAPDIVRGGDsGHDKAVDWWSLGVLMYE------LLTGASP-------FTVDGE- 260
Cdd:cd07855 155 MARGLCTSPEEHKYfmtEYVATRWYRAPELMLSLP-EYTQAIDMWSVGCIFAEmlgrrqLFPGKNYvhqlqliLTVLGTp 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 261 -----KNSQAEISRRILKSEPP---------YPQEmSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQKINWDDL 326
Cdd:cd07855 234 sqaviNAIGADRVRRYIQNLPNkqpvpwetlYPKA-DQQALDLLSQMLRFDPSERI-----TVAEALQHPFLAKYHDPDD 307
                       330
                ....*....|
gi 32528297 327 AAKKvPAPFK 336
Cdd:cd07855 308 EPDC-APPFD 316
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
432-548 4.79e-18

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 84.46  E-value: 4.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHK-KSNQAFAVKIISKRMEANTQK----------EITALKLCeGHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd14076   9 LGEGEFGKVKLGWPLpKANHRSGVQVAIKLIRRDTQQencqtskimrEINILKGL-THPNIVRLLDVLKTKKYIGIVLEF 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14076  88 VSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLE 135
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
432-548 4.80e-18

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 84.28  E-value: 4.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHK--KSNQAFAVKIISKRMEANTQKEITALKLCE-------GHPNIVKLHEVFHDQLHTF-LVMELL 501
Cdd:cd13994   1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRDDESKRKDYVKRLTSEyiissklHHPNIVKVLDLCQDLHGKWcLVMEYC 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd13994  81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPE 127
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
48-354 4.85e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 85.53  E-value: 4.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGHDTGKLyamkVLKKAT-IVQKAKTTEHTRTERQVLEHIRQSPFLVTLhyaFQTEtk 126
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNAETSEEETV----AIKKITnVFSKKILAKRALRELKLLRHFRGHKNITCL---YDMD-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 lhlILDYINGGELFTH-------LSQ----RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTD 195
Cdd:cd07857  72 ---IVFPGNFNELYLYeelmeadLHQiirsGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 196 FGLSKEFVADETERA---YSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLtGASPF-----TVD--------- 258
Cdd:cd07857 149 FGLARGFSENPGENAgfmTEYVATRWYRAPEIML-SFQSYTKAIDVWSVGCILAELL-GRKPVfkgkdYVDqlnqilqvl 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 259 GEKNSqaEISRRI--------LKSEPPYPQ--------EMSALAKDLIQRLLMKDPKKRLGCgprdaDEIKEHLFFqkIN 322
Cdd:cd07857 227 GTPDE--ETLSRIgspkaqnyIRSLPNIPKkpfesifpNANPLALDLLEKLLAFDPTKRISV-----EEALEHPYL--AI 297
                       330       340       350
                ....*....|....*....|....*....|...
gi 32528297 323 WDDLAAKKV-PAPFKPVIRDELDVSNFAEEFTE 354
Cdd:cd07857 298 WHDPDDEPVcQKPFDFSFESEDSMEELRDMIIE 330
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
55-301 4.87e-18

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 83.73  E-value: 4.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKATIVQKAKTTEHTRtERQVLEHIrQSPFLVTLHYA-FQTETKLHLILDY 133
Cdd:cd14064   1 IGSGSFGKVY-----KGRCRNKIVAIKRYRANTYCSKSDVDMFCR-EVSILCRL-NHPCVIQFVGAcLDDPSQFAIVTQY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHLSQRERFTEHEVQIYVG-EIVLALEHLHKLG--IIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERA 210
Cdd:cd14064  74 VSGGSLFSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNM 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 YSFCGTIEYMAPDiVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRilKSEPPYPQEMSALAKDLI 290
Cdd:cd14064 154 TKQPGNLRWMAPE-VFTQCTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYH--HIRPPIGYSIPKPISSLL 230
                       250
                ....*....|.
gi 32528297 291 QRLLMKDPKKR 301
Cdd:cd14064 231 MRGWNAEPESR 241
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
54-318 5.44e-18

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 83.81  E-value: 5.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFLvrkisGHDT--GKLYAMKVLKkatiVQKAKTTEHTR--TERQVLEHIrQSPFLVTLHYAFQTETKLHL 129
Cdd:cd13983   8 VLGRGSFKTVYR-----AFDTeeGIEVAWNEIK----LRKLPKAERQRfkQEIEILKSL-KHPNIIKFYDSWESKSKKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 IL--DYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLG--IIYRDIKLENILLD-SNGHVVLTDFGLSKEFva 204
Cdd:cd13983  78 IFitELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLL-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 dETERAYSFCGTIEYMAPDIVrggDSGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRRILKSEPpyPQEMSA 284
Cdd:cd13983 156 -RQSFAKSVIGTPEFMAPEMY---EEHYDEKVDIYAFGMCLLEMATGEYPY---SECTNAAQIYKKVTSGIK--PESLSK 226
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 32528297 285 L----AKDLIQrLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd13983 227 VkdpeLKDFIE-KCLKPPDERP-----SARELLEHPFF 258
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
48-318 8.15e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 84.02  E-value: 8.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFlvrKISGHDTGKLYAmkvLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKL 127
Cdd:cd07839   1 KYEKLEKIGEGTYGTVF---KAKNRETHEIVA---LKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGgELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAde 206
Cdd:cd07839  75 TLVFEYCDQ-DLKKYFdSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGI-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSF-CGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASP--------------FTVDGEKNSQAEISRRI 271
Cdd:cd07839 152 PVRCYSAeVVTLWYRPPDVLFGA-KLYSTSIDMWSAGCIFAELANAGRPlfpgndvddqlkriFRLLGTPTEESWPGVSK 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 272 LKSEPPYPQ------------EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07839 231 LPDYKPYPMypattslvnvvpKLNSTGRDLLQNLLVCNPVQRI-----SAEEALQHPYF 284
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
43-301 8.19e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 84.08  E-value: 8.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  43 KVGIENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkativqkaktTEHTRtERQVLEHIRQSPFLVTLHYA-- 120
Cdd:cd07864   3 KRCVDKFDIIGIIGEGTYGQVY---KAKDKDTGELVALKKVR----------LDNEK-EGFPITAIREIKILRQLNHRsv 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 121 ---------------FQTETK-LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL 184
Cdd:cd07864  69 vnlkeivtdkqdaldFKKDKGaFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNIL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 185 LDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnSQ 264
Cdd:cd07864 149 LNNKGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLL-GEERYGPAIDVWSCGCILGELFTKKPIFQANQEL-AQ 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 265 AEISRRILKSEPP--YP-------------------------QEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd07864 227 LELISRLCGSPCPavWPdviklpyfntmkpkkqyrrrlreefSFIPTPALDLLDHMLTLDPSKR 290
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
43-300 8.33e-18

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 85.43  E-value: 8.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   43 KVGIEN--FELLKVLGTGAYGKVFLvrkisghdtgklyAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYA 120
Cdd:PHA03212  86 RAGIEKagFSILETFTPGAEGFAFA-------------CIDNKTCEHVVIKAGQRGGTATEAHILRAINH-PSIIQLKGT 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  121 FQTETKLHLILDYINGgELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK 200
Cdd:PHA03212 152 FTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAAC 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  201 EFVADETERAYSFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPF----TVDGEKNSQAEIsRRILKSEP 276
Cdd:PHA03212 231 FPVDINANKYYGWAGTIATNAPELLARDPYG--PAVDIWSAGIVLFEMATCHDSLfekdGLDGDCDSDRQI-KLIIRRSG 307
                        250       260
                 ....*....|....*....|....
gi 32528297  277 PYPQEMSALAKDLIQRLLMKDPKK 300
Cdd:PHA03212 308 THPNEFPIDAQANLDEIYIGLAKK 331
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
432-548 1.29e-17

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 82.69  E-value: 1.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKcVHKKSNQAFAVKIISKRMEANTQ------KEITALK-LCegHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd14161  11 LGKGTYGRVKK-ARDSSGRLVAIKSIRKDRIKDEQdllhirREIEIMSsLN--HPHIISVYEVFENSSKIVIVMEYASRG 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14161  88 DLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLE 131
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
49-302 2.44e-17

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 82.26  E-value: 2.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRkisGHDtGKLYAMKV--LKKAtivqKAKTTEHTRTERQVLEHIRQSPFLVTL--HYAFQTE 124
Cdd:cd14131   3 YEILKQLGKGGSSKVYKVL---NPK-KKIYALKRvdLEGA----DEQTLQSYKNEIELLKKLKGSDRIIQLydYEVTDED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYingGE--LFTHLSQRER--FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLdSNGHVVLTDFGLSK 200
Cdd:cd14131  75 DYLYMVMEC---GEidLATILKKKRPkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFVADETE--RAySFCGTIEYMAPD-IVRGGDSGHDKAV-------DWWSLGVLMYELLTGASPFtvdgeknsqAEISRR 270
Cdd:cd14131 151 AIQNDTTSivRD-SQVGTLNYMSPEaIKDTSASGEGKPKskigrpsDVWSLGCILYQMVYGKTPF---------QHITNP 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 32528297 271 ILK--------SEPPYPQEMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14131 221 IAKlqaiidpnHEIEFPDIPNPDLIDVMKRCLQRDPKKRP 260
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
55-301 2.81e-17

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 81.93  E-value: 2.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFlvrKISGHDTGKLYAMKVL------KKATIVQKAKTTehtrterQVLEHIRQSPFLVTLHyafqTETKLH 128
Cdd:cd14221   1 LGKGCFGQAI---KVTHRETGEVMVMKELirfdeeTQRTFLKEVKVM-------RCLEHPNVLKFIGVLY----KDKRLN 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELF-------THL--SQRERFTEhevqiyvgEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd14221  67 FITEYIKGGTLRgiiksmdSHYpwSQRVSFAK--------DIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLA 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 200 KEFVADETE-------------RAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGAS------PFTVDGE 260
Cdd:cd14221 139 RLMVDEKTQpeglrslkkpdrkKRYTVVGNPYWMAPEMING--RSYDEKVDVFSFGIVLCEIIGRVNadpdylPRTMDFG 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 32528297 261 KNSQAEISRRILKSEPPYPQEMSALAKDLiqrllmkDPKKR 301
Cdd:cd14221 217 LNVRGFLDRYCPPNCPPSFFPIAVLCCDL-------DPEKR 250
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
49-320 3.48e-17

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 83.11  E-value: 3.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVflvrkISGHD--TGKLYAMKVLKkativQKAKTTEHT-RTERQV--LEHIRQsPFLVTLHYAFQT 123
Cdd:cd07851  17 YQNLSPVGSGAYGQV-----CSAFDtkTGRKVAIKKLS-----RPFQSAIHAkRTYRELrlLKHMKH-ENVIGLLDVFTP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILD-YinggeLFTHL--------SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLT 194
Cdd:cd07851  86 ASSLEDFQDvY-----LVTHLmgadlnniVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKIL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 195 DFGLSKEfvADETERAYsfCGTIEYMAPDIVRggDSGH-DKAVDWWSLGVLMYELLTGASPF-----------------T 256
Cdd:cd07851 161 DFGLARH--TDDEMTGY--VATRWYRAPEIML--NWMHyNQTVDIWSVGCIMAELLTGKTLFpgsdhidqlkrimnlvgT 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 257 VDGE--KNSQAEISRRILKSEPPYPQE--------MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQK 320
Cdd:cd07851 235 PDEEllKKISSESARNYIQSLPQMPKKdfkevfsgANPLAIDLLEKMLVLDPDKRI-----TAAEALAHPYLAE 303
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
430-548 3.77e-17

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 82.45  E-value: 3.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFS---ICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKL------CEGHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd05584   2 KVLGKGGYGkvfQVRKTTGSDKGKIFAMKVLKKASIVRNQKDTAHTKAernileAVKHPFIVDLHYAFQTGGKLYLILEY 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05584  82 LSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPE 129
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
55-255 3.88e-17

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 81.77  E-value: 3.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisghDTGKLYAMKVLKKAtivQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLhLILDYI 134
Cdd:cd14664   1 IGRGGAGTVYKGVM----PNGTLVAVKRLKGE---GTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNL-LVYEYM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEH-----EVQIYVGEiVLALEHLHK---LGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd14664  73 PNGSLGELLHSRPESQPPldwetRQRIALGS-ARGLAYLHHdcsPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKD 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 207 TERAYSFCGTIEYMAPDIVRGGDSghDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd14664 152 SHVMSSVAGSYGYIAPEYAYTGKV--SEKSDVYSYGVVLLELITGKRPF 198
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
49-318 4.48e-17

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 81.55  E-value: 4.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKatIVQKAKTTEHTRtERQVLEHIRQSPFLVTLH-YAFQTET-K 126
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRK---TGKYYAIKCMKK--HFKSLEQVNNLR-EIQALRRLSPHPNILRLIeVLFDRKTgR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLIL--------DYINGgelfthlsQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNgHVVLTDFGl 198
Cdd:cd07831  75 LALVFelmdmnlyELIKG--------RKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKEFVADE---TEraysFCGTIEYMAPD-IVRGGDSGHdkAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEI------- 267
Cdd:cd07831 145 SCRGIYSKppyTE----YISTRWYRAPEcLLTDGYYGP--KMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIhdvlgtp 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 268 SRRILK-------SEPPYPQE-----------MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07831 219 DAEVLKkfrksrhMNYNFPSKkgtglrkllpnASAEGLDLLKKLLAYDPDERI-----TAKQALRHPYF 282
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
432-547 4.62e-17

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 81.15  E-value: 4.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM-------EANTQKEITALKLCEgHPNIVKLHEVFHDQL--HTFLVMELLN 502
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKlrripngEANVKREIQILRRLN-HRNVIKLVDVLYNEEkqKLYMVMEYCV 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 503 GG--ELFERIKKKKhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14119  80 GGlqEMLDSAPDKR-LPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKP 125
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
46-255 4.72e-17

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 81.59  E-value: 4.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkativqkaktTEHTR-------TERQVLEHIRQSPfLVTLH 118
Cdd:cd07871   4 LETYVKLDKLGEGTYATVF---KGRSKLTENLVALKEIR----------LEHEEgapctaiREVSLLKNLKHAN-IVTLH 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 119 YAFQTETKLHLILDYINGgELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd07871  70 DIIHTERCLTLVFEYLDS-DLKQYLDNcGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFG 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 198 LSKefVADETERAYSF-CGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd07871 149 LAR--AKSVPTKTYSNeVVTLWYRPPDVLL-GSTEYSTPIDMWGVGCILYEMATGRPMF 204
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
50-256 5.75e-17

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 80.83  E-value: 5.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  50 ELLKVLGTGAYGKVFlvrkiSGHDTGKLyAMKVLKKATivQKAKTTEHTRTERQVLEHIRQSPFLvtLHYAFQTETKLHL 129
Cdd:cd14150   3 SMLKRIGTGSFGTVF-----RGKWHGDV-AVKILKVTE--PTPEQLQAFKNEMQVLRKTRHVNIL--LFMGFMTRPNFAI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGL----SKEFVA 204
Cdd:cd14150  73 ITQWCEGSSLYRHLHVTEtRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLatvkTRWSGS 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 205 DETERAysfCGTIEYMAPDIVRGGD-SGHDKAVDWWSLGVLMYELLTGASPFT 256
Cdd:cd14150 153 QQVEQP---SGSILWMAPEVIRMQDtNPYSFQSDVYAYGVVLYELMSGTLPYS 202
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
430-548 7.39e-17

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 80.58  E-value: 7.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT-QKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELL--NGGEL 506
Cdd:cd14016   6 KKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQlEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLLgpSLEDL 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FEriKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14016  86 FN--KCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPE 125
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
430-548 7.71e-17

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 80.26  E-value: 7.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVK------IISKRMEAnTQKEITALK-LCegHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGELMAVKevelsgDSEEELEA-LEREIRILSsLK--HPNIVRYLGTERTENTLNIFLEYVP 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd06606  83 GGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGA 128
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
428-548 8.36e-17

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 80.34  E-value: 8.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIIskrmEANTQKEITALKlCE-------GHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd14193   8 KEEILGGGRFGQVHKCEEKSSGLKLAAKII----KARSQKEKEEVK-NEievmnqlNHANLIQLYDAFESRNDIVLVMEY 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 501 LNGGELFERIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14193  83 VDGGELFDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPE 131
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
432-547 8.49e-17

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 81.05  E-value: 8.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM--------EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14094  11 IGKGPFSVVRRCIHRETGQQFAVKIVDVAKftsspglsTEDLKREASICHMLK-HPHIVELLETYSSDGMLYMVFEFMDG 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 504 GEL-FERIKKKKH---FSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14094  90 ADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKP 137
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
430-548 9.72e-17

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 80.91  E-value: 9.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK----RME--ANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14209   7 KTLGTGSFGRVMLVRHKETGNYYAMKILDKqkvvKLKqvEHTLNEKRILQAIN-FPFLVKLEYSFKDNSNLYMVMEYVPG 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14209  86 GEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPE 130
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
430-548 1.18e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 81.16  E-value: 1.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN--TQKEITA-----LKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd05604   2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNrkEQKHIMAernvlLKNVK-HPFLVGLHYSFQTTDKLYFVLDFVN 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05604  81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPE 126
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
58-303 1.23e-16

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 79.71  E-value: 1.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  58 GAYGKVFLVRKISGHDTGKLyamkvlKKATIVQKAKTTEHTRTERQVLE-------HIRQsPFLVTLhYAFQTET----- 125
Cdd:cd14012   4 SPSGTFYLVYEVVLDNSKKP------GKFLTSQEYFKTSNGKKQIQLLEkeleslkKLRH-PNLVSY-LAFSIERrgrsd 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 --KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH---VVLTDFGLSK 200
Cdd:cd14012  76 gwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFvADETERAYSFcgTIE---YMAPDIVRGGDSGHDKAvDWWSLGVLMYELLTGASPFtvdgEKNSQAeisrrilkSEPP 277
Cdd:cd14012 156 TL-LDMCSRGSLD--EFKqtyWLPPELAQGSKSPTRKT-DVWDLGLLFLQMLFGLDVL----EKYTSP--------NPVL 219
                       250       260
                ....*....|....*....|....*.
gi 32528297 278 YPQEMSALAKDLIQRLLMKDPKKRLG 303
Cdd:cd14012 220 VSLDLSASLQDFLSKCLSLDPKKRPT 245
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
58-314 2.46e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 78.90  E-value: 2.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  58 GAYGKVFLVRKIsghDTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQspflvtLHYAFQTETKLHLILDYINGG 137
Cdd:cd13995  15 GAFGKVYLAQDT---KTKKRMACKLIP----VEQFKPSDVEIQACFRHENIAE------LYGALLWEETVHLFMEAGEGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 138 ELFTHLSQRERFTEHEVqIYVGEIVL-ALEHLHKLGIIYRDIKLENILLDSNgHVVLTDFGLSKEFvadeTERAY---SF 213
Cdd:cd13995  82 SVLEKLESCGPMREFEI-IWVTKHVLkGLDFLHSKNIIHHDIKPSNIVFMST-KAVLVDFGLSVQM----TEDVYvpkDL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 214 CGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPY---PQEMSALAKDLI 290
Cdd:cd13995 156 RGTEIYMSPEVILC--RGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHKQAPPLediAQDCSPAMRELL 233
                       250       260
                ....*....|....*....|....
gi 32528297 291 QRLLMKDPKKRlgcgPRDADEIKE 314
Cdd:cd13995 234 EAALERNPNHR----SSAAELLKH 253
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
49-318 2.73e-16

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 80.30  E-value: 2.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRkisGHDTGKLYAMKVLKKatiVQKakTTEHTRTERQVLEHIRQS-----PFLVTLHYAFQT 123
Cdd:cd14134  14 YKILRLLGEGTFGKVLECW---DRKRKRYVAVKIIRN---VEK--YREAAKIEIDVLETLAEKdpngkSHCVQLRDWFDY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDyINGGELFTHLSQR--ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDS-------------- 187
Cdd:cd14134  86 RGHMCIVFE-LLGPSLYDFLKKNnyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDsdyvkvynpkkkrq 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 188 -----NGHVVLTDFGlSKEFvadetERAY--SFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTG--------- 251
Cdd:cd14134 165 irvpkSTDIKLIDFG-SATF-----DDEYhsSIVSTRHYRAPEVILG--LGWSYPCDVWSIGCILVELYTGellfqthdn 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 252 -------------------------ASPFTVDG------EKNSQAEISRRILKSEPPYPQEMS---ALAKDLIQRLLMKD 297
Cdd:cd14134 237 lehlammerilgplpkrmirrakkgAKYFYFYHgrldwpEGSSSGRSIKRVCKPLKRLMLLVDpehRLLFDLIRKMLEYD 316
                       330       340
                ....*....|....*....|.
gi 32528297 298 PKKRLgcgprDADEIKEHLFF 318
Cdd:cd14134 317 PSKRI-----TAKEALKHPFF 332
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
423-548 2.84e-16

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 78.90  E-value: 2.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 423 YDLDLKDKpLGEGSFSICRKCVHK-KSNQAFAVKIISKRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd14202   2 FEFSRKDL-IGHGAFAVVFKGRHKeKHDLEVAVKCINKKNLAKSQtllgKEIKILKELK-HENIVALYDFQEIANSVYLV 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14202  80 MEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQ 130
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
320-379 2.98e-16

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 73.16  E-value: 2.98e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297    320 KINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPA---ALPQSSEKLFQGYSFVA 379
Cdd:smart00133   2 GIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVdspLSGGIQQEPFRGFSYVF 64
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
415-548 2.98e-16

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 79.86  E-value: 2.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  415 KDSPFYQHYDLDLKDKpLGEGSFSICRKCVHKKSNQAFAVKIISKR--MEANTQKEITALK--LCE-GHPNIVKLHEVFH 489
Cdd:PTZ00263  10 PDTSSWKLSDFEMGET-LGTGSFGRVRIAKHKGTGEYYAIKCLKKReiLKMKQVQHVAQEKsiLMElSHPFIVNMMCSFQ 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297  490 DQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:PTZ00263  89 DENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPE 147
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
426-548 3.07e-16

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 78.89  E-value: 3.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKDKpLGEGSFSICRKCVHKKSNQAFAVKII---SKRMEANTQKEITALKlCEGHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd14191   5 DIEER-LGSGKFGQVFRLVEKKTKKVWAGKFFkaySAKEKENIRQEISIMN-CLHHPKLVQCVDAFEEKANIVMVLEMVS 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 503 GGELFERIKKKK-HFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14191  83 GGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPE 129
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
48-220 3.15e-16

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 78.65  E-value: 3.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATivqKAKTTEHtrtERQVLEHIRQSPFLVTLHYAFQTETKL 127
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLK---TGEEVAIKIEKKDS---KHPQLEY---EAKVYKLLQGGPGIPRLYWFGQEGDYN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYI--NGGELFThlSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL--LDSNGHVV-LTDFGLSKEF 202
Cdd:cd14016  72 VMVMDLLgpSLEDLFN--KCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLmgLGKNSNKVyLIDFGLAKKY 149
                       170       180
                ....*....|....*....|....
gi 32528297 203 VADETER------AYSFCGTIEYM 220
Cdd:cd14016 150 RDPRTGKhipyreGKSLTGTARYA 173
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
432-548 3.69e-16

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 78.42  E-value: 3.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCE--GHPNIVKLHEVFHDQLHTFLVMELLNGGELFER 509
Cdd:cd14190  12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNqlNHRNLIQLYEAIETPNEIVLFMEYVEGGELFER 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 510 I-KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14190  92 IvDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPE 131
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
432-548 4.27e-16

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 78.28  E-value: 4.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR------MEANTQKEITALKLCEgHPNIVKLHEVFH-DQLHTFLVMELLNGG 504
Cdd:cd14165   9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKkapddfVEKFLPRELEILARLN-HKSIIKTYEIFEtSDGKVYIVMELGVQG 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14165  88 DLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCE 131
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
122-318 4.50e-16

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 77.78  E-value: 4.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYiNGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd14023  55 LGDTKAYVFFEK-DFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDT 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETERAYS-FCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQ 280
Cdd:cd14023 134 HIMKGEDDALSdKHGCPAYVSPEILNTTGTYSGKSADVWSLGVMLYTLLVGRYPF----HDSDPSALFSKIRRGQFCIPD 209
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 32528297 281 EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14023 210 HVSPKARCLIRSLLRREPSERL-----TAPEILLHPWF 242
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
422-548 4.99e-16

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 78.02  E-value: 4.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCE-GHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd14108   3 YYDIH---KEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAElDHKSIVRFHDAFEKRRVVIIVTEL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGgELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14108  80 CHE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPE 126
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
52-250 5.03e-16

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 78.40  E-value: 5.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKIS-GHDTGKLYAMKVLKKATivqkAKTTEHTRTERQVLeHIRQSPFLVT---LHYAfQTETKL 127
Cdd:cd05081   9 ISQLGKGNFGSVELCRYDPlGDNTGALVAVKQLQHSG----PDQQRDFQREIQIL-KALHSDFIVKyrgVSYG-PGRRSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd05081  83 RLVMEYLPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDK 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 207 TERAYSFCGT--IEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLT 250
Cdd:cd05081 163 DYYVVREPGQspIFWYAPESL--SDNIFSRQSDVWSFGVVLYELFT 206
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
47-319 5.36e-16

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 79.27  E-value: 5.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFL-----------VRKISGHDTgKLYAMKVLKKATIVQkaktteHTRTERQV-LEHIRQSPFL 114
Cdd:cd07849   5 PRYQNLSYIGEGAYGMVCSavhkptgqkvaIKKISPFEH-QTYCLRTLREIKILL------RFKHENIIgILDIQRPPTF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 115 VTLH--YAFQ--TETKLHLILdyinggelfthLSQRerFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH 190
Cdd:cd07849  78 ESFKdvYIVQelMETDLYKLI-----------KTQH--LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 191 VVLTDFGLSKefVADETERAYSF----CGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTG--------------- 251
Cdd:cd07849 145 LKICDFGLAR--IADPEHDHTGFlteyVATRWYRAPEIML-NSKGYTKAIDIWSVGCILAEMLSNrplfpgkdylhqlnl 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 252 -----ASPFTVD--GEKNSQAeisRRILKSEPPYPQ--------EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHL 316
Cdd:cd07849 222 ilgilGTPSQEDlnCIISLKA---RNYIKSLPFKPKvpwnklfpNADPKALDLLDKMLTFNPHKRI-----TVEEALAHP 293

                ...
gi 32528297 317 FFQ 319
Cdd:cd07849 294 YLE 296
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
430-547 5.78e-16

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 78.80  E-value: 5.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR-------MEAnTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEviiedddVEC-TMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVN 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd05570  80 GGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKL 124
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
55-249 6.16e-16

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 77.53  E-value: 6.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFlvrKISGHDTGKLYAMKVLK----KATIVQKAKTTehtrterQVLEHirqsPFLVTLHYAFQTETKLHLI 130
Cdd:cd14065   1 LGKGFFGEVY---KVTHRETGKVMVMKELKrfdeQRSFLKEVKLM-------RRLSH----PNILRFIGVCVKDNKLNFI 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQRERFTEHEVQIYVG-EIVLALEHLHKLGIIYRDIKLENILL---DSNGHVVLTDFGLSKEFV--- 203
Cdd:cd14065  67 TEYVNGGTLEELLKSMDEQLPWSQRVSLAkDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPdek 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 204 ADETER--AYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELL 249
Cdd:cd14065 147 TKKPDRkkRLTVVGSPYWMAPEMLRG--ESYDEKVDVFSFGIVLCEII 192
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
48-318 8.12e-16

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 77.91  E-value: 8.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkatIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKL 127
Cdd:cd07836   1 NFKQLEKLGEGTYATVY---KGRNRTTGEIVALKEIH---LDAEEGTPSTAIREISLMKELKH-ENIVRLHDVIHTENKL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGG---ELFTHlSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFvA 204
Cdd:cd07836  74 MLVFEYMDKDlkkYMDTH-GVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAF-G 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISR-----------RILK 273
Cdd:cd07836 152 IPVNTFSNEVVTLWYRAPDVLLGSRT-YSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRimgtptestwpGISQ 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 274 SE------PPYPQE--------MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07836 231 LPeykptfPRYPPQdlqqlfphADPLGIDLLHRLLQLNPELRI-----SAHDALQHPWF 284
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
124-318 8.71e-16

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 77.00  E-value: 8.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYiNGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV 203
Cdd:cd14022  57 ETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYI 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYS-FCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSqaeISRRILKSEPPYPQEM 282
Cdd:cd14022 136 LRGHDDSLSdKHGCPAYVSPEILNTSGSYSGKAADVWSLGVMLYTMLVGRYPFH-DIEPSS---LFSKIRRGQFNIPETL 211
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 32528297 283 SALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14022 212 SPKAKCLIRSILRREPSERL-----TSQEILDHPWF 242
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
430-548 8.92e-16

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 77.86  E-value: 8.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKI------ISKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05612   7 KTIGTGTFGRVHLVRDRISEHYYALKVmaipevIRLKQEQHVHNEKRVLKEVS-HPFIIRLFWTEHDQRFLYMLMEYVPG 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05612  86 GELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPE 130
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
55-249 8.92e-16

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 77.68  E-value: 8.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFlvrKISGHDTGKLYAMKVLkkatIVQKAKTTEHTRTERQV---LEHIRQSPFLVTLHyafqTETKLHLIL 131
Cdd:cd14222   1 LGKGFFGQAI---KVTHKATGKVMVMKEL----IRCDEETQKTFLTEVKVmrsLDHPNVLKFIGVLY----KDKRLNLLT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADET---- 207
Cdd:cd14222  70 EFIEGGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKkppp 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 208 ---------------ERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELL 249
Cdd:cd14222 150 dkpttkkrtlrkndrKKRYTVVGNPYWMAPEMLNGKS--YDEKVDIFSFGIVLCEII 204
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
45-318 9.55e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 78.18  E-value: 9.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  45 GIENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMK--------------VLKKATIVQKAK------TTEHTRTERQV 104
Cdd:cd07865  10 EVSKYEKLAKIGQGTFGEVFKARHRK---TGQIVALKkvlmenekegfpitALREIKILQLLKhenvvnLIEICRTKATP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 105 LEHIRQSPFLVtlhYAFqTETKLHLILDYINggelfthlsqrERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENIL 184
Cdd:cd07865  87 YNRYKGSIYLV---FEF-CEHDLAGLLSNKN-----------VKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANIL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 185 LDSNGHVVLTDFGLSKEFVADETERAYSFCG---TIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEK 261
Cdd:cd07865 152 ITKDGVLKLADFGLARAFSLAKNSQPNRYTNrvvTLWYRPPELLL-GERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQ 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 262 NSQAEIS------------------------------RRILKSEPPYPQEMSALakDLIQRLLMKDPKKRLgcgprDADE 311
Cdd:cd07865 231 HQLTLISqlcgsitpevwpgvdklelfkkmelpqgqkRKVKERLKPYVKDPYAL--DLIDKLLVLDPAKRI-----DADT 303

                ....*..
gi 32528297 312 IKEHLFF 318
Cdd:cd07865 304 ALNHDFF 310
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
49-320 9.99e-16

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 78.17  E-value: 9.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKativQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETKLH 128
Cdd:cd06635  27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGK----QSNEKWQDIIKEVKFLQRI-KHPNSIEYKGCYLREHTAW 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGlskefVADETE 208
Cdd:cd06635 102 LVMEYCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-----SASIAS 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSFCGTIEYMAPDIVRGGDSG-HDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEIsRRILKSEPPYPQ--EMSAL 285
Cdd:cd06635 177 PANSFVGTPYWMAPEVILAMDEGqYDGKVDVWSLGITCIELAERKPPLF---NMNAMSAL-YHIAQNESPTLQsnEWSDY 252
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 286 AKDLIQRLLMKDPKKRlgcgpRDADEIKEHLFFQK 320
Cdd:cd06635 253 FRNFVDSCLQKIPQDR-----PTSEELLKHMFVLR 282
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
430-548 1.01e-15

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 77.37  E-value: 1.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSIcrkcVHKKSNQAFAVKIISKRMEANTQ-------KEITALKLCEGHPNIVKL--HEVFHD--QLHTFLVM 498
Cdd:cd13985   6 KQLGEGGFSY----VYLAHDVNTGRRYALKRMYFNDEeqlrvaiKEIEIMKRLCGHPNIVQYydSAILSSegRKEVLLLM 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 499 ELLnGGELFERIKK--KKHFSETEASYIMRKLVSAVSHMHDVG--VVHRDLKPE 548
Cdd:cd13985  82 EYC-PGSLVDILEKspPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIE 134
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
49-318 1.15e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 77.70  E-value: 1.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLKkatiVQKAKTTEHTRTERQV-----LEHIrQSPFLVTLHYAFQT 123
Cdd:cd07863   2 YEPVAEIGVGAYGTVYKARDP---HSGHFVALKSVR----VQTNEDGLPLSTVREVallkrLEAF-DHPNIVRLMDVCAT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 -----ETKLHLILDYINGgELFTHLSQRER--FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDF 196
Cdd:cd07863  74 srtdrETKVTLVFEHVDQ-DLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 197 GLSkefvadeteRAYSF-------CGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISR 269
Cdd:cd07863 153 GLA---------RIYSCqmaltpvVVTLWYRAPEVLL--QSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFD 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 270 RI-LKSEPPYPQ----------------------EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07863 222 LIgLPPEDDWPRdvtlprgafsprgprpvqsvvpEIEESGAQLLLEMLTFNPHKRI-----SAFRALQHPFF 288
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
433-548 1.33e-15

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 76.52  E-value: 1.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 433 GEGSFSICRKCVHKKSNQAFAVKIISKRME-----ANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGgELF 507
Cdd:cd14002  10 GEGSFGKVYKGRRKYTGQVVALKFIPKRGKsekelRNLRQEIEILRKLN-HPNIIEMLDSFETKKEFVVVTEYAQG-ELF 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 508 ERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14002  88 QILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQ 128
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
430-546 1.60e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 76.55  E-value: 1.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKII----SKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd08219   6 RVVGEGSFGRALLVQHVNSDQKYAMKEIrlpkSSSAVEDSRKEAVLLAKMK-HPNIVAFKESFEADGHLYIVMEYCDGGD 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 506 LFERIK--KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd08219  85 LMQKIKlqRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIK 127
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
430-548 1.63e-15

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 77.78  E-value: 1.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRM------EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEViiakdeVAHTLTENRVLQNTR-HPFLTSLKYSFQTNDRLCFVMEYVNG 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05571  80 GELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLE 124
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
435-548 1.70e-15

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 76.87  E-value: 1.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 435 GSFSICRKcvhKKSNQAFAVKIISKR--MEANTQKEITALK--LCEGH-PNIVKLHEVFHDQLHTFLVMELLNGGELFER 509
Cdd:cd05579   7 GRVYLAKK---KSTGDLYAIKVIKKRdmIRKNQVDSVLAERniLSQAQnPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSL 83
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 510 IKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05579  84 LENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPD 122
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
50-268 1.86e-15

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 76.62  E-value: 1.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  50 ELLKVLGTGAYGKVFLVR----------KISGHDTGKLYAMKvlkkaTIVQKAKTTEHtrterqvlEHIrqspflVTLHY 119
Cdd:cd14063   3 EIKEVIGKGRFGRVHRGRwhgdvaikllNIDYLNEEQLEAFK-----EEVAAYKNTRH--------DNL------VLFMG 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 AFQTETKLHLILDYINGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDsNGHVVLTDFGL 198
Cdd:cd14063  64 ACMDPPHLAIVTSLCKGRTLYSLIhERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDFGL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKefVADETERAYSFC------GTIEYMAPDIVR----GGDSGHD----KAVDWWSLGVLMYELLTGASPFTVD------ 258
Cdd:cd14063 143 FS--LSGLLQPGRREDtlvipnGWLCYLAPEIIRalspDLDFEESlpftKASDVYAFGTVWYELLAGRWPFKEQpaesii 220
                       250
                ....*....|....*
gi 32528297 259 -----GEKNSQAEIS 268
Cdd:cd14063 221 wqvgcGKKQSLSQLD 235
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
55-249 1.91e-15

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 76.78  E-value: 1.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERqVLEHIRQSPFLVTLHyafqTETKLHLILDYI 134
Cdd:cd14154   1 LGKGFFGQAI---KVTHRETGEVMVMKELIRFDEEAQRNFLKEVKVMR-SLDHPNVLKFIGVLY----KDKKLNLITEYI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHL---------SQRERFTEhevqiyvgEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd14154  73 PGGTLKDVLkdmarplpwAQRVRFAK--------DIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEE 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 206 ETE-------------------RAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELL 249
Cdd:cd14154 145 RLPsgnmspsetlrhlkspdrkKRYTVVGNPYWMAPEMLNGRS--YDEKVDIFSFGIVLCEII 205
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
47-319 1.97e-15

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 77.64  E-value: 1.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVflvrkISGHD--TGKLYAMKVLKKAtiVQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTE 124
Cdd:cd07879  15 ERYTSLKQVGSGAYGSV-----CSAIDkrTGEKVAIKKLSRP--FQSEIFAKRAYRELTLLKHM-QHENVIGLLDVFTSA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILD-YINGGELFTHLSQ--RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd07879  87 VSGDEFQDfYLVMPYMQTDLQKimGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARH 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETeraySFCGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFT----------------VDGEKNSQ- 264
Cdd:cd07879 167 ADAEMT----GYVVTRWYRAPEVILNW-MHYNQTVDIWSVGCIMAEMLTGKTLFKgkdyldqltqilkvtgVPGPEFVQk 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 265 --AEISRRILKSEPPYPQE--------MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd07879 242 leDKAAKSYIKSLPKYPRKdfstlfpkASPQAVDLLEKMLELDVDKRL-----TATEALEHPYFD 301
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
54-306 1.98e-15

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 76.14  E-value: 1.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKATivqkakTTEHTRTERQVLEHIRQsPFLVTLhYAFQTETKLhLILDY 133
Cdd:cd14068   1 LLGDGGFGSVY-----RAVYRGEDVAVKIFNKHT------SFRLLRQELVVLSHLHH-PSLVAL-LAAGTAPRM-LVMEL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELfTHLSQRE-----RFTEHEVQIYVGEivlALEHLHKLGIIYRDIKLENILL-----DSNGHVVLTDFGLSKEFV 203
Cdd:cd14068  67 APKGSL-DALLQQDnasltRTLQHRIALHVAD---GLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCC 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETEraySFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFtVDGEKnsqaeisrrilkseppYPQEMS 283
Cdd:cd14068 143 RMGIK---TSEGTPGFRAPEVAR-GNVIYNQQADVYSFGLLLYDILTCGERI-VEGLK----------------FPNEFD 201
                       250       260
                ....*....|....*....|...
gi 32528297 284 ALAkdlIQRLLmKDPKKRLGCGP 306
Cdd:cd14068 202 ELA---IQGKL-PDPVKEYGCAP 220
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
49-318 2.02e-15

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 76.56  E-value: 2.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTehTRTERQVLEHIRqSPFLVTLHYAFQTETKLH 128
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKL---TGEIVALKKIRLETEDEGVPST--AIREISLLKELN-HPNIVRLLDVVHSENKLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGgELFTHLSQ--RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF---V 203
Cdd:cd07835  75 LVFEFLDL-DLKKYMDSspLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFgvpV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 adeteRAYSF-CGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNsqaEISR--RIL-------- 272
Cdd:cd07835 154 -----RTYTHeVVTLWYRAPEILLGSKH-YSTPVDIWSVGCIFAEMVTRRPLFPGDSEID---QLFRifRTLgtpdedvw 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 273 ---KSEPPY--------PQEMSAL-------AKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07835 225 pgvTSLPDYkptfpkwaRQDLSKVvpsldedGLDLLSQMLVYDPAKRI-----SAKAALQHPYF 283
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
46-321 2.13e-15

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 76.97  E-value: 2.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkativqkaktTEHTR-------TERQVLEHIRQSPfLVTLH 118
Cdd:cd07873   1 LETYIKLDKLGEGTYATVY---KGRSKLTDNLVALKEIR----------LEHEEgapctaiREVSLLKDLKHAN-IVTLH 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 119 YAFQTETKLHLILDYINGgELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd07873  67 DIIHTEKSLTLVFEYLDK-DLKQYLDDcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEfVADETERAYSFCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPF---TVDGE--------KNSQAE 266
Cdd:cd07873 146 LARA-KSIPTKTYSNEVVTLWYRPPDILL-GSTDYSTQIDMWGVGCIFYEMSTGRPLFpgsTVEEQlhfifrilGTPTEE 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 267 ISRRILKSE-------PPYPQE--------MSALAKDLIQRLLMKDPKKRLGcgprdADEIKEHLFFQKI 321
Cdd:cd07873 224 TWPGILSNEefksynyPKYRADalhnhaprLDSDGADLLSKLLQFEGRKRIS-----AEEAMKHPYFHSL 288
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
47-306 2.32e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 76.61  E-value: 2.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISghDTGKLYAMKVLKKATivQKAKTTEHTRTERQVLEHIR--QSPFLVTLHYAFQT- 123
Cdd:cd07862   1 QQYECVAEIGEGAYGKVFKARDLK--NGGRFVALKRVRVQT--GEEGMPLSTIREVAVLRHLEtfEHPNVVRLFDVCTVs 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ----ETKLHLILDYINGgELFTHLSQ-------RERFTEHEVQIYVGeivlaLEHLHKLGIIYRDIKLENILLDSNGHVV 192
Cdd:cd07862  77 rtdrETKLTLVFEHVDQ-DLTTYLDKvpepgvpTETIKDMMFQLLRG-----LDFLHSHRVVHRDLKPQNILVTSSGQIK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 193 LTDFGLSkefvadeteRAYSF-------CGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQA 265
Cdd:cd07862 151 LADFGLA---------RIYSFqmaltsvVVTLWYRAPEVLL--QSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLG 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 266 EISRRI-LKSEPPYPQE----------------------MSALAKDLIQRLLMKDPKKRLGCGP 306
Cdd:cd07862 220 KILDVIgLPGEEDWPRDvalprqafhsksaqpiekfvtdIDELGKDLLLKCLTFNPAKRISAYS 283
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
47-306 2.48e-15

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 77.02  E-value: 2.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTET- 125
Cdd:cd14041   6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDH-PRIVKLYDYFSLDTd 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLG--IIYRDIKLENILL---DSNGHVVLTDFGLSK 200
Cdd:cd14041  85 SFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGLSK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EF------VADETERAYSFCGTIEYMAPD--IVRGGDSGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRR-- 270
Cdd:cd14041 165 IMdddsynSVDGMELTSQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPF---GHNQSQQDILQEnt 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 32528297 271 ILKSE----PPYPQeMSALAKDLIQRLLMKDPKKR-----LGCGP 306
Cdd:cd14041 242 ILKATevqfPPKPV-VTPEAKAFIRRCLAYRKEDRidvqqLACDP 285
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
49-301 2.65e-15

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 75.78  E-value: 2.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIR-QSPF--LVTLHYAFQTET 125
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGIRVA---DGAPVAIKHVEKDRVSEWGELPNGTRVPMEIVLLKKvGSGFrgVIRLLDWFERPD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYING-GELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD-SNGHVVLTDFGlSKEFV 203
Cdd:cd14100  79 SFVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFG-SGALL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETeraYS-FCGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEknsqaeisrrILKSEPPYPQEM 282
Cdd:cd14100 158 KDTV---YTdFDGTRVYSPPEWIR-FHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEE----------IIRGQVFFRQRV 223
                       250
                ....*....|....*....
gi 32528297 283 SALAKDLIQRLLMKDPKKR 301
Cdd:cd14100 224 SSECQHLIKWCLALRPSDR 242
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
433-546 3.14e-15

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 76.19  E-value: 3.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 433 GEGSFSICRKCVHKKSNQAFAVKI--ISKRMEANTQKEITALKLCEGHPNIVKLHEVF--------HDQLhtFLVMELLN 502
Cdd:cd06608  15 GEGTYGKVYKARHKKTGQLAAIKImdIIEDEEEEIKLEINILRKFSNHPNIATFYGAFikkdppggDDQL--WLVMEYCG 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 503 GG---ELFERIKKK-KHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06608  93 GGsvtDLVKGLRKKgKRLKEEWIAYILRETLRGLAYLHENKVIHRDIK 140
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
432-546 3.47e-15

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 76.87  E-value: 3.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM-------EAN-TQKEItaLKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVilqdddvECTmTEKRI--LSLARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05590  81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLK 123
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
47-302 3.57e-15

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 76.25  E-value: 3.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd14040   6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDH-PRIVKLYDYFSLDTD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LH-LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLG--IIYRDIKLENILL---DSNGHVVLTDFGLSK 200
Cdd:cd14040  85 TFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 -----EFVADETERAYSFCGTIEYMAPD--IVRGGDSGHDKAVDWWSLGVLMYELLTGASPFtvdGEKNSQAEISRR--I 271
Cdd:cd14040 165 imdddSYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPF---GHNQSQQDILQEntI 241
                       250       260       270
                ....*....|....*....|....*....|....
gi 32528297 272 LK-SEPPYPQE--MSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14040 242 LKaTEVQFPVKpvVSNEAKAFIRRCLAYRKEDRF 275
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
48-250 3.93e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 75.82  E-value: 3.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGHD-TGKLYAMKVLKKATivqkaktTEHTRT-ERQV-----LEHIRQSPFLVTLHYA 120
Cdd:cd14205   5 HLKFLQQLGKGNFGSVEMCRYDPLQDnTGEVVAVKKLQHST-------EEHLRDfEREIeilksLQHDNIVKYKGVCYSA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 121 fqTETKLHLILDYINGGELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd14205  78 --GRRNLRLIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLT 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 200 KEFVADETERAYSFCGT--IEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT 250
Cdd:cd14205 156 KVLPQDKEYYKVKEPGEspIFWYAPESLT--ESKFSVASDVWSFGVVLYELFT 206
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
46-318 4.30e-15

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 76.11  E-value: 4.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKkatiVQKAKTTEHTRTERQV-----LEHirqsPFLVTLHYA 120
Cdd:cd07843   4 VDEYEKLNRIEEGTYGVVYRARDKK---TGEIVALKKLK----MEKEKEGFPITSLREInillkLQH----PNIVTVKEV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 121 F--QTETKLHLILDYINGgELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd07843  73 VvgSNLDKIYMVMEYVEH-DLKSLMETmKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 198 LSKEFvaDETERAY-SFCGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTVDGEKN-------------- 262
Cdd:cd07843 152 LAREY--GSPLKPYtQLVVTLWYRAPELLLGAKE-YSTAIDMWSVGCIFAELLTKKPLFPGKSEIDqlnkifkllgtpte 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 263 ------SQAEISRRILKSEPPYPQ--------EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07843 229 kiwpgfSELPGAKKKTFTKYPYNQlrkkfpalSLSDNGFDLLNRLLTYDPAKRI-----SAEDALKHPYF 293
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
432-546 4.33e-15

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 75.34  E-value: 4.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIS-----KRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd06627   8 IGRGAFGSVYKGLNLNTGEFVAIKQISlekipKSDLKSVMGEIDLLKKLN-HPNIVKYIGSVKTKDSLYIILEYVENGSL 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06627  87 ASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIK 126
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
52-318 4.35e-15

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 75.77  E-value: 4.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFL-VRKISGHdtgkLYAMKVLKKATivQKAKTTEHTRtERQVLEHIRQSPfLVTLHYAFQTETKLHLI 130
Cdd:cd07870   5 LEKLGEGSYATVYKgISRINGQ----LVALKVISMKT--EEGVPFTAIR-EASLLKGLKHAN-IVLLHDIIHTKETLTFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGgELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK-EFVADETE 208
Cdd:cd07870  77 FEYMHT-DLAQYMIQHPGgLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARaKSIPSQTY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSFcgTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRIL---------------- 272
Cdd:cd07870 156 SSEVV--TLWYRPPDVLLGA-TDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEKIWTVLgvptedtwpgvsklpn 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 273 -KSE---PPYPQEMSAL---------AKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07870 233 yKPEwflPCKPQQLRVVwkrlsrppkAEDLASQMLMMFPKDRI-----SAQDALLHPYF 286
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
430-548 4.50e-15

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 75.67  E-value: 4.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR------MEANTQKEITaLKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14117  12 RPLGKGKFGNVYLAREKQSKFIVALKVLFKSqiekegVEHQLRREIE-IQSHLRHPNILRLYNYFHDRKRIYLILEYAPR 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14117  91 GELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPE 135
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
49-290 4.79e-15

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 77.09  E-value: 4.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkativQKAKTTEHTRTERQVLEHIRQSPFLVTL-------HYAF 121
Cdd:cd14224  67 YEVLKVIGKGSFGQVV---KAYDHKTHQHVALKMVR-----NEKRFHRQAAEEIRILEHLKKQDKDNTMnvihmleSFTF 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFthlsQRERFTEHEVQI---YVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH--VVLTDF 196
Cdd:cd14224 139 RNHICMTFELLSMNLYELI----KKNKFQGFSLQLvrkFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDF 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 197 GLSkefvADETERAYSFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISrRILKSEP 276
Cdd:cd14224 215 GSS----CYEHQRIYTYIQSRFYRAPEVILGARYG--MPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMI-ELLGMPP 287
                       250
                ....*....|....
gi 32528297 277 PYPQEMSALAKDLI 290
Cdd:cd14224 288 QKLLETSKRAKNFI 301
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
430-548 4.92e-15

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 76.16  E-value: 4.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR--MEANTQKEITA-----LKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKtiLKKKEQNHIMAernvlLKNLK-HPFLVGLHYSFQTSEKLYFVLDYVN 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05603  80 GGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPE 125
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
47-321 5.50e-15

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 76.53  E-value: 5.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVflvrkISGHD--TGKLYAMKVLKKAtiVQKAKTTEHTRTERQVLEHIRQSPfLVTLHYAFQTE 124
Cdd:cd07880  15 DRYRDLKQVGSGAYGTV-----CSALDrrTGAKVAIKKLYRP--FQSELFAKRAYRELRLLKHMKHEN-VIGLLDVFTPD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKL------HLILDYIngGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGL 198
Cdd:cd07880  87 LSLdrfhdfYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKEfvADETERAYSFcgTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPF-------------------TVDG 259
Cdd:cd07880 165 ARQ--TDSEMTGYVV--TRWYRAPEVILNW-MHYTQTVDIWSVGCIMAEMLTGKPLFkghdhldqlmeimkvtgtpSKEF 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 260 EKNSQAEISRRILKSEPPYPQE--------MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQKI 321
Cdd:cd07880 240 VQKLQSEDAKNYVKKLPRFRKKdfrsllpnANPLAVNVLEKMLVLDAESRI-----TAAEALAHPYFEEF 304
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
47-320 5.57e-15

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 75.84  E-value: 5.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKativQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETK 126
Cdd:cd06633  21 EIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGK----QTNEKWQDIIKEVKFLQQLKH-PNTIEYKGCYLKDHT 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGlskefVADE 206
Cdd:cd06633  96 AWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-----SASI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 TERAYSFCGTIEYMAPDIVRGGDSG-HDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISrRILKSEPPYPQ--EMS 283
Cdd:cd06633 171 ASPANSFVGTPYWMAPEVILAMDEGqYDGKVDIWSLGITCIELAERKPPLF---NMNAMSALY-HIAQNDSPTLQsnEWT 246
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32528297 284 ALAKDLIQRLLMKDPKKRLGCGprdadEIKEHLFFQK 320
Cdd:cd06633 247 DSFRGFVDYCLQKIPQERPSSA-----ELLRHDFVRR 278
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
424-547 6.09e-15

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 74.99  E-value: 6.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKDKpLGEGSFSICRKCVHKKSNQAFAVKIISkrMEANTQ---KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd06612   4 VFDILEK-LGEGSYGSVYKAIHKETGQVVAIKVVP--VEEDLQeiiKEISILKQCD-SPYIVKYYGSYFKNTDLWIVMEY 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIK-KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd06612  80 CGAGSVSDIMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKA 127
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
46-304 6.28e-15

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 78.24  E-value: 6.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    46 IENFELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTteHTRTERQVLEHIRQSPFLVTL-HYAFQTE 124
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKH---KRTQEFFCWKAISYRGLKEREKS--QLVIEVNVMRELKHKNIVRYIdRFLNKAN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   125 TKLHLILDYINGGELFTHLSQ----RERFTEHEVQIYVGEIVLALEHLHKLG-------IIYRDIKLENILLDS------ 187
Cdd:PTZ00266   87 QKLYILMEFCDAGDLSRNIQKcykmFGKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLSTgirhig 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   188 ---------NGHVV--LTDFGLSKEFVADETerAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFt 256
Cdd:PTZ00266  167 kitaqannlNGRPIakIGDFGLSKNIGIESM--AHSCVGTPYYWSPELLLHETKSYDDKSDMWALGCIIYELCSGKTPF- 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 32528297   257 vDGEKNSQAEISRriLKSEPPYP-----QEMSALAKDLIQrLLMKDPKKRLGC 304
Cdd:PTZ00266  244 -HKANNFSQLISE--LKRGPDLPikgksKELNILIKNLLN-LSAKERPSALQC 292
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
41-266 6.49e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 76.45  E-value: 6.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   41 AEKVGIENFELLKVLGTGAYGKVFLVRKISGHDTgklyamKVLKkatIVQKAKTTehtrTERQVLEHIRQSPFLVTLHYA 120
Cdd:PHA03209  60 REVVASLGYTVIKTLTPGSEGRVFVATKPGQPDP------VVLK---IGQKGTTL----IEAMLLQNVNHPSVIRMKDTL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  121 FQTETKLhLILDYINGgELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:PHA03209 127 VSGAITC-MVLPHYSS-DLYTYLTKRSRpLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAA 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297  200 KEFVADETEraYSFCGTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLtgASPFTVDGEKNSQAE 266
Cdd:PHA03209 205 QFPVVAPAF--LGLAGTVETNAPEVL--ARDKYNSKADIWSAGIVLFEML--AYPSTIFEDPPSTPE 265
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
435-548 6.57e-15

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 74.95  E-value: 6.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 435 GSFSICRKCVHKKSNQAFAVKIISKRMEANTQ--KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKK 512
Cdd:cd14110  14 GRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLvlREYQVLRRLS-HPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAE 92
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 32528297 513 KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14110  93 RNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSE 128
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
432-548 6.59e-15

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 74.58  E-value: 6.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKrmEANTQ-----------KEITALKLCE--GHPNIVKLHEVFHDQLHTFLVM 498
Cdd:cd14005   8 LGKGGFGTVYSGVRIRDGLPVAVKFVPK--SRVTEwamingpvpvpLEIALLLKASkpGVPGVIRLLDWYERPDGFLLIM 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 499 ELLNGGE-LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14005  86 ERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDE 136
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
48-254 7.20e-15

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 74.60  E-value: 7.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTtehtrtERQVLEHIRQSPFLVTLHYAFQTETKL 127
Cdd:cd14017   1 RWKVVKKIGGGGFGEIYKVRDVV---DGEEVAMKVESKSQPKQVLKM------EVAVLKKLQGKPHFCRLIGCGRTERYN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYInGGELFTHL-SQRERFTEHEVQIYVGE-IVLALEHLHKLGIIYRDIKLENILL---DSNGHVV-LTDFGLSKE 201
Cdd:cd14017  72 YIVMTLL-GPNLAELRrSQPRGKFSVSTTLRLGIqILKAIEDIHEVGFLHRDVKPSNFAIgrgPSDERTVyILDFGLARQ 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETER------AYSFCGTIEYMAPDIVRGGDSG-HDkavDWWSLGVLMYELLTGASP 254
Cdd:cd14017 151 YTNKDGEVerpprnAAGFRGTVRYASVNAHRNKEQGrRD---DLWSWFYMLIEFVTGQLP 207
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
47-302 8.73e-15

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 75.11  E-value: 8.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkatiVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd07869   5 DSYEKLEKLGEGSYATVY---KGKSKVNGKLVALKVIR----LQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKET 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGgELFTHLSQRER-FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfvad 205
Cdd:cd07869  78 LTLVFEYVHT-DLCQYMDKHPGgLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARA---- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCG---TIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRIL---------- 272
Cdd:cd07869 153 KSVPSHTYSNevvTLWYRPPDVLL-GSTEYSTCLDMWGVGCIFVEMIQGVAAFP--GMKDIQDQLERIFLvlgtpnedtw 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 273 ---KSEPPYPQEMSAL------------------AKDLIQRLLMKDPKKRL 302
Cdd:cd07869 230 pgvHSLPHFKPERFTLyspknlrqawnklsyvnhAEDLASKLLQCFPKNRL 280
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
147-304 9.09e-15

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 75.94  E-value: 9.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 147 ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVR 226
Cdd:cd07853  98 QPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESKHMTQEVVTQYYRAPEILM 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 227 GgdSGH-DKAVDWWSLGVLMYELLTGASPFTVDG------------------EKNSQAEISRRILKSEPPYPQEMSAL-- 285
Cdd:cd07853 178 G--SRHyTSAVDIWSVGCIFAELLGRRILFQAQSpiqqldlitdllgtpsleAMRSACEGARAHILRGPHKPPSLPVLyt 255
                       170       180
                ....*....|....*....|....*..
gi 32528297 286 --------AKDLIQRLLMKDPKKRLGC 304
Cdd:cd07853 256 lssqatheAVHLLCRMLVFDPDKRISA 282
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
421-548 9.17e-15

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 74.37  E-value: 9.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 421 QHYDLdLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEANTQKEITALK-LCegHPNIVKLHEVFHDQLHT 494
Cdd:cd14082   1 QLYQI-FPDEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKlrfptKQESQLRNEVAILQqLS--HPGVVNLECMFETPERV 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 495 FLVMELLNG-----------GELFERIKKkkhfseteasYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14082  78 FVVMEKLHGdmlemilssekGRLPERITK----------FLVTQILVALRYLHSKNIVHCDLKPE 132
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
430-546 9.41e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 74.46  E-value: 9.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKII-----SKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd08218   6 KKIGEGSFGKALLVKSKEDGKQYVIKEIniskmSPKEREESRKEVAVLSKMK-HPNIVQYQESFEENGNLYIVMDYCDGG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKK--HFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd08218  85 DLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIK 128
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
47-312 9.46e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 74.72  E-value: 9.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVR-KISGHDTGKLYAMKVLKKAtivQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAF--QT 123
Cdd:cd05038   4 RHLKFIKQLGEGHFGSVELCRyDPLGDNTGEQVAVKSLQPS---GEEQHMSDFKREIEILRTL-DHEYIVKYKGVCesPG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGELFTHLS-QRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKef 202
Cdd:cd05038  80 RRSLRLIMEYLPSGSLRDYLQrHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAK-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 vADETERAYSFCGT-----IEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgeKNSQAEISRRILKSEPP 277
Cdd:cd05038 158 -VLPEDKEYYYVKEpgespIFWYAPECLR--ESRFSSASDVWSFGVTLYELFTYGDPS-----QSPPALFLRMIGIAQGQ 229
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 278 YPQEmsalakDLIQRLlmkDPKKRLGCGPRDADEI 312
Cdd:cd05038 230 MIVT------RLLELL---KSGERLPRPPSCPDEV 255
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
432-547 1.04e-14

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 73.73  E-value: 1.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKksNQAFAVKII-SKRMEANT----QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd13999   1 IGSGSFGEVYKGKWR--GTDVAIKKLkVEDDNDELlkefRREVSILSKLR-HPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERI-KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd13999  78 YDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKS 119
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
51-303 1.05e-14

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 74.34  E-value: 1.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKATivQKAKTTEHTRTERQVL----EHI-----------RQSPFLV 115
Cdd:cd13979   7 LQEPLGSGGFGSVY-----KATYKGETVAVKIVRRRR--KNRASRQSFWAELNAArlrhENIvrvlaaetgtdFASLGLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 116 TLHYaFQTETkLHLILDyinggELFTHLSQRERFTehevqiYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTD 195
Cdd:cd13979  80 IMEY-CGNGT-LQQLIY-----EGSEPLPLAHRIL------ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 196 FGLSKEF--VADETERAYSFCGTIEYMAPDIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILK 273
Cdd:cd13979 147 FGCSVKLgeGNEVGTPRSHIGGTYTYRAPELLKGERVT--PKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRP 224
                       250       260       270
                ....*....|....*....|....*....|.
gi 32528297 274 SEPPYPQEMSALA-KDLIQRLLMKDPKKRLG 303
Cdd:cd13979 225 DLSGLEDSEFGQRlRSLISRCWSAQPAERPN 255
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
429-547 1.10e-14

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 74.23  E-value: 1.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSFSICRKCVHKKSNQAFAVKI--ISKRMEANTQ----KEITALK-LCegHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd08224   5 EKKIGKGQFSVVYRARCLLDGRLVALKKvqIFEMMDAKARqdclKEIDLLQqLN--HPNIIKYLASFIENNELNIVLELA 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 502 NGGELFERIKK----KKHFSETEA-SYIMrKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd08224  83 DAGDLSRLIKHfkkqKRLIPERTIwKYFV-QLCSALEHMHSKRIMHRDIKP 132
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
427-546 1.24e-14

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 74.20  E-value: 1.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANT-QKEITALKLC----EGHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd14187  10 VRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPhQKEKMSMEIAihrsLAHQHVVGFHGFFEDNDFVYVVLELC 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 502 NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd14187  90 RRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLK 134
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
432-548 1.32e-14

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 73.84  E-value: 1.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII---SKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIkvkGAKEREEVKNEINIMNQLN-HVNLIQLYDAFESKTNLTLIMEYVDGGELFD 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 509 RIKKKK-HFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14192  91 RITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPE 131
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
430-548 1.37e-14

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 75.40  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRM------EANTQKEITALKLCEGhPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05573   7 KVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDmlkreqIAHVRAERDILADADS-PWIVRLHYAFQDEDHLYLVMEYMPG 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05573  86 GDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPD 130
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
164-320 1.37e-14

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 74.02  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 164 ALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGlSKEFVADeterAYSFCGTIEYMAPDIVRGGDSGH-DKAVDWWSLG 242
Cdd:cd06607 113 GLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG-SASLVCP----ANSFVGTPYWMAPEVILAMDEGQyDGKVDVWSLG 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 243 VLMYELLTGASPFTvdgEKNSQAEIsRRILKSEPPY--PQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQK 320
Cdd:cd06607 188 ITCIELAERKPPLF---NMNAMSAL-YHIAQNDSPTlsSGEWSDDFRNFVDSCLQKIPQDRP-----SAEDLLKHPFVTR 258
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
430-548 1.42e-14

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 74.02  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCE-----------------GHPNIVKLHEVFHDQL 492
Cdd:cd14077   7 KTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEisrdirtireaalssllNHPHICRLRDFLRTPN 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 493 HTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14077  87 HYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIE 142
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
432-546 1.46e-14

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 74.20  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRmEANT-----QKEITALKLCEGhPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd06609   9 IGKGSFGEVYKGIDKRTNQVVAIKVIDLE-EAEDeiediQQEIQFLSQCDS-PYITKYYGSFLKGSKLWIIMEYCGGGSV 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 507 FERIKKKKhFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06609  87 LDLLKPGP-LDETYIAFILREVLLGLEYLHSEGKIHRDIK 125
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
129-301 1.46e-14

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 74.07  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIyVGEIVLALEHLHKLG--IIYRDIKLENILLDSNGHVVLTDFGLSK--EFVA 204
Cdd:cd14025  70 LVMEYMETGSLEKLLASEPLPWELRFRI-IHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwnGLSH 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdGEKNsQAEISRRILKSEPP------- 277
Cdd:cd14025 149 SHDLSRDGLRGTIAYLPPERFKEKNRCPDTKHDVYSFAIVIWGILTQKKPFA--GENN-ILHIMVKVVKGHRPslspipr 225
                       170       180
                ....*....|....*....|....*
gi 32528297 278 -YPQEMSALAkDLIQRLLMKDPKKR 301
Cdd:cd14025 226 qRPSECQQMI-CLMKRCWDQDPRKR 249
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
135-305 1.51e-14

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 73.37  E-value: 1.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERA-YSF 213
Cdd:cd14024  67 HYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNGDDDSlTDK 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 214 CGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKnsqAEISRRILKSEPPYPQEMSALAKDLIQRL 293
Cdd:cd14024 147 HGCPAYVGPEILSSRRSYSGKAADVWSLGVCLYTMLLGRYPFQ-DTEP---AALFAKIRRGAFSLPAWLSPGARCLVSCM 222
                       170
                ....*....|..
gi 32528297 294 LMKDPKKRLGCG 305
Cdd:cd14024 223 LRRSPAERLKAS 234
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
432-548 1.58e-14

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 73.86  E-value: 1.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ--KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFER 509
Cdd:cd14113  15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQvtHELGVLQSLQ-HPQLVGLLDTFETPTSYILVLEMADQGRLLDY 93
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 510 IKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14113  94 VVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPE 132
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
430-548 1.68e-14

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 74.57  E-value: 1.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFS---ICRKCVHKKSNQAFAVKIISK-------RMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVME 499
Cdd:cd05614   6 KVLGTGAYGkvfLVRKVSGHDANKLYAMKVLRKaalvqkaKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKLHLILD 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05614  86 YVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLE 134
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
430-546 1.71e-14

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 73.49  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISkrME-----ANTQKEITALKLCEgHPNIVKLHEVFH--DQLhtFLVMELLN 502
Cdd:cd06613   6 QRIGSGTYGDVYKARNIATGELAAVKVIK--LEpgddfEIIQQEISMLKECR-HPNIVAYFGSYLrrDKL--WIVMEYCG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06613  81 GGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIK 124
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
52-302 1.73e-14

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 74.53  E-value: 1.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGkvfLVRKISGHDTGKLYAMKVLKKAtiVQKAKTTEHTRTERQVLEHIRQSPfLVTLHYAFQTETKLHLIL 131
Cdd:cd07856  15 LQPVGMGAFG---LVCSARDQLTGQNVAVKKIMKP--FSTPVLAKRTYRELKLLKHLRHEN-IISLSDIFISPLEDIYFV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLSQReRFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERAY 211
Cdd:cd07856  89 TELLGTDLHRLLTSR-PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR--IQDPQMTGY 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 sfCGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTG---------ASPFTVDGE----------KNSQAEISRRIL 272
Cdd:cd07856 166 --VSTRYYRAPEIMLTWQK-YDVEVDIWSAGCIFAEMLEGkplfpgkdhVNQFSIITEllgtppddviNTICSENTLRFV 242
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 32528297 273 KSEP-----PYPQEM---SALAKDLIQRLLMKDPKKRL 302
Cdd:cd07856 243 QSLPkrervPFSEKFknaDPDAIDLLEKMLVFDPKKRI 280
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
432-548 1.79e-14

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 73.89  E-value: 1.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVH-KKSNQAFAVKIISKRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd14201  14 VGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQillgKEIKILKELQ-HENIVALYDVQEMPNSVFLVMEYCNGGDL 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14201  93 ADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQ 134
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
430-548 1.89e-14

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 73.49  E-value: 1.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR------MEANTQKEITALKLCEgHPNIVKLHEVFHD-QLHTFLVMELLN 502
Cdd:cd14163   6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSggpeefIQRFLPRELQIVERLD-HKNIIHVYEMLESaDGKIYLVMELAE 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14163  85 DGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCE 130
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
430-548 1.91e-14

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 73.45  E-value: 1.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR------MEANTQKEI---TALKlcegHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd14116  11 RPLGKGKFGNVYLAREKQSKFILALKVLFKAqlekagVEHQLRREVeiqSHLR----HPNILRLYGYFHDATRVYLILEY 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14116  87 APLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPE 134
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
430-548 2.01e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 74.67  E-value: 2.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVK------IISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05602  13 KVIGKGSFGKVLLARHKSDEKFYAVKvlqkkaILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYING 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05602  93 GELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPE 137
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
46-274 2.15e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 75.50  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   46 IENFELLKVLGTGAYGKVFL--VRKISGHDtgklyamkvlkKATIVQKAKTTEHTRTERQVLEHIRQspflvTLHYAFQT 123
Cdd:PHA03210 147 LAHFRVIDDLPAGAFGKIFIcaLRASTEEA-----------EARRGVNSTNQGKPKCERLIAKRVKA-----GSRAAIQL 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  124 ETKLhLILDYING-----------GELFTH-LSQRERFTEH-----------------EVQIYVGEIVLALEHLHKLGII 174
Cdd:PHA03210 211 ENEI-LALGRLNHenilkieeilrSEANTYmITQKYDFDLYsfmydeafdwkdrpllkQTRAIMKQLLCAVEYIHDKKLI 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  175 YRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASP 254
Cdd:PHA03210 290 HRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAFDYGWVGTVATNSPEILAG--DGYCEITDIWSCGLILLDMLSHDFC 367
                        250       260
                 ....*....|....*....|
gi 32528297  255 FTVDGEKNSQAEIsRRILKS 274
Cdd:PHA03210 368 PIGDGGGKPGKQL-LKIIDS 386
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
430-546 2.18e-14

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 74.34  E-value: 2.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR--MEAN----TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDvvLEDDdvecTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05592  81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLK 123
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
432-548 2.64e-14

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 73.13  E-value: 2.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM--EANTQKEIT-ALKLCEgHPNIVKLHEV-FHDQLHTFLVMELLNGGELF 507
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPStkLKDFLREYNiSLELSV-HPHIIKTYDVaFETEDYYVFAQEYAPYGDLF 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 508 ERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd13987  80 SIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPE 120
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
49-301 3.39e-14

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 73.52  E-value: 3.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGHDTGKL-YAMKVLKKATivqKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETkL 127
Cdd:cd05108   9 FKKIKVLGSGAFGTVYKGLWIPEGEKVKIpVAIKELREAT---SPKANKEILDEAYVMASV-DNPHVCRLLGICLTST-V 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADe 206
Cdd:cd05108  84 QLITQLMPFGCLLDYVREhKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAE- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 207 tERAYSFCG---TIEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLT-GASPFtvDGEKNSqaEISRRILKSEP-PYPQE 281
Cdd:cd05108 163 -EKEYHAEGgkvPIKWMALESILHRIYTHQS--DVWSYGVTVWELMTfGSKPY--DGIPAS--EISSILEKGERlPQPPI 235
                       250       260
                ....*....|....*....|
gi 32528297 282 MSALAKDLIQRLLMKDPKKR 301
Cdd:cd05108 236 CTIDVYMIMVKCWMIDADSR 255
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
46-318 3.42e-14

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 73.50  E-value: 3.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKVLkkatIVQKAKTTEHTRTERQV-----LEH--IRQSPFLVTLH 118
Cdd:cd07866   7 LRDYEILGKLGEGTFGEVYKARQI---KTGRVVALKKI----LMHNEKDGFPITALREIkilkkLKHpnVVPLIDMAVER 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 119 YAFQTETK--LHLILDYINGgELFTHLS-QRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTD 195
Cdd:cd07866  80 PDKSKRKRgsVYMVTPYMDH-DLSGLLEnPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIAD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 196 FGLSKEFVAD---------ETERAYSFC-GTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGaSPFTVDGEKNSQA 265
Cdd:cd07866 159 FGLARPYDGPppnpkggggGGTRKYTNLvVTRWYRPPELLL-GERRYTTAVDIWGIGCVFAEMFTR-RPILQGKSDIDQL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 266 EISRRI--------------------LKSEPPYPQ-------EMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07866 237 HLIFKLcgtpteetwpgwrslpgcegVHSFTNYPRtleerfgKLGPEGLDLLSKLLSLDPYKRL-----TASDALEHPYF 311
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
17-281 3.63e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 74.50  E-value: 3.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   17 DGGDGGEQLltvkHELRTAnlTGHAEKVGIEnFELLKVLGTGAYGKVFLVRKiSGHDTGKlyamKVLKKAtiVQKAKTTE 96
Cdd:PHA03207  69 PQTDVCQEP----CETTSS--SDPASVVRMQ-YNILSSLTPGSEGEVFVCTK-HGDEQRK----KVIVKA--VTGGKTPG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   97 htrTERQVLEHIRQSPFLVTLHyAFQTETKLHLILDYINGgELFTHLSQRERFTEHEVqIYVGEIVL-ALEHLHKLGIIY 175
Cdd:PHA03207 135 ---REIDILKTISHRAIINLIH-AYRWKSTVCMVMPKYKC-DLFTYVDRSGPLPLEQA-ITIQRRLLeALAYLHGRGIIH 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  176 RDIKLENILLDSNGHVVLTDFGLS-KEFVADETERAYSFCGTIEYMAPDIVrGGDSGHDKaVDWWSLGVLMYELLTGASP 254
Cdd:PHA03207 209 RDVKTENIFLDEPENAVLGDFGAAcKLDAHPDTPQCYGWSGTLETNSPELL-ALDPYCAK-TDIWSAGLVLFEMSVKNVT 286
                        250       260
                 ....*....|....*....|....*..
gi 32528297  255 FTVDGEKNSQAEIsRRILKSEPPYPQE 281
Cdd:PHA03207 287 LFGKQVKSSSSQL-RSIIRCMQVHPLE 312
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
432-548 3.70e-14

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 72.69  E-value: 3.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII--SKRMEANTQKEITALKL-----CEGHPNIVKLHEVFHDQLHTFLVMELLnGG 504
Cdd:cd14133   7 LGKGTFGQVVKCYDLLTGEEVALKIIknNKDYLDQSLDEIRLLELlnkkdKADKYHIVRLKDVFYFKNHLCIVFELL-SQ 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 505 ELFERIK--KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14133  86 NLYEFLKqnKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPE 131
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
446-548 3.77e-14

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 72.75  E-value: 3.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 446 KKSNQAFAVKIISKRMEANTQK----EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEA 521
Cdd:cd14088  23 KTTGKLYTCKKFLKRDGRKVRKaaknEINILKMVK-HPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGYYSERDT 101
                        90       100
                ....*....|....*....|....*..
gi 32528297 522 SYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14088 102 SNVIRQVLEAVAYLHSLKIVHRNLKLE 128
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
432-547 4.31e-14

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 72.78  E-value: 4.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR---------------------------MEaNTQKEITALKLCEgHPNIVKL 484
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKkllkqagffrrppprrkpgalgkpldpLD-RVYREIAILKKLD-HPNVVKL 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 485 HEVFHD--QLHTFLVMELLNGGELFErIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14118  80 VEVLDDpnEDNLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKP 143
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
49-255 4.41e-14

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 72.83  E-value: 4.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGHDTGKL-YAMKVLKKATivqKAKTTEHTRTERQVLEHIrQSPFLVTLhYAFQTETKL 127
Cdd:cd05057   9 LEKGKVLGSGAFGTVYKGVWIPEGEKVKIpVAIKVLREET---GPKANEEILDEAYVMASV-DHPHLVRL-LGICLSSQV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADE 206
Cdd:cd05057  84 QLITQLMPLGCLLDYVRNhRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDE 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 207 TERAYSFCGT-IEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLT-GASPF 255
Cdd:cd05057 164 KEYHAEGGKVpIKWMALESIQYRIYTHKS--DVWSYGVTVWELMTfGAKPY 212
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
52-255 5.80e-14

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 72.36  E-value: 5.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFL-VRKISGHDTGKLYAMKVLKKATivqKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETkLHLI 130
Cdd:cd05109  12 VKVLGSGAFGTVYKgIWIPDGENVKIPVAIKVLRENT---SPKANKEILDEAYVMAGV-GSPYVCRLLGICLTST-VQLV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETEr 209
Cdd:cd05109  87 TQLMPYGCLLDYVREnKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETE- 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 aYSFCG---TIEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLT-GASPF 255
Cdd:cd05109 166 -YHADGgkvPIKWMALESILHRRFTHQS--DVWSYGVTVWELMTfGAKPY 212
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
137-302 6.49e-14

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 71.69  E-value: 6.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 137 GELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD-ETERAYSFCG 215
Cdd:cd13976  69 GDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEgEDDSLSDKHG 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 216 TIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRrilkSEPPYPQEMSALAKDLIQRLLM 295
Cdd:cd13976 149 CPAYVSPEILNSGATYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRR----GQFAIPETLSPRARCLIRSLLR 224

                ....*..
gi 32528297 296 KDPKKRL 302
Cdd:cd13976 225 REPSERL 231
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
138-301 7.04e-14

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 71.52  E-value: 7.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 138 ELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD-SNGHVVLTDFGlSKEFVADETeraYS-FCG 215
Cdd:cd14102  91 DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFG-SGALLKDTV---YTdFDG 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 216 TIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEknsqaeisrrILKSEPPYPQEMSALAKDLIQRLLM 295
Cdd:cd14102 167 TRVYSPPEWIR-YHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEE----------ILRGRLYFRRRVSPECQQLIKWCLS 235

                ....*.
gi 32528297 296 KDPKKR 301
Cdd:cd14102 236 LRPSDR 241
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
53-249 7.19e-14

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 72.30  E-value: 7.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLvrkisGHDTGKLYAMKVLkkativqkaktteHTRTER-----------QVLEH--IRQspFLVTLHY 119
Cdd:cd14056   1 KTIGKGRYGEVWL-----GKYRGEKVAVKIF-------------SSRDEDswfreteiyqtVMLRHenILG--FIAADIK 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 AFQTETKLHLILDYINGGELFTHLsQRERFTEHEVQIYVGEIVLALEHLH--------KLGIIYRDIKLENILLDSNGHV 191
Cdd:cd14056  61 STGSWTQLWLITEYHEHGSLYDYL-QRNTLDTEEALRLAYSAASGLAHLHteivgtqgKPAIAHRDLKSKNILVKRDGTC 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 192 VLTDFGLSKEFVADETERAYSF---CGTIEYMAPDIVRGGDSG----HDKAVDWWSLGVLMYELL 249
Cdd:cd14056 140 CIADLGLAVRYDSDTNTIDIPPnprVGTKRYMAPEVLDDSINPksfeSFKMADIYSFGLVLWEIA 204
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
430-548 7.37e-14

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 72.65  E-value: 7.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR--------MEANTQKEITALKlceGHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd05574   7 KLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEemikrnkvKRVLTEREILATL---DHPFLPTLYASFQTSTHLCFVMDYC 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 502 NGGELFERIKK--KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05574  84 PGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPE 132
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
49-320 7.71e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 72.36  E-value: 7.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKativQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLH 128
Cdd:cd06634  17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGK----QSNEKWQDIIKEVKFLQKLRH-PNTIEYRGCYLREHTAW 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGlSKEFVADete 208
Cdd:cd06634  92 LVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG-SASIMAP--- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 rAYSFCGTIEYMAPDIVRGGDSG-HDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISrRILKSEPPYPQ--EMSAL 285
Cdd:cd06634 168 -ANSFVGTPYWMAPEVILAMDEGqYDGKVDVWSLGITCIELAERKPPLF---NMNAMSALY-HIAQNESPALQsgHWSEY 242
                       250       260       270
                ....*....|....*....|....*....|....*
gi 32528297 286 AKDLIQRLLMKDPKKRlgcgpRDADEIKEHLFFQK 320
Cdd:cd06634 243 FRNFVDSCLQKIPQDR-----PTSDVLLKHRFLLR 272
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
164-302 8.96e-14

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 72.14  E-value: 8.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 164 ALEHLHKLGIIYRDIKLENILL--DSNG--HVVLTDFG---------LSKEFVADETERAysfcGTIEYMAPDIV----- 225
Cdd:cd14018 150 GVDHLVRHGIAHRDLKSDNILLelDFDGcpWLVIADFGccladdsigLQLPFSSWYVDRG----GNACLMAPEVStavpg 225
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 226 RGGDSGHDKAvDWWSLGVLMYELLTGASPFTvdGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd14018 226 PGVVINYSKA-DAWAVGAIAYEIFGLSNPFY--GLGDTMLESRSYQESQLPALPSAVPPDVRQVVKDLLQRDPNKRV 299
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
430-548 9.05e-14

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 71.36  E-value: 9.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKI------ISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05611   2 KPISKGAFGSVYLAKKRSTGDYFAIKVlkksdmIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNG 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05611  82 GDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPE 126
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
49-318 9.06e-14

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 72.32  E-value: 9.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGhDTGKLYAMKvlkkativqKAKTTEHTRT--------ERQVLEHIRQsPFLVTLHYA 120
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKAKRKNG-KDGKEYAIK---------KFKGDKEQYTgisqsacrEIALLRELKH-ENVVSLVEV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 121 F--QTETKLHLILDYI--NGGELFTHLSQRERFTEHE--VQIYVGEIVLALEHLHKLGIIYRDIKLENILL----DSNGH 190
Cdd:cd07842  71 FleHADKSVYLLFDYAehDLWQIIKFHRQAKRVSIPPsmVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 191 VVLTDFGLSKEFVAdETERAYSFCG---TIEYMAPDIVRGgdSGH-DKAVDWWSLGVLMYELLTGASPFTVDGEKNS--- 263
Cdd:cd07842 151 VKIGDLGLARLFNA-PLKPLADLDPvvvTIWYRAPELLLG--ARHyTKAIDIWAIGCIFAELLTLEPIFKGREAKIKksn 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 264 --QAEISRRI--------------LKSEPPYPQEMSA----------LAK-------------DLIQRLLMKDPKKRLgc 304
Cdd:cd07842 228 pfQRDQLERIfevlgtptekdwpdIKKMPEYDTLKSDtkastypnslLAKwmhkhkkpdsqgfDLLRKLLEYDPTKRI-- 305
                       330
                ....*....|....
gi 32528297 305 gprDADEIKEHLFF 318
Cdd:cd07842 306 ---TAEEALEHPYF 316
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
423-548 9.52e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 71.55  E-value: 9.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 423 YDLDLKD-KPLGEGSFSICRKCVHKKSNQAFAVKII----SKRMEANTQKEITAL-KLceGHPNIVKLHEVFHDQLHTFL 496
Cdd:cd13996   4 YLNDFEEiELLGSGGFGSVYKVRNKVDGVTYAIKKIrlteKSSASEKVLREVKALaKL--NHPNIVRYYTAWVEEPPLYI 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 497 VMELLNGGELFERIKKKKHFS---ETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd13996  82 QMELCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPS 136
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
55-292 2.16e-13

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 70.48  E-value: 2.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFlvrkisghdTGKLYAMKVLKKATIVQKA-KTTEHTRTERQVLEHIRQSPFLVTLHYAfqTETKLHLILDY 133
Cdd:cd14151  16 IGSGSFGTVY---------KGKWHGDVAVKMLNVTAPTpQQLQAFKNEVGVLRKTRHVNILLFMGYS--TKPQLAIVTQW 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHLSQRERFTEHEVQIYVG-EIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERAYS 212
Cdd:cd14151  85 CEGSSLYHHLHIIETKFEMIKLIDIArQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT--VKSRWSGSHQ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 F---CGTIEYMAPDIVRGGDSG-HDKAVDWWSLGVLMYELLTGASPFTVDGEKNS------QAEISRRILKSEPPYPQEM 282
Cdd:cd14151 163 FeqlSGSILWMAPEVIRMQDKNpYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQiifmvgRGYLSPDLSKVRSNCPKAM 242
                       250
                ....*....|
gi 32528297 283 SALAKDLIQR 292
Cdd:cd14151 243 KRLMAECLKK 252
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
424-548 2.38e-13

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 70.83  E-value: 2.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAntQKEITALKLCEGHPNIVKLHEVFHDQLHT----FLVME 499
Cdd:cd14170   2 DYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKA--RREVELHWRASQCPHIVRIVDVYENLYAGrkclLIVME 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 500 LLNGGELFERIKKK--KHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14170  80 CLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPE 130
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
51-298 2.49e-13

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 70.45  E-value: 2.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFlvrkiSGHDTGKLyAMKVLKkaTIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYafQTETKLHLI 130
Cdd:cd14149  16 LSTRIGSGSFGTVY-----KGKWHGDV-AVKILK--VVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGY--MTKDNLAIV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK-EFVADETE 208
Cdd:cd14149  86 TQWCEGSSLYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRWSGSQ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSFCGTIEYMAPDIVRGGDSG-HDKAVDWWSLGVLMYELLTGASPFTVDGEKNS------QAEISRRILKSEPPYPQE 281
Cdd:cd14149 166 QVEQPTGSILWMAPEVIRMQDNNpFSFQSDVYSYGIVLYELMTGELPYSHINNRDQiifmvgRGYASPDLSKLYKNCPKA 245
                       250
                ....*....|....*..
gi 32528297 282 MSALAKDLIQRLLMKDP 298
Cdd:cd14149 246 MKRLVADCIKKVKEERP 262
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
55-249 3.18e-13

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 69.86  E-value: 3.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISghdTGKLYAMKVLKKativqkaKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd14156   1 IGSGFFSKVYKVTHGA---TGKVMVVKIYKN-------DVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVG-EIVLALEHLHKLGIIYRDIKLENILL--DSNG-HVVLTDFGLSKEFV---ADET 207
Cdd:cd14156  71 SGGCLEELLAREELPLSWREKVELAcDISRGMVYLHSKNIYHRDLNSKNCLIrvTPRGrEAVVTDFGLAREVGempANDP 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 32528297 208 ERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELL 249
Cdd:cd14156 151 ERKLSLVGSAFWMAPEMLRGEP--YDRKVDVFSFGIVLCEIL 190
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
55-255 3.24e-13

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 69.73  E-value: 3.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFlvrkiSGHDTGKLyAMKVLKKATivQKAKTTEHTRTERQVLEHIRQSPFLvtLHYAFQTETKLHLILDYI 134
Cdd:cd14062   1 IGSGSFGTVY-----KGRWHGDV-AVKKLNVTD--PTPSQLQAFKNEVAVLRKTRHVNIL--LFMGYMTKPQLAIVTQWC 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQIYVG-EIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS---KEFVADETERA 210
Cdd:cd14062  71 EGSSLYKHLHVLETKFEMLQLIDIArQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAtvkTRWSGSQQFEQ 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 211 YSfcGTIEYMAPDIVRGGDSG-HDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd14062 151 PT--GSILWMAPEVIRMQDENpYSFQSDVYAFGIVLYELLTGQLPY 194
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
432-548 3.31e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 69.88  E-value: 3.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIS--------KRM---EANTQKEITalklcegHPNIVKLHEVFHDQLHT--FLVM 498
Cdd:cd08217   8 IGKGSFGTVRKVRRKSDGKILVWKEIDygkmsekeKQQlvsEVNILRELK-------HPNIVRYYDRIVDRANTtlYIVM 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 499 ELLNGGELFERIKK-KKHFSETEASYI---MRKLVSAVSHMH----DVGVV-HRDLKPE 548
Cdd:cd08217  81 EYCEGGDLAQLIKKcKKENQYIPEEFIwkiFTQLLLALYECHnrsvGGGKIlHRDLKPA 139
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
430-546 3.38e-13

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 70.60  E-value: 3.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN------TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQdddvdcTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05591  81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLK 123
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
432-545 3.45e-13

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 69.50  E-value: 3.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM---EANTQKEITALKL-CE-GHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd14186   9 LGKGSFACVYRARSLHTGLEVAIKMIDKKAmqkAGMVQRVRNEVEIhCQlKHPSILELYNYFEDSNYVYLVLEMCHNGEM 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 507 FERIK-KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd14186  89 SRYLKnRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDL 128
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
427-548 4.69e-13

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 69.50  E-value: 4.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMeaNTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:PHA03390  19 VKKLKLIDGKFGKVSVLKHKPTQKLFVQKIIKAKN--FNAIEPMVHQLMKDNPNFIKLYYSVTTLKGHVLIMDYIKDGDL 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 32528297  507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:PHA03390  97 FDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLE 138
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
432-548 4.75e-13

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 69.65  E-value: 4.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN-----TQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELL--NGG 504
Cdd:cd07833   9 VGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEdvkktALREVKVLRQLR-HENIVNLKEAFRRKGRLYLVFEYVerTLL 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERikKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07833  88 ELLEA--SPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPE 129
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
432-547 5.59e-13

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 69.83  E-value: 5.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKI---ISKRMEANTQK-EITALKLCEgHPNIVKLHEVFHDQL--HTFLVMELLNGGE 505
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVfnnLSFMRPLDVQMrEFEVLKKLN-HKNIVKLFAIEEELTtrHKVLVMELCPCGS 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 506 LFERIKKKKH---FSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd13988  80 LYTVLEEPSNaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKP 124
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
430-548 5.78e-13

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 69.64  E-value: 5.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFS---ICRKCVHKKSNQAFAVKIISK-------RMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVME 499
Cdd:cd05613   6 KVLGTGAYGkvfLVRKVSGHDAGKLYAMKVLKKativqkaKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKLHLILD 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05613  86 YINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLE 134
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
48-318 5.85e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 69.37  E-value: 5.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATIVQKAKTTehTRTERQVLEHIrQSPFLVTLHYAFQTETKL 127
Cdd:cd07861   1 DYTKIEKIGEGTYGVVY---KGRNKKTGQIVAMKKIRLESEEEGVPST--AIREISLLKEL-QHPNIVCLEDVLMQENRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGgELFTHLSQ--RERFTEHE-VQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd07861  75 YLVFEFLSM-DLKKYLDSlpKGKYMDAElVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 deTERAYSF-CGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRI----------LK 273
Cdd:cd07861 154 --PVRVYTHeVVTLWYRAPEVLLGS-PRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILgtptediwpgVT 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 274 SEPPYP---------------QEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd07861 231 SLPDYKntfpkwkkgslrtavKNLDEDGLDLLEKMLIYDPAKRI-----SAKKALVHPYF 285
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
432-548 6.21e-13

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 68.96  E-value: 6.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFS---ICRKCVHKKSNQAFAVKII--------SKRMEaNTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd05583   2 LGTGAYGkvfLVRKVGGHDAGKLYAMKVLkkativqkAKTAE-HTMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDY 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05583  81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLE 128
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
47-283 6.54e-13

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 68.75  E-value: 6.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISGHDTgklyAMKVLKKATI-----VQKAKTTEHtrterqvLEHirqsPFLVTLHYAF 121
Cdd:cd05113   4 KDLTFLKELGTGQFGVVKYGKWRGQYDV----AIKMIKEGSMsedefIEEAKVMMN-------LSH----EKLVQLYGVC 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK 200
Cdd:cd05113  69 TKQRPIFIITEYMANGCLLNYLrEMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFVADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLT-GASPFtvdgEKNSQAEISRRILKSEPPY- 278
Cdd:cd05113 149 YVLDDEYTSSVGSKFPVRWSPPEVLMY--SKFSSKSDVWAFGVLMWEVYSlGKMPY----ERFTNSETVEHVSQGLRLYr 222

                ....*
gi 32528297 279 PQEMS 283
Cdd:cd05113 223 PHLAS 227
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
47-255 8.10e-13

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 69.06  E-value: 8.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRK--ISGHDTGKLYAMKVLKKAtivqkAKTTEHTR--TERQVLEHIRQSPFLVTLHYAFQ 122
Cdd:cd05054   7 DRLKLGKPLGRGAFGKVIQASAfgIDKSATCRTVAVKMLKEG-----ATASEHKAlmTELKILIHIGHHLNVVNLLGACT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETK-LHLILDYINGGELFTHL-SQRERFT--------EHEVQIYVGEIV---LALEHLHKLGI--------------IY 175
Cdd:cd05054  82 KPGGpLMVIVEFCKFGNLSNYLrSKREEFVpyrdkgarDVEEEEDDDELYkepLTLEDLICYSFqvargmeflasrkcIH 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 176 RDIKLENILLDSNGHVVLTDFGLSKEFVADeteraysfcgtieymaPDIVRGGD-----------SGHDKAV----DWWS 240
Cdd:cd05054 162 RDLAARNILLSENNVVKICDFGLARDIYKD----------------PDYVRKGDarlplkwmapeSIFDKVYttqsDVWS 225
                       250
                ....*....|....*.
gi 32528297 241 LGVLMYELLT-GASPF 255
Cdd:cd05054 226 FGVLLWEIFSlGASPY 241
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
49-301 8.22e-13

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 69.81  E-value: 8.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVflVRKISGHdTGKLYAMKvlKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAF---QTET 125
Cdd:cd07859   2 YKIQEVIGKGSYGVV--CSAIDTH-TGEKVAIK--KINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLppsRREF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd07859  77 KDIYVVFELMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFND 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAY--SFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTG----------------------ASPFTVDGEK 261
Cdd:cd07859 157 TPTAIFwtDYVATRWYRAPELCGSFFSKYTPAIDIWSIGCIFAEVLTGkplfpgknvvhqldlitdllgtPSPETISRVR 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 262 NSQAeisRRIL----KSEP-PYPQEMSA---LAKDLIQRLLMKDPKKR 301
Cdd:cd07859 237 NEKA---RRYLssmrKKQPvPFSQKFPNadpLALRLLERLLAFDPKDR 281
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
152-319 8.45e-13

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 68.89  E-value: 8.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 152 HEVQIYVG--EIVLALEHLH-KLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfVADETERAYSFCG-----------TI 217
Cdd:cd14011 112 YDVEIKYGllQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCIS-SEQATDQFPYFREydpnlpplaqpNL 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 218 EYMAPDIVRGgdSGHDKAVDWWSLGVLMYELL-TGASPFTVDG-----EKNSQAEISRRILKSEPPyPQEMsalaKDLIQ 291
Cdd:cd14011 191 NYLAPEYILS--KTCDPASDMFSLGVLIYAIYnKGKPLFDCVNnllsyKKNSNQLRQLSLSLLEKV-PEEL----RDHVK 263
                       170       180
                ....*....|....*....|....*...
gi 32528297 292 RLLMKDPKKRLgcgprDADEIKEHLFFQ 319
Cdd:cd14011 264 TLLNVTPEVRP-----DAEQLSKIPFFD 286
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
47-316 8.90e-13

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 68.60  E-value: 8.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKK-ATIVQKAKTTEHTRTERQvLEHirqsPFLVTLhYAFQTET 125
Cdd:cd05056   6 EDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNcTSPSVREKFLQEAYIMRQ-FDH----PHIVKL-IGVITEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERFTEHEVQI-YVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd05056  80 PVWIVMELAPLGELRSYLQVNKYSLDLASLIlYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMED 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIV--RGGDSghdkAVDWWSLGVLMYELLT-GASPFTvdGEKNSqaEISRRILKSE-PPYPQ 280
Cdd:cd05056 160 ESYYKASKGKLPIKWMAPESInfRRFTS----ASDVWMFGVCMWEILMlGVKPFQ--GVKNN--DVIGRIENGErLPMPP 231
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32528297 281 EMSALAKDLIQRLLMKDPKKRlgcgPRdADEIKEHL 316
Cdd:cd05056 232 NCPPTLYSLMTKCWAYDPSKR----PR-FTELKAQL 262
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
430-547 9.66e-13

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 69.18  E-value: 9.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR--MEANTQKEITALK--LCEG-HPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd05599   7 KVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSemLEKEQVAHVRAERdiLAEAdNPWVVKLYYSFQDEENLYLIMEFLPGG 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd05599  87 DMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKP 129
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
432-548 9.97e-13

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 68.18  E-value: 9.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM-----EANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd13997   8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFrgpkeRARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENGSL 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 507 ---FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd13997  88 qdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPD 132
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
426-547 1.04e-12

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 68.53  E-value: 1.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKD-KPLGEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQK------EITALKLCEGhPNIVKLHEVFHDQLHTFLVM 498
Cdd:cd06605   2 DLEYlGELGEGNGGVVSKVRHRPSGQIMAVKVI--RLEIDEALqkqilrELDVLHKCNS-PYIVGFYGAFYSEGDISICM 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 499 ELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDV-GVVHRDLKP 547
Cdd:cd06605  79 EYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKP 128
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
432-547 1.11e-12

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 68.47  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII--SKRME-ANTQKEITALKlcegHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd14010   8 IGRGKHSVVYKGRRKGTIEFVAIKCVdkSKRPEvLNEVRLTHELK----HPNVLKFYEWYETSNHLWLVVEYCTGGDLET 83
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 509 RIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14010  84 LLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKP 122
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
432-546 1.16e-12

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 68.62  E-value: 1.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK---EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDfmvEIDILSECK-HPNIVGLYEAYFYENKLWILIEFCDGGALDS 91
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 509 RIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06611  92 IMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLK 130
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
422-548 1.22e-12

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 69.13  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDLKD---------KPLGEGSFSICRKCVHKKSNQAFAVKII--------SKRMEANTQKEItALKLCEGHPNIVKL 484
Cdd:cd14134   1 HLIYKPGDlltnrykilRLLGEGTFGKVLECWDRKRKRYVAVKIIrnvekyreAAKIEIDVLETL-AEKDPNGKSHCVQL 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 485 HEVFHDQLHTFLVMELLnGGELFERIKKKKH--FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14134  80 RDWFDYRGHMCIVFELL-GPSLYDFLKKNNYgpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPE 144
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
432-546 1.22e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 68.93  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIskRME-------ANTQKEITALKLCEgHPNIVKLHEVF-HDQLHT-FLVMELLN 502
Cdd:cd07845  15 IGEGTYGIVYRARDTTSGEIVALKKV--RMDnerdgipISSLREITLLLNLR-HPNIVELKEVVvGKHLDSiFLVMEYCE 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 G--GELFERIKKKkhFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd07845  92 QdlASLLDNMPTP--FSESQVKCLMLQLLRGLQYLHENFIIHRDLK 135
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
93-317 1.26e-12

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 67.94  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  93 KTTEHTRTERqVLEHIRQSPFLvtlhyAFQTEtKLHlildyingGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLG 172
Cdd:cd14112  55 RTLQHENVQR-LIAAFKPSNFA-----YLVME-KLQ--------EDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKG 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 173 IIYRDIKLENILLDSNGHVV--LTDFGLSKefvADETERAYSFCGTIEYMAPDIVRGGDSGHDKAvDWWSLGVLMYELLT 250
Cdd:cd14112 120 IAHLDVQPDNIMFQSVRSWQvkLVDFGRAQ---KVSKLGKVPVDGDTDWASPEFHNPETPITVQS-DIWGLGVLTFCLLS 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 251 GASPFTvdGEKNSQAEISRRIL--KSEPPY-PQEMSALAKDLIQRLLMKDPKKRlgcgPRdADEIKEHLF 317
Cdd:cd14112 196 GFHPFT--SEYDDEEETKENVIfvKCRPNLiFVEATQEALRFATWALKKSPTRR----MR-TDEALEHRW 258
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
433-548 1.34e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 68.10  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 433 GEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQKEITA----LKLCEG--HPNIVKLH--EVFHDQLHTFlvMELLNGG 504
Cdd:cd06626   9 GEGTFGKVYTAVNLDTGELMAMKEI--RFQDNDPKTIKEiadeMKVLEGldHPNLVRYYgvEVHREEVYIF--MEYCQEG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 505 ELFERIKKKKHFSETeasYIMR---KLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd06626  85 TLEELLRHGRILDEA---VIRVytlQLLEGLAYLHENGIVHRDIKPA 128
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
432-547 1.42e-12

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 67.85  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKksNQAFAVKII-SKRMEANTQKEITAL-KLCegHPNIVKLHEVFHDQLHTFLVMELLNGGELFER 509
Cdd:cd14058   1 VGRGSFGVVCKARWR--NQIVAVKIIeSESEKKAFEVEVRQLsRVD--HPNIIKLYGACSNQKPVCLVMEYAEGGSLYNV 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 510 I---KKKKHFSETEASYIMRKLVSAVSHMH---DVGVVHRDLKP 547
Cdd:cd14058  77 LhgkEPKPIYTAAHAMSWALQCAKGVAYLHsmkPKALIHRDLKP 120
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
422-547 1.74e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 68.71  E-value: 1.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIIS---------KRmeanTQKEITALKlCEGHPNIVKLHEVF-HDQ 491
Cdd:cd07834   1 RYELL---KPIGSGAYGVVCSAYDKRTGRKVAIKKISnvfddlidaKR----ILREIKILR-HLKHENIIGLLDILrPPS 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 492 LHTF----LVMELLnGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07834  73 PEEFndvyIVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKP 131
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
432-548 1.80e-12

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 68.75  E-value: 1.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRmEANTQKEI------------TALKLCeghPNIVKLHEVFHDQLHTFLVME 499
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKK-VIVAKKEVahtigernilvrTALDES---PFIVGLKFSFQTPTDLYLVTD 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05586  77 YMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPE 125
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
430-547 1.87e-12

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 67.42  E-value: 1.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKII-----SKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd08530   6 KKLGKGSYGSVYKVKRLSDNQVYALKEVnlgslSQKEREDSVNEIRLLASVN-HPNIIRYKEAFLDGNRLCIVMEYAPFG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 505 ELFERI----KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd08530  85 DLSKLIskrkKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKS 131
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
55-301 1.92e-12

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 67.47  E-value: 1.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFlvrKISGHDTGKLYAMKVLKKA-TIVQKAKTTEHTRTERQvLEHirqsPFLVTL-HYAFQTEtKLHLILD 132
Cdd:cd05041   3 IGRGNFGDVY---RGVLKPDNTEVAVKTCRETlPPDLKRKFLQEARILKQ-YDH----PNIVKLiGVCVQKQ-PIMIVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfvadETERAY 211
Cdd:cd05041  74 LVPGGSLLTFLrKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRE----EEDGEY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 212 SFCG-----TIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFTvdGEKNSQAeisRRILKS--EPPYPQEMS 283
Cdd:cd05041 150 TVSDglkqiPIKWTAPEALNYGR--YTSESDVWSFGILLWEIFSlGATPYP--GMSNQQT---REQIESgyRMPAPELCP 222
                       250
                ....*....|....*...
gi 32528297 284 ALAKDLIQRLLMKDPKKR 301
Cdd:cd05041 223 EAVYRLMLQCWAYDPENR 240
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
422-547 2.11e-12

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 67.38  E-value: 2.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDlkdKPLGEGSFSICRKCVHKKSNQAFAVKIIS-KRMEANTQ---KEITALKLCEgHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd06610   2 DYELI---EVIGSGATAVVYAAYCLPKKEKVAIKRIDlEKCQTSMDelrKEIQAMSQCN-HPNVVSYYTSFVVGDELWLV 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 498 MELLNGGELFERIK---KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd06610  78 MPLLSGGSLLDIMKssyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKA 130
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
55-301 2.31e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 67.65  E-value: 2.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVR-KISGHDTGKLYAMKVLKKATivqkakTTEHTRTERQVLEHIRQSPFLVTLHY-AFQTE---TKLHL 129
Cdd:cd05079  12 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKPES------GGNHIADLKKEIEILRNLYHENIVKYkGICTEdggNGIKL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQRERFTEHEVQI-YVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefvADETE 208
Cdd:cd05079  86 IMEFLPSGSLKEYLPRNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK---AIETD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAY-----SFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT----GASPFTV----DGEKNSQAEISR--RILK 273
Cdd:cd05079 163 KEYytvkdDLDSPVFWYAPECLI--QSKFYIASDVWSFGVTLYELLTycdsESSPMTLflkmIGPTHGQMTVTRlvRVLE 240
                       250       260       270
                ....*....|....*....|....*....|
gi 32528297 274 SEP--PYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd05079 241 EGKrlPRPPNCPEEVYQLMRKCWEFQPSKR 270
pknD PRK13184
serine/threonine-protein kinase PknD;
46-316 2.48e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 69.80  E-value: 2.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   46 IENFELLKVLGTGAYGKVFLvrkisGHDT--GKLYAMKVLKKATIvqkakttEHTRTERQVLEHIRQS-----PFLVTLH 118
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYL-----AYDPvcSRRVALKKIREDLS-------ENPLLKKRFLREAKIAadlihPGIVPVY 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  119 YAFQTETKLHLILDYINGGELFTHLS---QRERFT-EHEVQIYVG-------EIVLALEHLHKLGIIYRDIKLENILLDS 187
Cdd:PRK13184  69 SICSDGDPVYYTMPYIEGYTLKSLLKsvwQKESLSkELAEKTSVGaflsifhKICATIEYVHSKGVLHRDLKPDNILLGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  188 NGHVVLTDFGLSKEFVADETERA----------YS-------FCGTIEYMAPDIVRGGDSghDKAVDWWSLGVLMYELLT 250
Cdd:PRK13184 149 FGEVVILDWGAAIFKKLEEEDLLdidvdernicYSsmtipgkIVGTPDYMAPERLLGVPA--SESTDIYALGVILYQMLT 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297  251 GASPF-TVDGEKNSQAEisrRILKSE--PPY---PQEMSALAkdliQRLLMKDPKKRLGCGPRDADEIKEHL 316
Cdd:PRK13184 227 LSFPYrRKKGRKISYRD---VILSPIevAPYreiPPFLSQIA----MKALAVDPAERYSSVQELKQDLEPHL 291
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
432-548 2.55e-12

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 67.95  E-value: 2.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII--SKRMEANTQKEITALK-LCEGHP----NIVKLHEVFHDQLHTFLVMELLnGG 504
Cdd:cd14210  21 LGKGSFGQVVKCLDHKTGQLVAIKIIrnKKRFHQQALVEVKILKhLNDNDPddkhNIVRYKDSFIFRGHLCIVFELL-SI 99
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 505 ELFERIKKKKH--FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14210 100 NLYELLKSNNFqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPE 145
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
46-321 2.63e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 67.71  E-value: 2.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkatIVQKAKTTEHTRTERQVLEHIRQSPfLVTLHYAFQTET 125
Cdd:cd07872   5 METYIKLEKLGEGTYATVF---KGRSKLTENLVALKEIR---LEHEEGAPCTAIREVSLLKDLKHAN-IVTLHDIVHTDK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGgELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVA 204
Cdd:cd07872  78 SLTLVFEYLDK-DLKQYMDDcGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR--AK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSF-CGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYELLTGASPF---TVDGEK------------------N 262
Cdd:cd07872 155 SVPTKTYSNeVVTLWYRPPDVLL-GSSEYSTQIDMWGVGCIFFEMASGRPLFpgsTVEDELhlifrllgtpteetwpgiS 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 263 SQAEISRRILKSEPPYP-----QEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQKI 321
Cdd:cd07872 234 SNDEFKNYNFPKYKPQPlinhaPRLDTEGIELLTKFLQYESKKRI-----SAEEAMKHAYFRSL 292
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
427-547 2.69e-12

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 67.68  E-value: 2.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKpLGEGSFSICRKCVHKKSNQAFAVKIISKRM--------------------EANTQ---------KEITALKLCEg 477
Cdd:cd14199   6 LKDE-IGKGSYGVVKLAYNEDDNTYYAMKVLSKKKlmrqagfprrppprgaraapEGCTQprgpiervyQEIAILKKLD- 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 478 HPNIVKLHEVFHD--QLHTFLVMELLNGGELFErIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14199  84 HPNVVKLVEVLDDpsEDHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKP 154
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
430-546 2.96e-12

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 68.03  E-value: 2.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR---MEAN---TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05619  11 KMLGKGSFGKVFLAELKGTNQFFAIKALKKDvvlMDDDvecTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFFVMEYLNG 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05619  91 GDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLK 133
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
81-318 3.47e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 66.95  E-value: 3.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  81 KVLKKATIVQKA----KTTEHTRTERQ----VLEHIR--QSPFLVTLHYAFQTETKLH----LILDYINGGELFTHLSQR 146
Cdd:cd14033  19 RGLDTETTVEVAwcelQTRKLSKGERQrfseEVEMLKglQHPNIVRFYDSWKSTVRGHkciiLVTELMTSGTLKTYLKRF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 147 ERFTEHEVQIYVGEIVLALEHLHKLG--IIYRDIKLENILLDS-NGHVVLTDFGLSkefVADETERAYSFCGTIEYMAPD 223
Cdd:cd14033  99 REMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGpTGSVKIGDLGLA---TLKRASFAKSVIGTPEFMAPE 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 224 IVrggDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISRRILKSEPP---YPQEMSALaKDLIQRLLMKDPKK 300
Cdd:cd14033 176 MY---EEKYDEAVDVYAFGMCILEMATSEYPYS---ECQNAAQIYRKVTSGIKPdsfYKVKVPEL-KEIIEGCIRTDKDE 248
                       250
                ....*....|....*...
gi 32528297 301 RLgcgprDADEIKEHLFF 318
Cdd:cd14033 249 RF-----TIQDLLEHRFF 261
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
55-301 3.83e-12

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 66.88  E-value: 3.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKISGHDTGKlYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTL------HYAFQTETKLH 128
Cdd:cd14020   8 LGQGSSASVYRVSSGRGADQPT-SALKEFQLDHQGSQESGDYGFAKERAALEQLQGHRNIVTLygvftnHYSANVPSRCL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LI--LDyINGGELFTHlSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV-LTDFGLSKEfvad 205
Cdd:cd14020  87 LLelLD-VSVSELLLR-SSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDECFkLIDFGLSFK---- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPD------IVRGG---DSGHDKAVDWWSLGVLMYELLTGAS-PFTVDGEK---NSQAEISRRIL 272
Cdd:cd14020 161 EGNQDVKYIQTDGYRAPEaelqncLAQAGlqsETECTSAVDLWSLGIVLLEMFSGMKlKHTVRSQEwkdNSSAIIDHIFA 240
                       250       260
                ....*....|....*....|....*....
gi 32528297 273 KSEPPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14020 241 SNAVVNPAIPAYHLRDLIKSMLHNDPGKR 269
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
47-264 3.98e-12

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 66.60  E-value: 3.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKisgHDTGKLyAMKVLKKATIVQKAKTTEHTRTerQVLEHIRqspfLVTLHYAFQTETK 126
Cdd:cd05072   7 ESIKLVKKLGAGQFGEVWMGYY---NNSTKV-AVKTLKPGTMSVQAFLEEANLM--KTLQHDK----LVRLYAVVTKEEP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRE--RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK---- 200
Cdd:cd05072  77 IYIITEYMAKGSLLDFLKSDEggKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARvied 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 201 -EFVADETERAysfcgTIEYMAPDIVRGGdSGHDKAvDWWSLGVLMYELLT-GASPFTvdGEKNSQ 264
Cdd:cd05072 157 nEYTAREGAKF-----PIKWTAPEAINFG-SFTIKS-DVWSFGILLYEIVTyGKIPYP--GMSNSD 213
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
430-548 4.15e-12

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 67.79  E-value: 4.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEAN---TQKEITAlklcegHPN---IVKLHEVFHDQLHTFLVM 498
Cdd:cd05596  32 KVIGRGAFGEVQLVRHKSTKKVYAMKLLSKfemikRSDSAffwEERDIMA------HANsewIVQLHYAFQDDKYLYMVM 105
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 499 ELLNGGELFErIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05596 106 DYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPD 154
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
424-548 4.48e-12

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 67.34  E-value: 4.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKDKpLGEGSFSICRKCVHKKSNQAFAVKIIsKRMEANTQKEITALK-----LCEGH-PNIVKLHEVFHDQLHTFLV 497
Cdd:cd05601   2 DFEVKNV-IGRGHFGEVQVVKEKATGDIYAMKVL-KKSETLAQEEVSFFEeerdiMAKANsPWITKLQYAFQDSENLYLV 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 498 MELLNGGELFERIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05601  80 MEYHPGGDLLSLLSRYDDiFEESMARFYLAELVLAIHSLHSMGYVHRDIKPE 131
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
47-288 4.83e-12

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 66.71  E-value: 4.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvRKISGHDTGKLYAmkVLKKaTIVQKAKTTEHTR--TERQVLEHIRQSPFLVTLHYAFQTE 124
Cdd:cd05043   6 ERVTLSDLLQEGTFGRIF--HGILRDEKGKEEE--VLVK-TVKDHASEIQVTMllQESSLLYGLSHQNLLPILHVCIEDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQ--------RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDF 196
Cdd:cd05043  81 EKPMVLYPYMNWGNLKLFLQQcrlseannPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 197 GLSKE-FVADeteraYSFCGT-----IEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPFtvdgeknsqAEISr 269
Cdd:cd05043 161 ALSRDlFPMD-----YHCLGDnenrpIKWMSLESLV--NKEYSSASDVWSFGVLLWELMTlGQTPY---------VEID- 223
                       250
                ....*....|....*....
gi 32528297 270 rilkseppyPQEMSALAKD 288
Cdd:cd05043 224 ---------PFEMAAYLKD 233
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
47-301 4.85e-12

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 66.74  E-value: 4.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVF--LVRKISGHDTGKLYAMKVLKKATivqKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTE 124
Cdd:cd05055  35 NNLSFGKTLGAGAFGKVVeaTAYGLSKSDAVMKVAVKMLKPTA---HSSEREALMSELKIMSHLGNHENIVNLLGACTIG 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHL-SQRERFTEHEVQI-YVGEIVLALEHLHKLGIIYRDIKLENILLdSNGHVV-LTDFGLSKE 201
Cdd:cd05055 112 GPILVITEYCCYGDLLNFLrRKRESFLTLEDLLsFSYQVAKGMAFLASKNCIHRDLAARNVLL-THGKIVkICDFGLARD 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETeraYSFCGT----IEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPF---TVDGEKNSQAEISRRILK 273
Cdd:cd05055 191 IMNDSN---YVVKGNarlpVKWMAPESIF--NCVYTFESDVWSYGILLWEIFSlGSNPYpgmPVDSKFYKLIKEGYRMAQ 265
                       250       260
                ....*....|....*....|....*....
gi 32528297 274 sePPY-PQEMSalakDLIQRLLMKDPKKR 301
Cdd:cd05055 266 --PEHaPAEIY----DIMKTCWDADPLKR 288
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
150-335 4.91e-12

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 67.40  E-value: 4.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 150 TEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERAYS-FCGTIEYMAPDIVRGG 228
Cdd:cd07858 106 SDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLAR--TTSEKGDFMTeYVVTRWYRAPELLLNC 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 229 dSGHDKAVDWWSLGVLMYELLTGASPF-------------------TVDGEKNSQAEISRRILKSEPPYPQ--------E 281
Cdd:cd07858 184 -SEYTTAIDVWSVGCIFAELLGRKPLFpgkdyvhqlklitellgspSEEDLGFIRNEKARRYIRSLPYTPRqsfarlfpH 262
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 282 MSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQKINwdDLAAKKV-PAPF 335
Cdd:cd07858 263 ANPLAIDLLEKMLVFDPSKRI-----TVEEALAHPYLASLH--DPSDEPVcQTPF 310
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
430-548 5.28e-12

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 66.95  E-value: 5.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQKEITALKLCEG-------HPNIVKLHEVF--HDQLhtFLVMEL 500
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKIL--RKEVIIAKDEVAHTVTESrvlqntrHPFLTALKYAFqtHDRL--CFVMEY 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05595  77 ANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLE 124
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
129-301 5.74e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 65.75  E-value: 5.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQR--ERFTEHEVQIYVGEIVLALEHLHK---LGIIYRDIKLENILLDSNGHVVLTDFGLSKeFV 203
Cdd:cd14060  59 IVTEYASYGSLFDYLNSNesEEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASR-FH 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETEraYSFCGTIEYMAPDIVRGGDSghDKAVDWWSLGVLMYELLTGASPFT-VDGEKNSQAEISRrilKSEPPYPQEM 282
Cdd:cd14060 138 SHTTH--MSLVGTFPWMAPEVIQSLPV--SETCDTYSYGVVLWEMLTREVPFKgLEGLQVAWLVVEK---NERPTIPSSC 210
                       170
                ....*....|....*....
gi 32528297 283 SALAKDLIQRLLMKDPKKR 301
Cdd:cd14060 211 PRSFAELMRRCWEADVKER 229
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
432-548 6.07e-12

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 66.83  E-value: 6.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVK------IISKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKtirkahIVSRSEVTHTLAERTVLAQVD-CPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05585  81 LFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPE 123
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
46-321 6.97e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 66.38  E-value: 6.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   46 IENFELLKVLGTGAYGKVFLVRKISGHDTgklyamKVLKKATIVQKAKTTEHTRT-ERQVLEHIRQSPfLVTLHYAFQTE 124
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNET------IALKKIRLEQEDEGVPSTAIrEISLLKEMQHGN-IVRLQDVVHSE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  125 TKLHLILDYINGgELFTHLSQRERFTE--HEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD-SNGHVVLTDFGLSKE 201
Cdd:PLN00009  74 KRLYLVFEYLDL-DLKKHMDSSPDFAKnpRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLARA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  202 FVAdeTERAYSF-CGTIEYMAPDIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRI--------- 271
Cdd:PLN00009 153 FGI--PVRTFTHeVVTLWYRAPEILLGSRH-YSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILgtpneetwp 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297  272 -LKSEPPY--------PQEMSALAK-------DLIQRLLMKDPKKRLgcgprDADEIKEHLFFQKI 321
Cdd:PLN00009 230 gVTSLPDYksafpkwpPKDLATVVPtlepagvDLLSKMLRLDPSKRI-----TARAALEHEYFKDL 290
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
49-255 7.56e-12

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 66.25  E-value: 7.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkativqkakttehtrterqvLEH--------IRQSPFL------ 114
Cdd:cd07844   2 YKKLDKLGEGSYATVY---KGRSKLTGQLVALKEIR--------------------LEHeegapftaIREASLLkdlkha 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 115 --VTLHYAFQTETKLHLILDYINGgELFTHLSQRERFTE-HEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHV 191
Cdd:cd07844  59 niVTLHDIIHTKKTLTLVFEYLDT-DLKQYMDDCGGGLSmHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGEL 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 192 VLTDFGLSK-EFVADETeraYSF-CGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd07844 138 KLADFGLARaKSVPSKT---YSNeVVTLWYRPPDVLLGS-TEYSTSLDMWGVGCIFYEMATGRPLF 199
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
151-334 7.97e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 66.98  E-value: 7.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 151 EHEVQIYV-GEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFcgTIEYMAPDIVRGgd 229
Cdd:cd07876 121 DHERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVV--TRYYRAPEVILG-- 196
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 230 SGHDKAVDWWSLGVLMYELLTGASPF-----------------TVDGE-KNSQAEISRRILKSEPPYP----QEM----- 282
Cdd:cd07876 197 MGYKENVDIWSVGCIMGELVKGSVIFqgtdhidqwnkvieqlgTPSAEfMNRLQPTVRNYVENRPQYPgisfEELfpdwi 276
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 283 -----------SALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFFQKinWDDLAAKKVPAP 334
Cdd:cd07876 277 fpseserdklkTSQARDLLSKMLVIDPDKRI-----SVDEALRHPYITV--WYDPAEAEAPPP 332
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
457-546 9.56e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 65.53  E-value: 9.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 457 ISKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFERI--KKKKHFSETEASYIMRKLVSAVSH 534
Cdd:cd08221  38 LSEKERRDALNEIDILSLLN-HDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIaqQKNQLFPEEVVLWYLYQIVSAVSH 116
                        90
                ....*....|..
gi 32528297 535 MHDVGVVHRDLK 546
Cdd:cd08221 117 IHKAGILHRDIK 128
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
49-255 9.57e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 65.69  E-value: 9.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKISGHD-TGKLYAMKVLKKATIVQkakTTEHTRTERQVL-----EHIrqspflvtLHY--- 119
Cdd:cd05080   6 LKKIRDLGEGHFGKVSLYCYDPTNDgTGEMVAVKALKADCGPQ---HRSGWKQEIDILktlyhENI--------VKYkgc 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 -AFQTETKLHLILDYINGGELFTHLSqRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGL 198
Cdd:cd05080  75 cSEQGGKSLQLIMEYVPLGSLRDYLP-KHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGL 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 199 SKEFVADETERAYSFCGT--IEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd05080 154 AKAVPEGHEYYRVREDGDspVFWYAPECLK--EYKFYYASDVWSFGVTLYELLTHCDSS 210
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
46-301 1.01e-11

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 65.28  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKATIVQK--AKTTEHTRterqvLEHIRQSPFL-VTLHyafq 122
Cdd:cd05083   5 LQKLTLGEIIGEGEFGAVL-----QGEYMGQKVAVKNIKCDVTAQAflEETAVMTK-----LQHKNLVRLLgVILH---- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 teTKLHLILDYINGGELFTHLSQRERFTEHEVQ--IYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK 200
Cdd:cd05083  71 --NGLYIVMELMSKGNLVNFLRSRGRALVPVIQllQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 -EFVADETERAysfcgTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFTvdgeKNSQAEISRRILKS---E 275
Cdd:cd05083 149 vGSMGVDNSRL-----PVKWTAPEALKNKK--FSSKSDVWSYGVLLWEVFSyGRAPYP----KMSVKEVKEAVEKGyrmE 217
                       250       260
                ....*....|....*....|....*.
gi 32528297 276 PpyPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd05083 218 P--PEGCPPDVYSIMTSCWEAEPGKR 241
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
432-547 1.02e-11

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 65.60  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKcVHKKSNQA--FAVKIIS------KRMEANTQK-------EITALKLCEGHPNIVKLHEVFHDQLHTFL 496
Cdd:cd08528   8 LGSGAFGCVYK-VRKKSNGQtlLALKEINmtnpafGRTEQERDKsvgdiisEVNIIKEQLRHPNIVRYYKTFLENDRLYI 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 497 VMELLNG---GELFERIKKKK-HFSETEASYIMRKLVSAVSHMH-DVGVVHRDLKP 547
Cdd:cd08528  87 VMELIEGaplGEHFSSLKEKNeHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKP 142
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
432-547 1.05e-11

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 65.66  E-value: 1.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIskRMEanTQKE---ITAL-------KLCegHPNIVKLHEVFHDQLH------TF 495
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVALKKI--RME--NEKEgfpITAIreikllqKLD--HPNVVRLKEIVTSKGSakykgsIY 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 496 LVMEL----LNGgeLFERikKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07840  81 MVFEYmdhdLTG--LLDN--PEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKG 132
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
55-255 1.07e-11

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 65.60  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLvrkisGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAfQTETKLHLILDYI 134
Cdd:cd14158  23 LGEGGFGVVFK-----GYINDKNVAVKKLAAMVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYS-CDGPQLCLVYTYM 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFTEHEVQ----IYVGEiVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD----E 206
Cdd:cd14158  97 PNGSLLDRLACLNDTPPLSWHmrckIAQGT-ANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFsqtiM 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 207 TERaysFCGTIEYMAPDIVRGGDSghdKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd14158 176 TER---IVGTTAYMAPEALRGEIT---PKSDIFSFGVVLLEIITGLPPV 218
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
49-301 1.22e-11

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 65.43  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVF-LVRKISGHdtgkLYAMKVLKKATivqkAKTTEHTRTERQVLEH--IRQSPFLVTLHYAFQTET 125
Cdd:cd14138   7 FHELEKIGSGEFGSVFkCVKRLDGC----IYAIKRSKKPL----AGSVDEQNALREVYAHavLGQHSHVVRYYSAWAEDD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRER----FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD--------------- 186
Cdd:cd14138  79 HMLIQNEYCNGGSLADAISENYRimsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISrtsipnaaseegded 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 187 --SNGHVV--LTDFGLSKEFVADETERaysfcGTIEYMAPDIVRgGDSGHDKAVDWWSLGVLMYElLTGASPFTVDGEKn 262
Cdd:cd14138 159 ewASNKVIfkIGDLGHVTRVSSPQVEE-----GDSRFLANEVLQ-ENYTHLPKADIFALALTVVC-AAGAEPLPTNGDQ- 230
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 32528297 263 sQAEISRRILksePPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14138 231 -WHEIRQGKL---PRIPQVLSQEFLDLLKVMIHPDPERR 265
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
54-248 1.31e-11

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 65.54  E-value: 1.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  54 VLGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKAtivQKAKTTEHTRTERQV-LEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd13998   2 VIGKGRFGEVW-----KASLKNEPVAVKIFSSR---DKQSWFREKEIYRTPmLKHENILQFIAADERDTALRTELWLVTA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLsQRERFTEHEVQIYVGEIVLALEHLH---------KLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV 203
Cdd:cd13998  74 FHPNGSL*DYL-SLHTIDWVSLCRLALSVARGLAHLHseipgctqgKPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLS 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 204 ADETE---RAYSFCGTIEYMAPDIVRGGDSGHD----KAVDWWSLGVLMYEL 248
Cdd:cd13998 153 PSTGEednANNGQVGTKRYMAPEVLEGAINLRDfesfKRVDIYAMGLVLWEM 204
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
55-301 1.38e-11

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 65.21  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLV-RKISGHdtgklyamkvlkkatIVQKAKTTEHTRTERQ--VLE-----HIRQSPFLVTLHYAFQTETK 126
Cdd:cd14027   1 LDSGGFGKVSLCfHRTQGL---------------VVLKTVYTGPNCIEHNeaLLEegkmmNRLRHSRVVKLLGVILEEGK 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVgEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS-----KE 201
Cdd:cd14027  66 YSLVMEYMEKGNLMHVLKKVSVPLSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 FVADETER-------AYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgeKNSQAE--ISRRIL 272
Cdd:cd14027 145 LTKEEHNEqrevdgtAKKNAGTLYYMAPEHLNDVNAKPTEKSDVYSFAIVLWAIFANKEPY-----ENAINEdqIIMCIK 219
                       250       260       270
                ....*....|....*....|....*....|...
gi 32528297 273 KSEPP----YPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14027 220 SGNRPdvddITEYCPREIIDLMKLCWEANPEAR 252
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
432-547 1.43e-11

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 64.91  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII----SKRMEANTQKEITAlklCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELF 507
Cdd:cd14107  10 IGRGTFGFVKRVTHKGNGECCAAKFIplrsSTRARAFQERDILA---RLSHRRLTCLLDQFETRKTLILILELCSSEELL 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 508 ERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14107  87 DRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKP 126
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
17-355 1.65e-11

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 66.21  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   17 DGGDGGEQLLTVKHEL-RTANltghaekvgiENFELLKVLGTGAYGKVFLVRKIsghDTGKLYAMKvlkkaTIVQKAKTT 95
Cdd:PTZ00036  45 NAGEDEDEEKMIDNDInRSPN----------KSYKLGNIIGNGSFGVVYEAICI---DTSEKVAIK-----KVLQDPQYK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   96 EHTRTERQVLEHIrQSPFLVTLHY--AFQTETK---LHLILDYI--NGGELFTHLSQRER-FTEHEVQIYVGEIVLALEH 167
Cdd:PTZ00036 107 NRELLIMKNLNHI-NIIFLKDYYYteCFKKNEKnifLNVVMEFIpqTVHKYMKHYARNNHaLPLFLVKLYSYQLCRALAY 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  168 LHKLGIIYRDIKLENILLDSNGHVV-LTDFGLSKEFVADetERAYSFCGTIEYMAPDIVRGGdSGHDKAVDWWSLGVLMY 246
Cdd:PTZ00036 186 IHSKFICHRDLKPQNLLIDPNTHTLkLCDFGSAKNLLAG--QRSVSYICSRFYRAPELMLGA-TNYTTHIDLWSLGCIIA 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  247 ELLTGASPFTvdgEKNSQAEISRRI----------LKSEPP------------------YPQEMSALAKDLIQRLLMKDP 298
Cdd:PTZ00036 263 EMILGYPIFS---GQSSVDQLVRIIqvlgtptedqLKEMNPnyadikfpdvkpkdlkkvFPKGTPDDAINFISQFLKYEP 339
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297  299 KKRLGCGPRDADEikehlFFqkinwDDLaakKVPAPFKPVIRDEL-DVSNFA-EEFTEM 355
Cdd:PTZ00036 340 LKRLNPIEALADP-----FF-----DDL---RDPCIKLPKYIDKLpDLFNFCdAEIKEM 385
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
432-546 1.76e-11

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 65.03  E-value: 1.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIS--KRMEANTQKEITALKLCEGHPNIVKLHEVFH-------DQLhtFLVMELLN 502
Cdd:cd06638  26 IGKGTYGKVFKVLNKKNGSKAAVKILDpiHDIDEEIEAEYNILKALSDHPNVVKFYGMYYkkdvkngDQL--WLVLELCN 103
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 503 GGELFERIK----KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06638 104 GGSVTDLVKgflkRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVK 151
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
428-547 1.77e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 65.29  E-value: 1.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEI--TALK----LCE-GHPNIVKLHEVF-HDQ-LHtfLVM 498
Cdd:cd07841   4 KGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDGInfTALReiklLQElKHPNIIGLLDVFgHKSnIN--LVF 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 499 ELLnGGELFERIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07841  82 EFM-ETDLEKVIKDKSIvLTPADIKSYMLMTLRGLEYLHSNWILHRDLKP 130
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
138-283 1.84e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 66.45  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  138 ELFTHLSQRERFTEH-EVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGlSKEFV--ADETERAYSFC 214
Cdd:PHA03211 245 DLYTYLGARLRPLGLaQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFG-AACFArgSWSTPFHYGIA 323
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297  215 GTIEYMAPDIVrGGDSgHDKAVDWWSLGVLMYEL-LTGASPFTV---DGEKNSQAEISrRILKSEPPYPQEMS 283
Cdd:PHA03211 324 GTVDTNAPEVL-AGDP-YTPSVDIWSAGLVIFEAaVHTASLFSAsrgDERRPYDAQIL-RIIRQAQVHVDEFP 393
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
53-301 1.90e-11

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 64.55  E-value: 1.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVrkiSGHDTGKLyAMKVLKKATIvqkakTTEHTRTERQVLEHIRQSPfLVTLhYAFQTETKLHLILD 132
Cdd:cd14203   1 VKLGQGCFGEVWMG---TWNGTTKV-AIKTLKPGTM-----SPEAFLEEAQIMKKLRHDK-LVQL-YAVVSEEPIYIVTE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLSQRE-------RFTEHEVQIYVGeivlaLEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD 205
Cdd:cd14203  70 FMSKGSLLDFLKDGEgkylklpQLVDMAAQIASG-----MAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDN 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPF--TVDGEKNSQAEISRRIlksepPYPQEM 282
Cdd:cd14203 145 EYTARQGAKFPIKWTAPEAALYGR--FTIKSDVWSFGILLTELVTkGRVPYpgMNNREVLEQVERGYRM-----PCPPGC 217
                       250
                ....*....|....*....
gi 32528297 283 SALAKDLIQRLLMKDPKKR 301
Cdd:cd14203 218 PESLHELMCQCWRKDPEER 236
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
55-259 1.92e-11

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 65.23  E-value: 1.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisghdTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLhLILDYI 134
Cdd:cd14159   1 IGEGGFGCVYQAVM-----RNTEYAVKRLKEDSELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYC-LIYVYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHLSQRERFT----EHEVQIYVGEiVLALEHLHKL--GIIYRDIKLENILLDSNGHVVLTDFGLSK--EFVADE 206
Cdd:cd14159  75 PNGSLEDRLHCQVSCPclswSQRLHVLLGT-ARAIQYLHSDspSLIHGDVKSSNILLDAALNPKLGDFGLARfsRRPKQP 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32528297 207 TE-----RAYSFCGTIEYMAPDIVRGGDSGHDkaVDWWSLGVLMYELLTGASPFTVDG 259
Cdd:cd14159 154 GMsstlaRTQTVRGTLAYLPEEYVKTGTLSVE--IDVYSFGVVLLELLTGRRAMEVDS 209
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
48-255 1.96e-11

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 64.98  E-value: 1.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKV-----FLVRKISGHDTgklYAMKVLKKativqKAKTTEHTR--TERQVLEHIRQsPFLVTLHYA 120
Cdd:cd05045   1 NLVLGKTLGEGEFGKVvkataFRLKGRAGYTT---VAVKMLKE-----NASSSELRDllSEFNLLKQVNH-PHVIKLYGA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 121 FQTETKLHLILDYINGGEL--FTHLSQR----------------------ERFTEHEVQIYVGEIVLALEHLHKLGIIYR 176
Cdd:cd05045  72 CSQDGPLLLIVEYAKYGSLrsFLRESRKvgpsylgsdgnrnssyldnpdeRALTMGDLISFAWQISRGMQYLAEMKLVHR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 177 DIKLENILLDSNGHVVLTDFGLSKEFVADET--ERAYSFCgTIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLT-GAS 253
Cdd:cd05045 152 DLAARNVLVAEGRKMKISDFGLSRDVYEEDSyvKRSKGRI-PVKWMAIESL--FDHIYTTQSDVWSFGVLLWEIVTlGGN 228

                ..
gi 32528297 254 PF 255
Cdd:cd05045 229 PY 230
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
424-546 2.03e-11

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 65.82  E-value: 2.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN------TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd05618  21 DFDLL-RVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDdedidwVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFV 99
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05618 100 IEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLK 148
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
427-546 2.37e-11

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 64.18  E-value: 2.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIISK-RMEANTQKE--ITALKLCEG--HPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd14189   4 CKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHsRVAKPHQREkiVNEIELHRDlhHKHVVKFSHHFEDAENIYIFLELC 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 502 NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd14189  84 SRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLK 128
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
430-548 2.42e-11

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 64.21  E-value: 2.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIIS------KRMEAnTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd08225   6 KKIGEGSFGKIYLAKAKSDSEHCVIKEIDltkmpvKEKEA-SKKEVILLAKMK-HPNIVTFFASFQENGRLFIVMEYCDG 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 504 GELFERIKKKKH--FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd08225  84 GDLMKRINRQRGvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQ 130
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
50-268 2.48e-11

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 64.60  E-value: 2.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  50 ELLKVLGTGAYGKVFLVR----------KISGHDTGKLyamKVLKKATIvqkakTTEHTRTERQVLehirqspflvtLHY 119
Cdd:cd14152   3 ELGELIGQGRWGKVHRGRwhgevairllEIDGNNQDHL---KLFKKEVM-----NYRQTRHENVVL-----------FMG 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 AFQTETKLHLILDYINGGELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDsNGHVVLTDFGL 198
Cdd:cd14152  64 ACMHPPHLAIITSFCKGRTLYSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 -SKEFVADETERAYSFC---GTIEYMAPDIVRGGDSGHD-------KAVDWWSLGVLMYELLTGASPFtvdgeKNSQAEI 267
Cdd:cd14152 143 fGISGVVQEGRRENELKlphDWLCYLAPEIVREMTPGKDedclpfsKAADVYAFGTIWYELQARDWPL-----KNQPAEA 217

                .
gi 32528297 268 S 268
Cdd:cd14152 218 L 218
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
52-295 2.49e-11

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 64.55  E-value: 2.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATIVQKAKTtEHTRTERQVLEHIRQSPFLVTLHYAFQTETkLHLIL 131
Cdd:cd14026   2 LRYLSRGAFGTVSRARH---ADWRVTVAIKCLKLDSPVGDSER-NCLLKEAEILHKARFSYILPILGICNEPEF-LGIVT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLsqrerfteHEVQIY-----------VGEIVLALEHLHKLG--IIYRDIKLENILLDSNGHVVLTDFGL 198
Cdd:cd14026  77 EYMTNGSLNELL--------HEKDIYpdvawplrlriLYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SK----EFVADETERAYSFCGTIEYMAP-DIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISRRILK 273
Cdd:cd14026 149 SKwrqlSISQSRSSKSAPEGGTIIYMPPeEYEPSQKRRASVKHDIYSYAIIMWEVLSRKIPFE---EVTNPLQIMYSVSQ 225
                       250       260
                ....*....|....*....|..
gi 32528297 274 SEPPYPQEMSaLAKDLIQRLLM 295
Cdd:cd14026 226 GHRPDTGEDS-LPVDIPHRATL 246
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
428-548 2.56e-11

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 64.45  E-value: 2.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQ-------KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:cd07860   4 KVEKIGEGTYGVVYKARNKLTGEVVALKKI--RLDTETEgvpstaiREISLLKELN-HPNIVKLLDVIHTENKLYLVFEF 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 501 LNGgelferiKKKKHFSETEASYI--------MRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07860  81 LHQ-------DLKKFMDASALTGIplpliksyLFQLLQGLAFCHSHRVLHRDLKPQ 129
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
432-548 2.65e-11

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 64.62  E-value: 2.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQ-------KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGg 504
Cdd:cd07835   7 IGEGTYGVVYKARDKLTGEIVALKKI--RLETEDEgvpstaiREISLLKELN-HPNIVRLLDVVHSENKLYLVFEFLDL- 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 505 ELFERIKKKKHFSETEA---SYiMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07835  83 DLKKYMDSSPLTGLDPPlikSY-LYQLLQGIAFCHSHRVLHRDLKPQ 128
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
430-546 2.68e-11

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 64.97  E-value: 2.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR---MEAN---TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDvvlIDDDvecTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05620  81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLK 123
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
47-316 2.75e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 64.05  E-value: 2.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKkaTIVQKAkttehtrtERQV-----LEHirqsPFLVTLHYAF 121
Cdd:cd14047   6 QDFKEIELIGSGGFGQVF---KAKHRIDGKTYAIKRVK--LNNEKA--------EREVkalakLDH----PNIVRYNGCW 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 Q----------------TETKLHLILDYINGGELFTHLSQR--ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENI 183
Cdd:cd14047  69 DgfdydpetsssnssrsKTKCLFIQMEFCEKGTLESWIEKRngEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 184 LLDSNGHVVLTDFGLSKEfVADETERAYSFcGTIEYMAPDivRGGDSGHDKAVDWWSLGVLMYELLTGASpftvdgEKNS 263
Cdd:cd14047 149 FLVDTGKVKIGDFGLVTS-LKNDGKRTKSK-GTLSYMSPE--QISSQDYGKEVDIYALGLILFELLHVCD------SAFE 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 264 QAEISRRILKSE-PPYPQEMSALAKDLIQRLLMKDPKKRlgcgpRDADEIKEHL 316
Cdd:cd14047 219 KSKFWTDLRNGIlPDIFDKRYKIEKTIIKKMLSKKPEDR-----PNASEILRTL 267
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
432-548 2.76e-11

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 64.96  E-value: 2.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK--EITALKLC------EGHPNIVKLHEVFHDQLHTFLVMELLnG 503
Cdd:cd14212   7 LGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAmlEIAILTLLntkydpEDKHHIVRLLDHFMHHGHLCIVFELL-G 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 504 GELFERIKKKKH--FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14212  86 VNLYELLKQNQFrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPE 132
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
143-251 2.82e-11

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 64.05  E-value: 2.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 143 LSQRERfteheVQIYVgEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGlskeFVADETERAYSFCGTIEYMAP 222
Cdd:cd13975  99 LSLEER-----LQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLG----FCKPEAMMSGSIVGTPIHMAP 168
                        90       100       110
                ....*....|....*....|....*....|
gi 32528297 223 DIVrggdSGH-DKAVDWWSLGVLMYELLTG 251
Cdd:cd13975 169 ELF----SGKyDNSVDVYAFGILFWYLCAG 194
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
432-546 3.16e-11

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 64.24  E-value: 3.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIS--KRMEANTQKEITALKLCEGHPNIVKLHEVFH--DQL---HTFLVMELLNGG 504
Cdd:cd06639  30 IGKGTYGKVYKVTNKKDGSLAAVKILDpiSDVDEEIEAEYNILRSLPNHPNVVKFYGMFYkaDQYvggQLWLVLELCNGG 109
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 505 ELFERIK----KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06639 110 SVTELVKgllkCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVK 155
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
434-547 3.37e-11

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 64.17  E-value: 3.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 434 EGSFSICRKCVHKKSNQAFAVKIIskRMEanTQKE---ITALK-----LCEGHPNIVKLHEVF----HDQLhtFLVMEL- 500
Cdd:cd07843  15 EGTYGVVYRARDKKTGEIVALKKL--KME--KEKEgfpITSLReinilLKLQHPNIVTVKEVVvgsnLDKI--YMVMEYv 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 501 ---LNGgeLFERikKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07843  89 ehdLKS--LMET--MKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKT 134
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
160-304 3.51e-11

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 63.83  E-value: 3.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 160 EIVLALEHLHKLGIIYRDIKLENIL---LDSNGHV--VLTDFGLSKEFVAdetERAYSFCGTIEYMAPDIVRGgdSGHDK 234
Cdd:cd14067 122 QIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEHIniKLSDYGISRQSFH---EGALGVEGTPGYQAPEIRPR--IVYDE 196
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 235 AVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPY---PQEMSALAkdlIQRLLMK----DPKKRLGC 304
Cdd:cd14067 197 KVDMFSYGMVLYELLSGQRPSL----GHHQLQIAKKLSKGIRPVlgqPEEVQFFR---LQALMMEcwdtKPEKRPLA 266
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
79-288 3.89e-11

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 63.81  E-value: 3.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  79 AMKVLKKATivQKAKTTEHTRtERQVLeHIRQSPFLVTLHYAFQTETkLHLILDYINGGELFTHLS-QRERFTEHEVQIY 157
Cdd:cd05115  35 AIKVLKQGN--EKAVRDEMMR-EAQIM-HQLDNPYIVRMIGVCEAEA-LMLVMEMASGGPLNKFLSgKKDEITVSNVVEL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 158 VGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGT--IEYMAPDIV--RGGDSGHD 233
Cdd:cd05115 110 MHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKARSAGKwpLKWYAPECInfRKFSSRSD 189
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32528297 234 KavdwWSLGVLMYELLT-GASPF-TVDG-EKNSQAEISRRiLKSEPPYPQEMSALAKD 288
Cdd:cd05115 190 V----WSYGVTMWEAFSyGQKPYkKMKGpEVMSFIEQGKR-MDCPAECPPEMYALMSD 242
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
432-548 4.10e-11

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 63.93  E-value: 4.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVK-IISKRMEANTQK----EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd07847   9 IGEGSYGVVFKCRNRETGQIVAIKkFVESEDDPVIKKialrEIRMLKQLK-HPNLVNLIEVFRRKRKLHLVFEYCDHTVL 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07847  88 NELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPE 129
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
428-546 4.21e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 63.60  E-value: 4.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKII-----SKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd08220   4 KIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveqmTKEERQAALNEVKVLSMLH-HPNIIEYYESFLEDKALMIVMEYAP 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKH--FSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd08220  83 GGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLK 128
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
53-255 4.21e-11

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 63.73  E-value: 4.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRkisghdtgklyaMKVLKKATIVQKAKTTEHTRTERQVLEHIRQS--------PFLVTLHYAFQTE 124
Cdd:cd05066  10 KVIGAGEFGEVCSGR------------LKLPGKREIPVAIKTLKAGYTEKQRRDFLSEAsimgqfdhPNIIHLEGVVTRS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKeFV 203
Cdd:cd05066  78 KPVMIVTEYMENGSLDAFLRKHDgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSR-VL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32528297 204 ADETERAYSFCG---TIEYMAPDIV--RGGDSghdkAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05066 157 EDDPEAAYTTRGgkiPIRWTAPEAIayRKFTS----ASDVWSYGIVMWEVMSyGERPY 210
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
55-287 4.37e-11

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 63.44  E-value: 4.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKV----FLVRKisghdTGKLYAMKVLKKATivQKAKTTEHTRTERQVLEHIrQSPFLVTLHYAFQTETkLHLI 130
Cdd:cd05116   3 LGSGNFGTVkkgyYQMKK-----VVKTVAVKILKNEA--NDPALKDELLREANVMQQL-DNPYIVRMIGICEAES-WMLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERA 210
Cdd:cd05116  74 MEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 211 YSFCGT--IEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLT-GASPFT-VDGEKNSQAEISRRILKSEPPYPQEMSALA 286
Cdd:cd05116 154 AQTHGKwpVKWYAPECMNY--YKFSSKSDVWSFGVLMWEAFSyGQKPYKgMKGNEVTQMIEKGERMECPAGCPPEMYDLM 231

                .
gi 32528297 287 K 287
Cdd:cd05116 232 K 232
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
430-548 5.75e-11

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 64.29  E-value: 5.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK--RMEANTQKEITALK--LCEGHPN-IVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd05628   7 KVIGRGAFGEVRLVQKKDTGHVYAMKILRKadMLEKEQVGHIRAERdiLVEADSLwVVKMFYSFQDKLNLYLIMEFLPGG 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05628  87 DMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPD 130
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
428-545 6.11e-11

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 62.93  E-value: 6.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    428 KDKPLGEGSFSICRKCVHKKSNQAF----AVKIIskRMEANTQ------KEITALKLCEgHPNIVKLHEVFHDQLHTFLV 497
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKLKGKGGKKkvevAVKTL--KEDASEQqieeflREARIMRKLD-HPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 32528297    498 MELLNGGELFERIKKKKH-FSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRPkLSLSDLLSFALQIARGMEYLESKNFIHRDL 128
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
52-256 7.62e-11

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 63.05  E-value: 7.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKISGHDTGKL-YAMKVLKKATIVQK-AKTTEHTRTERQvLEHirqsPFLVTLhYAFQTETKLHL 129
Cdd:cd05111  12 LKVLGSGVFGTVHKGIWIPEGDSIKIpVAIKVIQDRSGRQSfQAVTDHMLAIGS-LDH----AYIVRL-LGICPGASLQL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQR------ERFTEHEVQIYVGeivlaLEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV 203
Cdd:cd05111  86 VTQLLPLGSLLDHVRQHrgslgpQLLLNWCVQIAKG-----MYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLY 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 204 ADETERAYSFCGT-IEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLT-GASPFT 256
Cdd:cd05111 161 PDDKKYFYSEAKTpIKWMALESIHFGKYTHQS--DVWSYGVTVWEMMTfGAEPYA 213
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
47-301 7.85e-11

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 62.87  E-value: 7.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVrKISGHDTGKLYAMkVLKKATivqkakttEHTRTERQVLEHIRQSPFLVTLHYAFQT--- 123
Cdd:cd05046   5 SNLQEITTLGRGEFGEVFLA-KAKGIEEEGGETL-VLVKAL--------QKTKDENLQSEFRRELDMFRKLSHKNVVrll 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ----ETKLH-LILDYINGGEL--FTHLSQRERF--------TEHEVQIyVGEIVLALEHLHKLGIIYRDIKLENILLDSN 188
Cdd:cd05046  75 glcrEAEPHyMILEYTDLGDLkqFLRATKSKDEklkppplsTKQKVAL-CTQIALGMDHLSNARFVHRDLAARNCLVSSQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 189 GHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFtvdgEKNSQAEI 267
Cdd:cd05046 154 REVKVSLLSLSKDVYNSEYYKLRNALIPLRWLAPEAVQEDD--FSTKSDVWSFGVLMWEVFTqGELPF----YGLSDEEV 227
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 32528297 268 SRRIL--KSEPPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd05046 228 LNRLQagKLELPVPEGCPSRLYKLMTRCWAVNPKDR 263
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
46-301 8.03e-11

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 62.75  E-value: 8.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLvrkisGHDTGKLYAMKVLKK-ATIVQK--AKTTEHTRterqvLEHirqsPFLVTLHYAFQ 122
Cdd:cd05039   5 KKDLKLGELIGKGEFGDVML-----GDYRGQKVAVKCLKDdSTAAQAflAEASVMTT-----LRH----PNLVQLLGVVL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGGELFTHLSQRER--FTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK 200
Cdd:cd05039  71 EGNGLYIVTEYMAKGSLVDYLRSRGRavITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EfvADETERAYSFcgTIEYMAPDIVRGGDSGhDKAvDWWSLGVLMYELLT-GASPFTvdgeKNSQAEISRRILKS---EP 276
Cdd:cd05039 151 E--ASSNQDGGKL--PIKWTAPEALREKKFS-TKS-DVWSFGILLWEIYSfGRVPYP----RIPLKDVVPHVEKGyrmEA 220
                       250       260
                ....*....|....*....|....*..
gi 32528297 277 PY--PQEMSALAKDLIQrllmKDPKKR 301
Cdd:cd05039 221 PEgcPPEVYKVMKNCWE----LDPAKR 243
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
48-315 8.30e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 62.97  E-value: 8.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISGHDTgklYAMKVLKKATivqkaKTTEHTRTERQV-----LEHirqsPFLVTLHYAF- 121
Cdd:cd14048   7 DFEPIQCLGRGGFGVVFEAKNKVDDCN---YAVKRIRLPN-----NELAREKVLREVralakLDH----PGIVRYFNAWl 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 --------QTETKLHLIL-----------DYINGGelfTHLSQRERFTEHEVQIyvgEIVLALEHLHKLGIIYRDIKLEN 182
Cdd:cd14048  75 erppegwqEKMDEVYLYIqmqlcrkenlkDWMNRR---CTMESRELFVCLNIFK---QIASAVEYLHSKGLIHRDLKPSN 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 183 ILLDSNGHVVLTDFGLSKEFVADETER-------AYSF----CGTIEYMAPDIVRGGDSGHDkaVDWWSLGVLMYELLTg 251
Cdd:cd14048 149 VFFSLDDVVKVGDFGLVTAMDQGEPEQtvltpmpAYAKhtgqVGTRLYMSPEQIHGNQYSEK--VDIFALGLILFELIY- 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32528297 252 asPFTVDGEKNSQAEISRRiLKSEP----PYPQEmsalaKDLIQRLLMKDPKKRlgcgPrDADEIKEH 315
Cdd:cd14048 226 --SFSTQMERIRTLTDVRK-LKFPAlftnKYPEE-----RDMVQQMLSPSPSER----P-EAHEVIEH 280
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
478-548 8.63e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.43  E-value: 8.63e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297  478 HPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:NF033483  66 HPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQ 136
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
139-302 8.71e-11

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 62.66  E-value: 8.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 139 LFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE--------------FVA 204
Cdd:cd13980  84 LYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKPtylpednpadfsyfFDT 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAY----SFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFTVDG---EKNSQAEISRRILKSEP 276
Cdd:cd13980 164 SRRRTCYiapeRFVDALTLDAESERRDGE--LTPAMDIFSLGCVIAELFTeGRPLFDLSQllaYRKGEFSPEQVLEKIED 241
                       170       180
                ....*....|....*....|....*.
gi 32528297 277 PYPQEMsalakdlIQRLLMKDPKKRL 302
Cdd:cd13980 242 PNIREL-------ILHMIQRDPSKRL 260
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
430-548 8.97e-11

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 63.49  E-value: 8.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSF---SICRKcvhKKSNQAFAVKIISKR--MEANTQKEITALK--LCEG-HPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd05598   7 KTIGVGAFgevSLVRK---KDTNALYAMKTLRKKdvLKRNQVAHVKAERdiLAEAdNEWVVKLYYSFQDKENLYFVMDYI 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05598  84 PGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPD 130
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
428-545 9.19e-11

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 62.57  E-value: 9.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    428 KDKPLGEGSFSICRKCVHKKSNQAF----AVKIIskRMEANTQ------KEITALKLCEgHPNIVKLHEVFHDQLHTFLV 497
Cdd:smart00221   3 LGKKLGEGAFGEVYKGTLKGKGDGKevevAVKTL--KEDASEQqieeflREARIMRKLD-HPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297    498 MELLNGGELFERIKKKKHFSETeasyiMRKLVS-------AVSHMHDVGVVHRDL 545
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRPKELS-----LSDLLSfalqiarGMEYLESKNFIHRDL 129
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
55-301 9.26e-11

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 62.26  E-value: 9.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRkISGHDTgkLYAMKVLKKATIVQ-KAKTTEHTRTERQvLEHirqsPFLVTLHYAFQTETKLHLILDY 133
Cdd:cd05084   4 IGRGNFGEVFSGR-LRADNT--PVAVKSCRETLPPDlKAKFLQEARILKQ-YSH----PNIVRLIGVCTQKQPIYIVMEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 134 INGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEfvadETERAYS 212
Cdd:cd05084  76 VQGGDFLTFLrTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSRE----EEDGVYA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 213 FCG-----TIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFTVDGEKNSQAEISRRIlksEPPYPQEMSALA 286
Cdd:cd05084 152 ATGgmkqiPVKWTAPEALNYGR--YSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAVEQGV---RLPCPENCPDEV 226
                       250
                ....*....|....*
gi 32528297 287 KDLIQRLLMKDPKKR 301
Cdd:cd05084 227 YRLMEQCWEYDPRKR 241
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
430-548 1.14e-10

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 63.54  E-value: 1.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR--MEANTQKEITALK--LCEGHPN-IVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd05627   8 KVIGRGAFGEVRLVQKKDTGHIYAMKILRKAdmLEKEQVAHIRAERdiLVEADGAwVVKMFYSFQDKRNLYLIMEFLPGG 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05627  88 DMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPD 131
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
432-548 1.18e-10

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 62.68  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR-----MEANTQKEITALKLCE--GHPNIVKLHEVFH-----DQLHTFLVME 499
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRFVALKKVRVPlseegIPLSTIREIALLKQLEsfEHPNVVRLLDVCHgprtdRELKLTLVFE 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 500 LLNGgELFERIKK--KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07838  87 HVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQ 136
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
43-301 1.25e-10

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 62.39  E-value: 1.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  43 KVGIENFELLKVLGTGAYGKVFLvrkisGHDTGKL-YAMKVLKKATIvqkakTTEHTRTERQVLEHIRQSPfLVTLhYAF 121
Cdd:cd05070   5 EIPRESLQLIKRLGNGQFGEVWM-----GTWNGNTkVAIKTLKPGTM-----SPESFLEEAQIMKKLKHDK-LVQL-YAV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQRE-------RFTEHEVQIYVGeivlaLEHLHKLGIIYRDIKLENILLDSNGHVVLT 194
Cdd:cd05070  73 VSEEPIYIVTEYMSKGSLLDFLKDGEgralklpNLVDMAAQVAAG-----MAYIERMNYIHRDLRSANILVGNGLICKIA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 195 DFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFTVDGEKNSQAEISRrilK 273
Cdd:cd05070 148 DFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGR--FTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVER---G 222
                       250       260
                ....*....|....*....|....*...
gi 32528297 274 SEPPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd05070 223 YRMPCPQDCPISLHELMIHCWKKDPEER 250
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
424-546 1.41e-10

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 63.12  E-value: 1.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN------TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd05617  16 DFDLI-RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDdedidwVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLV 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05617  95 IEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLK 143
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
428-548 1.60e-10

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 61.56  E-value: 1.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKII--SKRMEANTQKEITALKLCE---GHPNIVKLHEVFHDQLHTFLVMELLn 502
Cdd:cd14050   5 ILSKLGEGSFGEVFKVRSREDGKLYAVKRSrsRFRGEKDRKRKLEEVERHEklgEHPNCVRFIKAWEEKGILYIQTELC- 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14050  84 DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPA 129
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
154-251 1.61e-10

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 62.63  E-value: 1.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 154 VQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV-LTDFGlSKEFVADETERAY---SFcgtieYMAPDIVRGgd 229
Cdd:cd14135 107 VRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTLkLCDFG-SASDIGENEITPYlvsRF-----YRAPEIILG-- 178
                        90       100
                ....*....|....*....|..
gi 32528297 230 SGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14135 179 LPYDYPIDMWSVGCTLYELYTG 200
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
432-548 1.63e-10

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 62.19  E-value: 1.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM--EANTQKEITALKLCEgHPNIVKLHEVF--HDQLhtFLVMELLNGGELF 507
Cdd:cd14104   8 LGRGQFGIVHRCVETSSKKTYMAKFVKVKGadQVLVKKEISILNIAR-HRNILRLHESFesHEEL--VMIFEFISGVDIF 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 508 ERIKKKK-HFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14104  85 ERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPE 126
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
430-548 1.67e-10

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 62.13  E-value: 1.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVK--IISKR---MEANTQKEItalklceGHPNIVKLHEVFH------DQLHTFLVM 498
Cdd:cd14137  10 KVIGSGSFGVVYQAKLLETGEVVAIKkvLQDKRyknRELQIMRRL-------KHPNIVKLKYFFYssgekkDEVYLNLVM 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 499 ELLNGgELFERIKK----KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14137  83 EYMPE-TLYRVIRHysknKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQ 135
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
432-548 1.76e-10

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 58.99  E-value: 1.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIS---KRMEANTQKEITALKLCEGH-PNIVKLHEVF-HDQLHtFLVMELLNGGEL 506
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDdvnNEEGEDLESEMDILRRLKGLeLNIPKVLVTEdVDGPN-ILLMELVKGGTL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 507 FERIKKKKHFS-ETEAsyIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd13968  80 IAYTQEEELDEkDVES--IMYQLAECMRLLHSFHLIHRDLNND 120
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
51-299 1.81e-10

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 61.95  E-value: 1.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFLVR-KISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHirqsPFLVTLHYAFQTETKLHL 129
Cdd:cd05090   9 FMEELGECAFGKIYKGHlYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHH----PNIVCLLGVVTQEQPVCM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQRERFTE----------------HEVQIYVG-EIVLALEHLHKLGIIYRDIKLENILLDSNGHVV 192
Cdd:cd05090  85 LFEFMNQGDLHEFLIMRSPHSDvgcssdedgtvkssldHGDFLHIAiQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 193 LTDFGLSKEFVADETERAYS-FCGTIEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLT-GASPFTvdGEKNSQA-EI-- 267
Cdd:cd05090 165 ISDLGLSREIYSSDYYRVQNkSLLPIRWMPPEAIMYGKFSSDS--DIWSFGVVLWEIFSfGLQPYY--GFSNQEViEMvr 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 32528297 268 SRRILKSEPPYPQEMSALAKDLIQRLLMKDPK 299
Cdd:cd05090 241 KRQLLPCSEDCPPRMYSLMTECWQEIPSRRPR 272
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
99-318 1.83e-10

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 61.66  E-value: 1.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  99 RTERQVLEHIrQSPFLVTLHYAFQTETK----LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLG-- 172
Cdd:cd14031  57 KEEAEMLKGL-QHPNIVRFYDSWESVLKgkkcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTpp 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 173 IIYRDIKLENILLDS-NGHVVLTDFGLSKEFvadETERAYSFCGTIEYMAPDIVrggDSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14031 136 IIHRDLKCDNIFITGpTGSVKIGDLGLATLM---RTSFAKSVIGTPEFMAPEMY---EEHYDESVDVYAFGMCMLEMATS 209
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 252 ASPFTvdgEKNSQAEISRRILKSEPP--YPQEMSALAKDLIQRLLMKDPKKRLGCgpRDadeIKEHLFF 318
Cdd:cd14031 210 EYPYS---ECQNAAQIYRKVTSGIKPasFNKVTDPEVKEIIEGCIRQNKSERLSI--KD---LLNHAFF 270
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
47-301 1.88e-10

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 62.01  E-value: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVrkiSGHDTGKLyAMKVLKKATIvqkakTTEHTRTERQVLEHIRQSPfLVTLhYAFQTETK 126
Cdd:cd05071   9 ESLRLEVKLGQGCFGEVWMG---TWNGTTRV-AIKTLKPGTM-----SPEAFLQEAQVMKKLRHEK-LVQL-YAVVSEEP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQI--YVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd05071  78 IYIVTEYMSKGSLLDFLKGEMGKYLRLPQLvdMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIED 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPF--TVDGEKNSQAEISRRIlksepPYPQE 281
Cdd:cd05071 158 NEYTARQGAKFPIKWTAPEAALYGR--FTIKSDVWSFGILLTELTTkGRVPYpgMVNREVLDQVERGYRM-----PCPPE 230
                       250       260
                ....*....|....*....|
gi 32528297 282 MSALAKDLIQRLLMKDPKKR 301
Cdd:cd05071 231 CPESLHDLMCQCWRKEPEER 250
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
46-255 1.88e-10

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 61.54  E-value: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVFLvrkisGHDTGKLYAMKVLKKATivqkakTTEHTRTERQVLEHIRQSPFLVTLHYAFQTET 125
Cdd:cd05082   5 MKELKLLQTIGKGEFGDVML-----GDYRGNKVAVKCIKNDA------TAQAFLAEASVMTQLRHSNLVQLLGVIVEEKG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQRERftehevQIYVGEIVL--------ALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd05082  74 GLYIVTEYMAKGSLVDYLRSRGR------SVLGGDCLLkfsldvceAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 198 LSKEfvADETERAYSFcgTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05082 148 LTKE--ASSTQDTGKL--PVKWTAPEALR--EKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
47-301 2.00e-10

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 61.63  E-value: 2.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVrkiSGHDTGKLyAMKVLKKATIVQKAkttehTRTERQVLEHIRQSPfLVTLhYAFQTETK 126
Cdd:cd05069  12 ESLRLDVKLGQGCFGEVWMG---TWNGTTKV-AIKTLKPGTMMPEA-----FLQEAQIMKKLRHDK-LVPL-YAVVSEEP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRE--RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVA 204
Cdd:cd05069  81 IYIVTEFMGKGSLLDFLKEGDgkYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPF--TVDGEKNSQAEISRRIlksepPYPQE 281
Cdd:cd05069 161 NEYTARQGAKFPIKWTAPEAALYGR--FTIKSDVWSFGILLTELVTkGRVPYpgMVNREVLEQVERGYRM-----PCPQG 233
                       250       260
                ....*....|....*....|
gi 32528297 282 MSALAKDLIQRLLMKDPKKR 301
Cdd:cd05069 234 CPESLHELMKLCWKKDPDER 253
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
432-546 2.03e-10

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 62.32  E-value: 2.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN------TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd05616   8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQdddvecTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05616  88 LMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLK 128
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
430-545 2.05e-10

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 61.40  E-value: 2.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKC-VHKKSNQAF--AVKIISKRMEANTQKEItaLKLCE-----GHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd00192   1 KKLGEGAFGEVYKGkLKGGDGKTVdvAVKTLKEDASESERKDF--LKEARvmkklGHPNVVRLLGVCTEEEPLYLVMEYM 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 502 NGGELFERIKKKKH-FSETEASYI-MRKLVS-------AVSHMHDVGVVHRDL 545
Cdd:cd00192  79 EGGDLLDFLRKSRPvFPSPEPSTLsLKDLLSfaiqiakGMEYLASKKFVHRDL 131
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
428-547 2.10e-10

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 61.60  E-value: 2.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIIS-KRMEANTQKEITALKlCE-------GHPNIVKLHEVFHDQLHTFLVME 499
Cdd:cd06625   4 QGKLLGQGAFGQVYLCYDADTGRELAVKQVEiDPINTEASKEVKALE-CEiqllknlQHERIVQYYGCLQDEKSLSIFME 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd06625  83 YMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKG 130
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
430-548 2.39e-10

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 62.41  E-value: 2.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRM------EANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05593  21 KLLGKGTFGKVILVREKASGKYYAMKILKKEViiakdeVAHTLTESRVLKNTR-HPFLTSLKYSFQTKDRLCFVMEYVNG 99
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05593 100 GELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLE 144
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
432-547 2.46e-10

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 62.19  E-value: 2.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII----SKRMEAN-TQKEITALKLCEGHPNIVKLHEVFH--DQLHTFLVMELLNG- 503
Cdd:cd07852  15 LGKGAYGIVWKAIDKKTGEVVALKKIfdafRNATDAQrTFREIMFLQELNDHPNIIKLLNVIRaeNDKDIYLVFEYMETd 94
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 504 ------GELFERIKKKkhfseteasYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07852  95 lhavirANILEDIHKQ---------YIMYQLLKALKYLHSGGVIHRDLKP 135
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
55-197 2.54e-10

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 58.61  E-value: 2.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVrkiSGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTlhyAFQTETKLHLILDYI 134
Cdd:cd13968   1 MGEGASAKVFWA---EGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKGLELNIPKVLV---TEDVDGPNILLMELV 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 135 NGGELFTHLSQRERFtEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG 197
Cdd:cd13968  75 KGGTLIAYTQEEELD-EKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
51-264 2.55e-10

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 60.92  E-value: 2.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFLVRKISGHDTgklyAMKVLKKATIVQkakttEHTRTERQVLEHIrQSPFLVTLhYAFQTETK-LHL 129
Cdd:cd05059   8 FLKELGSGQFGVVHLGKWRGKIDV----AIKMIKEGSMSE-----DDFIEEAKVMMKL-SHPKLVQL-YGVCTKQRpIFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQRERFTEHEVQIYV-GEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKeFVADEtE 208
Cdd:cd05059  77 VTEYMANGCLLNYLRERRGKFQTEQLLEMcKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLAR-YVLDD-E 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 209 RAYSFcGT---IEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPFtvDGEKNSQ 264
Cdd:cd05059 155 YTSSV-GTkfpVKWSPPEVFM--YSKFSSKSDVWSFGVLMWEVFSeGKMPY--ERFSNSE 209
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
49-251 2.64e-10

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 62.03  E-value: 2.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVlkkatIVQKAKTTEHTRTERQVLEHIRQSP---FLVTLHYAFQTET 125
Cdd:cd14225  45 YEILEVIGKGSFGQVV---KALDHKTNEHVAIKI-----IRNKKRFHHQALVEVKILDALRRKDrdnSHNVIHMKEYFYF 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDY----INGGELFTHlSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH--VVLTDFGLS 199
Cdd:cd14225 117 RNHLCITFellgMNLYELIKK-NNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGSS 195
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 200 kefvADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14225 196 ----CYEHQRVYTYIQSRFYRSPEVILG--LPYSMAIDMWSLGCILAELYTG 241
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
428-546 2.74e-10

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 61.18  E-value: 2.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIIS-KRMEANTQ-----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd14188   5 RGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPhSRVSKPHQrekidKEIELHRILH-HKHVVQFYHYFEDKENIYILLEYC 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 502 NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd14188  84 SRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLK 128
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
53-310 3.01e-10

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 61.14  E-value: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFlvRKIsghdtgklyaMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFL--------VTLHYAFQTE 124
Cdd:cd05063  11 KVIGAGEFGEVF--RGI----------LKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMgqfshhniIRLEGVVTKF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKeFV 203
Cdd:cd05063  79 KPAMIITEYMENGALDKYLRDHDgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSR-VL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 204 ADETERAYSFCG---TIEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLT-GASPFTvdgeKNSQAEISRRILKS-EPPY 278
Cdd:cd05063 158 EDDPEGTYTTSGgkiPIRWTAPEAI--AYRKFTSASDVWSFGIVMWEVMSfGERPYW----DMSNHEVMKAINDGfRLPA 231
                       250       260       270
                ....*....|....*....|....*....|..
gi 32528297 279 PQEMSALAKDLIQRLLMKDPKKRlgcgPRDAD 310
Cdd:cd05063 232 PMDCPSAVYQLMLQCWQQDRARR----PRFVD 259
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
71-251 3.03e-10

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 61.39  E-value: 3.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  71 GHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQV---LEHIRQSPFLvtlhyAFQTETKLH-LILDYINGGELFTHLSQR 146
Cdd:cd14157  12 GYRHGKQYVIKRLKETECESPKSTERFFQTEVQIcfrCCHPNILPLL-----GFCVESDCHcLIYPYMPNGSLQDRLQQQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 147 ERFT----EHEVQIYVGeIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIE---- 218
Cdd:cd14157  87 GGSHplpwEQRLSISLG-LLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGLRLCPVDKKSVYTMMKTKVLQisla 165
                       170       180       190
                ....*....|....*....|....*....|...
gi 32528297 219 YMAPDIVRGGDSghDKAVDWWSLGVLMYELLTG 251
Cdd:cd14157 166 YLPEDFVRHGQL--TEKVDIFSCGVVLAEILTG 196
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
51-271 3.18e-10

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 61.03  E-value: 3.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFLvrkisghdtGKLYA-MKVLKKAtIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHL 129
Cdd:cd05114   8 FMKELGSGLFGVVRL---------GKWRAqYKVAIKA-IREGAMSEEDFIEEAKVMMKLTH-PKLVQLYGVCTQQKPIYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 130 ILDYINGGELFTHLSQRERFTEHEVQIYV-GEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETE 208
Cdd:cd05114  77 VTEFMENGCLLNYLRQRRGKLSRDMLLSMcQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYT 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 209 RAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLT-GASPFtvdgEKNSQAEISRRI 271
Cdd:cd05114 157 SSSGAKFPVKWSPPEVFNY--SKFSSKSDVWSFGVLMWEVFTeGKMPF----ESKSNYEVVEMV 214
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
429-547 3.30e-10

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 60.81  E-value: 3.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSFSICRKCVHKKSNQAFAVKIIS--KRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd08228   7 EKKIGRGQFSEVYRATCLLDRKPVALKKVQifEMMDAKARqdcvKEIDLLKQLN-HPNVIKYLDSFIEDNELNIVLELAD 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 503 GGELFERI----KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd08228  86 AGDLSQMIkyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKP 134
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
47-301 3.37e-10

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 61.09  E-value: 3.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIvqkakttehtrTERQVLEHIRQSPFLVTLHY------- 119
Cdd:cd05074   9 QQFTLGRMLGKGEFGSVREAQLKSEDGSFQKVAVKMLKADIF-----------SSSDIEEFLREAACMKEFDHpnvikli 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 --AFQTETKLHL-----ILDYINGGELFTHLSQrERFTEHEVQI-------YVGEIVLALEHLHKLGIIYRDIKLENILL 185
Cdd:cd05074  78 gvSLRSRAKGRLpipmvILPFMKHGDLHTFLLM-SRIGEEPFTLplqtlvrFMIDIASGMEYLSSKNFIHRDLAARNCML 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 186 DSNGHVVLTDFGLSKEFVADETERaySFCGT---IEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLT-GASPFTvdGEK 261
Cdd:cd05074 157 NENMTVCVADFGLSKKIYSGDYYR--QGCASklpVKWLALESL--ADNVYTTHSDVWAFGVTMWEIMTrGQTPYA--GVE 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 32528297 262 NSQAE---ISRRILKSEPPYPQEMSalakDLIQRLLMKDPKKR 301
Cdd:cd05074 231 NSEIYnylIKGNRLKQPPDCLEDVY----ELMCQCWSPEPKCR 269
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
55-249 3.88e-10

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 60.57  E-value: 3.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLVRKisgHDTGKLYAMKVLKKATivQKAKTTEhtrtERQVLEHIRQSPFLVTLHYAFQtETKLHLILDYI 134
Cdd:cd14155   1 IGSGFFSEVYKVRH---RTSGQVMALKMNTLSS--NRANMLR----EVQLMNRLSHPNILRFMGVCVH-QGQLHALTEYI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELfTHLSQRERFTEHEVQIYVG-EIVLALEHLHKLGIIYRDIKLENILL--DSNGH-VVLTDFGLSKEF--VADETE 208
Cdd:cd14155  71 NGGNL-EQLLDSNEPLSWTVRVKLAlDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYtAVVGDFGLAEKIpdYSDGKE 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 32528297 209 RaYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELL 249
Cdd:cd14155 150 K-LAVVGSPYWMAPEVLRG--EPYNEKADVFSYGIILCEII 187
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
55-271 4.72e-10

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 60.35  E-value: 4.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  55 LGTGAYGKVFLvrkisGHDTGKlyaMKVLKKaTIVQKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETKLHLILDYI 134
Cdd:cd05112  12 IGSGQFGLVHL-----GYWLNK---DKVAIK-TIREGAMSEEDFIEEAEVMMKLSH-PKLVQLYGVCLEQAPICLVFEFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 135 NGGELFTHL-SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKeFVADetERAYSF 213
Cdd:cd05112  82 EHGCLSDYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTR-FVLD--DQYTSS 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 214 CGT---IEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFtvdgEKNSQAEISRRI 271
Cdd:cd05112 159 TGTkfpVKWSSPEVFSFSR--YSSKSDVWSFGVLMWEVFSeGKIPY----ENRSNSEVVEDI 214
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
430-548 4.96e-10

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 61.43  E-value: 4.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKI------ISKRMEANTQKEITALKLCEGhPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05610  10 KPISRGAFGKVYLGRKKNNSKLYAVKVvkkadmINKNMVHQVQAERDALALSKS-PFIVHLYYSLQSANNVYLVMEYLIG 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05610  89 GDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPD 133
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
51-248 6.41e-10

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 60.53  E-value: 6.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFlvrkiSGHDTGKLYAMKVLKKATIVQKAKTTEHTRTerQVLEHIRQSPFLVTLHYAFQTETKLHLI 130
Cdd:cd14142   9 LVECIGKGRYGEVW-----RGQWQGESVAVKIFSSRDEKSWFRETEIYNT--VLLRHENILGFIASDMTSRNSCTQLWLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLsQRERFTEHEVQIYVGEIVLALEHLH--------KLGIIYRDIKLENILLDSNGHVVLTDFGL---- 198
Cdd:cd14142  82 THYHENGSLYDYL-QRTTLDHQEMLRLALSAASGLVHLHteifgtqgKPAIAHRDLKSKNILVKSNGQCCIADLGLavth 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 199 ---SKEFVADETERAysfcGTIEYMAPDI------VRGGDSGhdKAVDWWSLGVLMYEL 248
Cdd:cd14142 161 sqeTNQLDVGNNPRV----GTKRYMAPEVldetinTDCFESY--KRVDIYAFGLVLWEV 213
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
52-334 6.41e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 60.89  E-value: 6.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVflvrkISGHDTgklyamkVLKKATIVQK-----AKTTEHTRTERQ-VLEHIRQSPFLVTLHYAFQTET 125
Cdd:cd07850   5 LKPIGSGAQGIV-----CAAYDT-------VTGQNVAIKKlsrpfQNVTHAKRAYRElVLMKLVNHKNIIGLLNVFTPQK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTH-LSQR-ERFTEHEVQIY-VGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKef 202
Cdd:cd07850  73 SLEEFQDVYLVMELMDAnLCQViQMDLDHERMSYlLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 203 VADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPF-----------------TVDGEKNSQA 265
Cdd:cd07850 151 TAGTSFMMTPYVVTRYYRAPEVILG--MGYKENVDIWSVGCIMGEMIRGTVLFpgtdhidqwnkiieqlgTPSDEFMSRL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 266 EISRR-ILKSEPPY---------PQEM------------SALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFfqkIN- 322
Cdd:cd07850 229 QPTVRnYVENRPKYagysfeelfPDVLfppdseehnklkASQARDLLSKMLVIDPEKRI-----SVDDALQHPY---INv 300
                       330
                ....*....|..
gi 32528297 323 WDDLAAKKVPAP 334
Cdd:cd07850 301 WYDPSEVEAPPP 312
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
430-546 6.55e-10

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 60.51  E-value: 6.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN------TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDdedidwVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05588  81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLK 123
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
420-546 7.16e-10

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 60.18  E-value: 7.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 420 YQHYDLdlkdkpLGEGSFSICRKCVHKKSNQAFAVKIISKRME----ANTQKEITAL-KLCEGHP-NIVKLHEVFHDQLH 493
Cdd:cd06917   3 YRRLEL------VGRGSYGAVYRGYHVKTGRVVALKVLNLDTDdddvSDIQKEVALLsQLKLGQPkNIIKYYGSYLKGPS 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 494 TFLVMELLNGGELFERIKKKKhFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06917  77 LWIIMDYCEGGSIRTLMRAGP-IAERYIAVIMREVLVALKFIHKDGIIHRDIK 128
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
129-250 7.20e-10

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 60.45  E-value: 7.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHLSQRErFTEHEVQIYVGEIVLALEHLH---------KLGIIYRDIKLENILLDSNGHVVLTDFGLS 199
Cdd:cd14054  71 LVLEYAPKGSLCSYLRENT-LDWMSSCRMALSLTRGLAYLHtdlrrgdqyKPAIAHRDLNSRNVLVKADGSCVICDFGLA 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 200 ---------KEFVADETERAYSFCGTIEYMAPDIVRGGDSGHD-----KAVDWWSLGVLMYELLT 250
Cdd:cd14054 150 mvlrgsslvRGRPGAAENASISEVGTLRYMAPEVLEGAVNLRDcesalKQVDVYALGLVLWEIAM 214
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
426-547 7.26e-10

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 59.54  E-value: 7.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKDKpLGEGSFS-------ICRKCVHKKSNQAFAVKII-----SKRMEAntqkEITALKLCEGHPNIVKLHEVFHDQLH 493
Cdd:cd14019   4 RIIEK-IGEGTFSsvykaedKLHDLYDRNKGRLVALKHIyptssPSRILN----ELECLERLGGSNNVSGLITAFRNEDQ 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 494 TFLVMELlnggelFERIKKK---KHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14019  79 VVAVLPY------IEHDDFRdfyRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKP 129
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
432-548 8.37e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 59.85  E-value: 8.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR--------MEANTQKEITALKLCeghPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKrikkkkgeTMALNEKIILEKVSS---PFIVSLAYAFETKDKLCLVLTLMNG 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 504 GELFERIKK--KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05577  78 GDLKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPE 124
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
430-548 8.57e-10

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 60.63  E-value: 8.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRmEANTQKEITALK-----LCEGH-PNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05629   7 KVIGKGAFGEVRLVQKKDTGKIYAMKTLLKS-EMFKKDQLAHVKaerdvLAESDsPWVVSLYYSFQDAQYLYLIMEFLPG 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05629  86 GDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPD 130
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
478-547 8.59e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 59.64  E-value: 8.59e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 478 HPNIVKLHEVFHDQLHTFL-VMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHM--HDVGVVHRDLKP 547
Cdd:cd13990  63 HPRIVKLYDVFEIDTDSFCtVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKP 135
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
58-250 8.84e-10

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 60.03  E-value: 8.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  58 GAYGKVFLVRKisghdTGKLYAMKVLKkatIVQKAK-TTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYING 136
Cdd:cd14053   6 GRFGAVWKAQY-----LNRLVAVKIFP---LQEKQSwLTEREIYSLPGMKHENILQFIGAEKHGESLEAEYWLITEFHER 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 137 GELFTHLSQRERFTEHEVQIYVGeIVLALEHLH----------KLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD- 205
Cdd:cd14053  78 GSLCDYLKGNVISWNELCKIAES-MARGLAYLHedipatngghKPSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGk 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 206 ETERAYSFCGTIEYMAPDIVRGG-----DSGhdKAVDWWSLGVLMYELLT 250
Cdd:cd14053 157 SCGDTHGQVGTRRYMAPEVLEGAinftrDAF--LRIDMYAMGLVLWELLS 204
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
430-547 9.10e-10

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 59.86  E-value: 9.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQL--HTFLVMELLNGGELF 507
Cdd:cd14132  24 RKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKIKREIKILQNLRGGPNIVKLLDVVKDPQskTPSLIFEYVNNTDFK 103
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 508 ERIKKkkhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14132 104 TLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKP 140
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
432-548 9.29e-10

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 59.83  E-value: 9.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVK-IISKRMEANTQ--KEITALKLCEGHPNIVKL--------HEVFHDQLHTFLVMEL 500
Cdd:cd14036   8 IAEGGFAFVYEAQDVGTGKEYALKrLLSNEEEKNKAiiQEINFMKKLSGHPNIVQFcsaasigkEESDQGQAEYLLLTEL 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 501 LNGG--ELFERIKKKKHFSETEASYIMRKLVSAVSHMH--DVGVVHRDLKPE 548
Cdd:cd14036  88 CKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHkqSPPIIHRDLKIE 139
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
432-546 9.73e-10

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 59.66  E-value: 9.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK---EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd06643  13 LGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDymvEIDILASCD-HPNIVKLLDAFYYENNLWILIEFCAGGAVDA 91
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 509 -RIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06643  92 vMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLK 130
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
427-548 1.03e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 59.74  E-value: 1.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQ-------KEITALKLCEgHPNIVKLHEVFHDQLHTFLVME 499
Cdd:cd07861   3 TKIEKIGEGTYGVVYKGRNKKTGQIVAMKKI--RLESEEEgvpstaiREISLLKELQ-HPNIVCLEDVLMQENRLYLVFE 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 500 LLNGG--ELFERIKKKKHF-SETEASYiMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07861  80 FLSMDlkKYLDSLPKGKYMdAELVKSY-LYQILQGILFCHSRRVLHRDLKPQ 130
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
432-546 1.10e-09

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 59.64  E-value: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKI--ISKRMEANTQKEITALKLCEGHPNIVKLHEVF--------HDQLhtFLVMELL 501
Cdd:cd06636  24 VGNGTYGQVYKGRHVKTGQLAAIKVmdVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFikksppghDDQL--WLVMEFC 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 NGGELFERIKKKK--HFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06636 102 GAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIK 148
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
47-302 1.31e-09

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 59.28  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVF--LVRKISGHDTGKLYAMKvlkkaTIVQKAKTTEHTR--TERQVLEHIrQSPFLVTLHYAFQ 122
Cdd:cd05032   6 EKITLIRELGQGSFGMVYegLAKGVVKGEPETRVAIK-----TVNENASMRERIEflNEASVMKEF-NCHHVVRLLGVVS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGGELFTHL-SQRERFTEHEVQI---------YVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVV 192
Cdd:cd05032  80 TGQPTLVVMELMAKGDLKSYLrSRRPEAENNPGLGpptlqkfiqMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 193 LTDFGLSKefvaDETERAYSFCGT-----IEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPFTvdGEKNSQAE 266
Cdd:cd05032 160 IGDFGMTR----DIYETDYYRKGGkgllpVRWMAPESLK--DGVFTTKSDVWSFGVVLWEMATlAEQPYQ--GLSNEEVL 231
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 32528297 267 ---ISRRILksepPYPQEMSALAKDLIQRLLMKDPKKRL 302
Cdd:cd05032 232 kfvIDGGHL----DLPENCPDKLLELMRMCWQYNPKMRP 266
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
432-547 1.37e-09

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 59.23  E-value: 1.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII---SKRMEANTQKEITALKLCeGHPNIVKL--HEVFH--DQLHT-FLVMELLNG 503
Cdd:cd13986   8 LGEGGFSFVYLVEDLSTGRLYALKKIlchSKEDVKEAMREIENYRLF-NHPNILRLldSQIVKeaGGKKEvYLLLPYYKR 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 504 GEL---FERIKKKK-HFSETEASYIMRKLVSAVSHMHD---VGVVHRDLKP 547
Cdd:cd13986  87 GSLqdeIERRLVKGtFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKP 137
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
432-548 1.41e-09

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 58.72  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKR------MEANTQKEITALKLCEgHPNIVKLHEVFH-DQLHTFLVMELLnGG 504
Cdd:cd14164   8 IGEGSFSKVKLATSQKYCCKVAIKIVDRRraspdfVQKFLPRELSILRRVN-HPNIVQMFECIEvANGRLYIVMEAA-AT 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14164  86 DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCE 129
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
51-255 1.42e-09

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 59.64  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFLVRKIsGHDTGKlyAMKVLKKATIVQKAKTTEHTRT----ERQVLEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd05098  17 LGKPLGEGCFGQVVLAEAI-GLDKDK--PNRVTKVAVKMLKSDATEKDLSdlisEMEMMKMIGKHKNIINLLGACTQDGP 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQR----------------ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH 190
Cdd:cd05098  94 LYVIVEYASKGNLREYLQARrppgmeycynpshnpeEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNV 173
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 191 VVLTDFGLSKEF-VADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05098 174 MKIADFGLARDIhHIDYYKKTTNGRLPVKWMAPEALF--DRIYTHQSDVWSFGVLLWEIFTlGGSPY 238
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
423-547 1.44e-09

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 59.69  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 423 YDLDLKDKPL---GEGSFSICRKCVHKKSNQAFAVKIISKRMEA-----NTQKEITALKLCEgHPNIVKLHEVFH----- 489
Cdd:cd07855   1 FDVGDRYEPIetiGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVvttakRTLRELKILRHFK-HDNIIAIRDILRpkvpy 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 490 -DQLHTFLVMELLNGgELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07855  80 aDFKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKP 137
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
432-546 1.44e-09

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 59.63  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN------TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd05615  18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQdddvecTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGGD 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05615  98 LMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLK 138
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
47-255 1.51e-09

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 58.74  E-value: 1.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLvrkiSGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERqvLEHIRqspfLVTLHyAFQTETK 126
Cdd:cd05067   7 ETLKLVERLGAGQFGEVWM----GYYNGHTKVAIKSLKQGSMSPDAFLAEANLMKQ--LQHQR----LVRLY-AVVTQEP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRE--RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK---- 200
Cdd:cd05067  76 IYIITEYMENGSLVDFLKTPSgiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARlied 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 201 -EFVADETERAysfcgTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05067 156 nEYTAREGAKF-----PIKWTAPEAINYGT--FTIKSDVWSFGILLTEIVThGRIPY 205
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
79-301 1.51e-09

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 58.90  E-value: 1.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  79 AMKVLKKATIVQKAKttEHTRtERQV---LEHirqsPFLVTLHYAFQTETkLHLILDYINGGELFTHLSQRERFTEHEVQ 155
Cdd:cd05060  27 AVKTLKQEHEKAGKK--EFLR-EASVmaqLDH----PCIVRLIGVCKGEP-LMLVMELAPLGPLLKYLKKRREIPVSDLK 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 156 IYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGT--IEYMAPDIVRGGDSGHd 233
Cdd:cd05060  99 ELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRATTAGRwpLKWYAPECINYGKFSS- 177
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 234 kAVDWWSLGVLMYELLT-GASPFtvdGEKnSQAEISRRILKSEP-PYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd05060 178 -KSDVWSYGVTLWEAFSyGAKPY---GEM-KGPEVIAMLESGERlPRPEECPQEIYSIMLSCWKYRPEDR 242
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
47-255 1.60e-09

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 59.26  E-value: 1.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsGHDTGK-----LYAMKVLKKATivqKAKTTEHTRTERQVLEHIRQSPFLVTLHYAF 121
Cdd:cd05101  24 DKLTLGKPLGEGCFGQVVMAEAV-GIDKDKpkeavTVAVKMLKDDA---TEKDLSDLVSEMEMMKMIGKHKNIINLLGAC 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHLILDYINGGELFTHLSQR----------------ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL 185
Cdd:cd05101 100 TQDGPLYVIVEYASKGNLREYLRARrppgmeysydinrvpeEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLV 179
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 186 DSNGHVVLTDFGLSKEF-VADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05101 180 TENNVMKIADFGLARDInNIDYYKKTTNGRLPVKWMAPEALF--DRVYTHQSDVWSFGVLMWEIFTlGGSPY 249
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
428-546 1.62e-09

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 58.57  E-value: 1.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIIS------KRMEANTQ--KEITAL-KLCegHPNIVKLH--EVFHDQLHTFL 496
Cdd:cd06632   4 KGQLLGSGSFGSVYEGFNGDTGDFFAVKEVSlvdddkKSRESVKQleQEIALLsKLR--HPNIVQYYgtEREEDNLYIFL 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 497 vmELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06632  82 --EYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIK 129
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
432-548 1.65e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 59.38  E-value: 1.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK--EITALKLCEGHP----NIVKLHEVFHDQLHTFLVMELLNgGE 505
Cdd:cd14211   7 LGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGqiEVSILSRLSQENadefNFVRAYECFQHKNHTCLVFEMLE-QN 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 506 LFERIKKKKhFSETEASYI---MRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14211  86 LYDFLKQNK-FSPLPLKYIrpiLQQVLTALLKLKSLGLIHADLKPE 130
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
49-251 1.85e-09

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 59.19  E-value: 1.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKativQKAKTTEhTRTERQVLEhirqspflvTLHYAFQTETKLH 128
Cdd:cd14212   1 YLVLDLLGQGTFGQVV---KCQDLKTNKLVAVKVLKN----KPAYFRQ-AMLEIAILT---------LLNTKYDPEDKHH 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LI--LDYinggelFTH-----------------LSQRERFTEHEVQI---YVGEIVLALEHLHKLGIIYRDIKLENILLD 186
Cdd:cd14212  64 IVrlLDH------FMHhghlcivfellgvnlyeLLKQNQFRGLSLQLirkFLQQLLDALSVLKDARIIHCDLKPENILLV 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 187 SN--GHVVLTDFGLSkefvADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14212 138 NLdsPEIKLIDFGSA----CFENYTLYTYIQSRFYRSPEVLLG--LPYSTAIDMWSLGCIAAELFLG 198
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
430-548 1.88e-09

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 59.63  E-value: 1.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEAN---TQKEITALKlceGHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd05621  58 KVIGRGAFGEVQLVRHKASQKVYAMKLLSKfemikRSDSAffwEERDIMAFA---NSPWVVQLFCAFQDDKYLYMVMEYM 134
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 NGGELFErIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05621 135 PGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPD 180
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
47-301 1.91e-09

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 58.79  E-value: 1.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVlGTGAYGKVFlvRKISGHDtGKLYAMKVLKKATivqkAKTTEHTRTERQVLEH--IRQSPFLVTLHYAFQTE 124
Cdd:cd14139   1 EFLELEKI-GVGEFGSVY--KCIKRLD-GCVYAIKRSMRPF----AGSSNEQLALHEVYAHavLGHHPHVVRYYSAWAED 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TklHLIL--DYINGGELFTHLSQR----ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLdsnGHVVLTDFGL 198
Cdd:cd14139  73 D--HMIIqnEYCNGGSLQDAISENtksgNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFI---CHKMQSSSGV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 199 SKEfvaDETERAYSFCGTIEYMAPDI----------VRGGDS------------GHDKAVDWWSLGvLMYELLTGASPFT 256
Cdd:cd14139 148 GEE---VSNEEDEFLSANVVYKIGDLghvtsinkpqVEEGDSrflaneilqedyRHLPKADIFALG-LTVALAAGAEPLP 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 257 VDGEknsqaeISRRILKSE-PPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14139 224 TNGA------AWHHIRKGNfPDVPQELPESFSSLLKNMIQPDPEQR 263
PTZ00284 PTZ00284
protein kinase; Provisional
44-251 1.98e-09

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 59.98  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   44 VGIENFELLKVLGTGAYGKVflvrkISGHDTG-KLY-AMKVLKKAtivqkAKTTEHTRTERQVLEHIRQS------PFLV 115
Cdd:PTZ00284 126 VSTQRFKILSLLGEGTFGKV-----VEAWDRKrKEYcAVKIVRNV-----PKYTRDAKIEIQFMEKVRQAdpadrfPLMK 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  116 TLHYaFQTETKlHL----------ILDYINGGELFTHlsqrerftEHEVQIyVGEIVLALEHLH-KLGIIYRDIKLENIL 184
Cdd:PTZ00284 196 IQRY-FQNETG-HMcivmpkygpcLLDWIMKHGPFSH--------RHLAQI-IFQTGVALDYFHtELHLMHTDLKPENIL 264
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297  185 LDSNGHVV--LTDFGLSKE----------FVADETERAYSFCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTG 251
Cdd:PTZ00284 265 METSDTVVdpVTNRALPPDpcrvricdlgGCCDERHSRTAIVSTRHYRSPEVVLG--LGWMYSTDMWSMGCIIYELYTG 341
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
160-251 2.08e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 59.13  E-value: 2.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 160 EIVLALEHLH-KLGIIYRDIKLENILLD-SNGHVVLTDFG----LSKEFVADETERaysfcgtiEYMAPDIVRGgdSGHD 233
Cdd:cd14136 127 QVLQGLDYLHtKCGIIHTDIKPENVLLCiSKIEVKIADLGnacwTDKHFTEDIQTR--------QYRSPEVILG--AGYG 196
                        90
                ....*....|....*...
gi 32528297 234 KAVDWWSLGVLMYELLTG 251
Cdd:cd14136 197 TPADIWSTACMAFELATG 214
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
430-547 2.27e-09

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 59.23  E-value: 2.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSF-SICrKCVHKKSNQAFAVKIISKRMEAN-----TQKEITALKLCEgHPNIVKLHEVFH--DQLHTF----LV 497
Cdd:cd07851  21 SPVGSGAYgQVC-SAFDTKTGRKVAIKKLSRPFQSAihakrTYRELRLLKHMK-HENVIGLLDVFTpaSSLEDFqdvyLV 98
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 498 MELLnGGELfERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07851  99 THLM-GADL-NNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKP 146
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
47-248 2.28e-09

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 58.91  E-value: 2.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLvrkisGHDTGKLYAMKVLKKATIVQKAKTTEHTRTerQVLEHIRQSPFLVTLHYAFQTETK 126
Cdd:cd14219   5 KQIQMVKQIGKGRYGEVWM-----GKWRGEKVAVKVFFTTEEASWFRETEIYQT--VLMRHENILGFIAADIKGTGSWTQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEiVLALEHLH--------KLGIIYRDIKLENILLDSNGHVVLTDFGL 198
Cdd:cd14219  78 LYLITDYHENGSLYDYLKSTTLDTKAMLKLAYSS-VSGLCHLHteifstqgKPAIAHRDLKSKNILVKKNGTCCIADLGL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 199 SKEFVADETE---RAYSFCGTIEYMAPDIV-RGGDSGHDKA---VDWWSLGVLMYEL 248
Cdd:cd14219 157 AVKFISDTNEvdiPPNTRVGTKRYMPPEVLdESLNRNHFQSyimADMYSFGLILWEV 213
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
430-548 2.30e-09

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 58.90  E-value: 2.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd05597   7 KVIGRGAFGEVAVVKLKSTEKVYAMKILNKwemlkRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDYYCGG 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 505 ELFERIKK-KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05597  87 DLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPD 131
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
429-548 2.35e-09

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 58.45  E-value: 2.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSFSIcrkcVHKKSNQAFAVKIISKRMEAN-------TQKEITALKLCEGHPNIVKL------------HEVfh 489
Cdd:cd14037   8 EKYLAEGGFAH----VYLVKTSNGGNRAALKRVYVNdehdlnvCKREIEIMKRLSGHKNIVGYidssanrsgngvYEV-- 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 490 dqlhtFLVMELLNGGELFERIKKKKH--FSETEASYIMRKLVSAVSHMH--DVGVVHRDLKPE 548
Cdd:cd14037  82 -----LLLMEYCKGGGVIDLMNQRLQtgLTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVE 139
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
426-548 2.99e-09

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 57.91  E-value: 2.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKDKPLGEGSFSICRKCVHKKSNQAFAVKI--ISKRMEANTQKEITAlklceGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14109   6 EIGEEDEKRAAQGAPFHVTERSTGRNFLAQLryGDPFLMREVDIHNSL-----DHPNIVQMHDAYDDEKLAVTVIDNLAS 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 504 GELFERI---KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14109  81 TIELVRDnllPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPE 128
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
46-255 3.00e-09

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 58.16  E-value: 3.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  46 IENFELLKVLGTGAYGKVF---LVRKiSGHDTGKLYAMKVLKKATIVqkaKTTEHTRTERQVLEHIRQsPFLVTLHYAFQ 122
Cdd:cd05048   4 LSAVRFLEELGEGAFGKVYkgeLLGP-SSEESAISVAIKTLKENASP---KTQQDFRREAELMSDLQH-PNIVCLLGVCT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGI----------------IYRDIKLENILLD 186
Cdd:cd05048  79 KEQPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLDQSDFLHIaiqiaagmeylsshhyVHRDLAARNCLVG 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 187 SNGHVVLTDFGLSKEFVADETERAYSFCG-TIEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLT-GASPF 255
Cdd:cd05048 159 DGLTVKISDFGLSRDIYSSDYYRVQSKSLlPVRWMPPEAILYGKFTTES--DVWSFGVVLWEIFSyGLQPY 227
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
151-334 3.05e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 58.95  E-value: 3.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 151 EHEVQIYV-GEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERAYSFCGTIEYMAPDIVRGgd 229
Cdd:cd07874 117 DHERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR--TAGTSFMMTPYVVTRYYRAPEVILG-- 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 230 SGHDKAVDWWSLGVLMYELLTGASPFT----VDGEKNSQAEIS--------------RRILKSEPPY---------PQEM 282
Cdd:cd07874 193 MGYKENVDIWSVGCIMGEMVRHKILFPgrdyIDQWNKVIEQLGtpcpefmkklqptvRNYVENRPKYagltfpklfPDSL 272
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 283 -----------SALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFfqkIN-WDDLAAKKVPAP 334
Cdd:cd07874 273 fpadsehnklkASQARDLLSKMLVIDPAKRI-----SVDEALQHPY---INvWYDPAEVEAPPP 328
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
47-255 3.10e-09

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 58.84  E-value: 3.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKV-----FLVRKISGHDTgklYAMKVLKKAtivqkAKTTEHT--RTERQVLEHIRQSPFLVTLHY 119
Cdd:cd05102   7 DRLRLGKVLGHGAFGKVveasaFGIDKSSSCET---VAVKMLKEG-----ATASEHKalMSELKILIHIGNHLNVVNLLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 A-FQTETKLHLILDYINGGELFTHL------------------------------SQRER--------FTEHEVQ----- 155
Cdd:cd05102  79 AcTKPNGPLMVIVEFCKYGNLSNFLrakregfspyrersprtrsqvrsmveavraDRRSRqgsdrvasFTESTSStnqpr 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 156 -----------------IYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD-ETERAYSFCGTI 217
Cdd:cd05102 159 qevddlwqspltmedliCYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDpDYVRKGSARLPL 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 32528297 218 EYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05102 239 KWMAPESIF--DKVYTTQSDVWSFGVLLWEIFSlGASPY 275
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
53-255 3.14e-09

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 57.81  E-value: 3.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVF--LVRKISGHDTGKL-YAMKVLKK-ATIVQKAKTTEhtrtERQVLEHIRQSPFLVTLHYAFQTETKlH 128
Cdd:cd05044   1 KFLGSGAFGEVFegTAKDILGDGSGETkVAVKTLRKgATDQEKAEFLK----EAHLMSNFKHPNILKLLGVCLDNDPQ-Y 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGGELFTHL--SQRERFT------EHEVQIYVgEIVLALEHLHKLGIIYRDIKLENILLDSNGH----VVLTDF 196
Cdd:cd05044  76 IILELMEGGDLLSYLraARPTAFTpplltlKDLLSICV-DVAKGCVYLEDMHFVHRDLAARNCLVSSKDYrervVKIGDF 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 197 GLSKE-----FVADETERAYSfcgtIEYMAPD-IVRGGDSGHDkavDWWSLGVLMYELLT-GASPF 255
Cdd:cd05044 155 GLARDiykndYYRKEGEGLLP----VRWMAPEsLVDGVFTTQS---DVWAFGVLMWEILTlGQQPY 213
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
430-546 3.16e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 57.82  E-value: 3.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEG-------HPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd08222   6 RKLGSGNFGTVYLVSDLKATADEELKVLKEISVGELQPDETVDANREAkllskldHPAIVKFHDSFVEKESFCIVTEYCE 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 503 GGELFERI----KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd08222  86 GGDLDDKIseykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLK 133
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
98-320 3.58e-09

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 58.14  E-value: 3.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  98 TRTERQVLEHIR------QSPFLVTLHYAFQTETK----LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEH 167
Cdd:cd14030  64 SKSERQRFKEEAgmlkglQHPNIVRFYDSWESTVKgkkcIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQF 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 168 LHKLG--IIYRDIKLENILLDS-NGHVVLTDFGLSkefVADETERAYSFCGTIEYMAPDIVrggDSGHDKAVDWWSLGVL 244
Cdd:cd14030 144 LHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLA---TLKRASFAKSVIGTPEFMAPEMY---EEKYDESVDVYAFGMC 217
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32528297 245 MYELLTGASPFTvdgEKNSQAEISRRILKSEPPYPQEMSAL--AKDLIQRLLMKDPKKRLGCgprdaDEIKEHLFFQK 320
Cdd:cd14030 218 MLEMATSEYPYS---ECQNAAQIYRRVTSGVKPASFDKVAIpeVKEIIEGCIRQNKDERYAI-----KDLLNHAFFQE 287
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
53-248 3.81e-09

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 58.13  E-value: 3.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLvrkisGHDTGKLYAMKVLKKATIVQKAKTTEHTRTerQVLEHIRQSPFLVTLHYAFQTETKLHLILD 132
Cdd:cd14220   1 RQIGKGRYGEVWM-----GKWRGEKVAVKVFFTTEEASWFRETEIYQT--VLMRHENILGFIAADIKGTGSWTQLYLITD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHLsqreRFTEHEVQIYVG---EIVLALEHLH--------KLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd14220  74 YHENGSLYDFL----KCTTLDTRALLKlaySAACGLCHLHteiygtqgKPAIAHRDLKSKNILIKKNGTCCIADLGLAVK 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 202 FVADETERAYSF---CGTIEYMAPDIVRGG-DSGHDKA---VDWWSLGVLMYEL 248
Cdd:cd14220 150 FNSDTNEVDVPLntrVGTKRYMAPEVLDESlNKNHFQAyimADIYSFGLIIWEM 203
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
432-547 3.91e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 58.15  E-value: 3.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIskRMEanTQKE---ITAL---KLCE--GHPNIVKLHEVFH--------DQLHTF 495
Cdd:cd07865  20 IGQGTFGEVFKARHRKTGQIVALKKV--LME--NEKEgfpITALreiKILQllKHENVVNLIEICRtkatpynrYKGSIY 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 496 LVMEL----LNGgeLFERIKKKkhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07865  96 LVFEFcehdLAG--LLSNKNVK--FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKA 147
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
424-546 4.23e-09

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 57.42  E-value: 4.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKDKpLGEGSFSICRKCVHKKSNQAFAVKII-----SKRMEANTQKEITAL-KLceGHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd08529   1 DFEILNK-LGKGSFGVVYKVVRKVDGRVYALKQIdisrmSRKMREEAIDEARVLsKL--NSPYVIKYYDSFVDKGKLNIV 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 498 MELLNGGELFERIKKKKHFSETEAS----YIMRKLvsAVSHMHDVGVVHRDLK 546
Cdd:cd08529  78 MEYAENGDLHSLIKSQRGRPLPEDQiwkfFIQTLL--GLSHLHSKKILHRDIK 128
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
432-548 4.35e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 57.70  E-value: 4.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEIT--ALKLCE--GHPNIVKLHEVFHDQLHTFLVMELL--NGGE 505
Cdd:cd07848   9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTlrELKMLRtlKQENIVELKEAFRRRGKLYLVFEYVekNMLE 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 506 LFERIKKKKhFSETEASYIMrKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07848  89 LLEEMPNGV-PPEKVRSYIY-QLIKAIHWCHKNDIVHRDIKPE 129
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
432-546 4.82e-09

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 57.79  E-value: 4.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN------TQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd05587   4 LGKGSFGKVMLAERKGTDELYAIKILKKDVIIQdddvecTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 506 LFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05587  84 LMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLK 124
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
53-302 5.37e-09

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 57.52  E-value: 5.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISghdTGKLYAMKVL------KKATIVQkakttehtrtERQVLEHIRQSPFLVTLHYAFQT--E 124
Cdd:cd14036   6 RVIAEGGFAFVYEAQDVG---TGKEYALKRLlsneeeKNKAIIQ----------EINFMKKLSGHPNIVQFCSAASIgkE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGEL--------FTHLSQRERFTEHEVQIYVGEIVLALEHLHK--LGIIYRDIKLENILLDSNGHVVLT 194
Cdd:cd14036  73 ESDQGQAEYLLLTELckgqlvdfVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKqsPPIIHRDLKIENLLIGNQGQIKLC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 195 DFG---------------LSKEFVADETERAysfcGTIEYMAPDIVRG-GDSGHDKAVDWWSLGVLMYELLTGASPFTvD 258
Cdd:cd14036 153 DFGsatteahypdyswsaQKRSLVEDEITRN----TTPMYRTPEMIDLySNYPIGEKQDIWALGCILYLLCFRKHPFE-D 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 259 GEKnsqaeisRRILKSE---PPYPQEMSALaKDLIQRLLMKDPKKRL 302
Cdd:cd14036 228 GAK-------LRIINAKytiPPNDTQYTVF-HDLIRSTLKVNPEERL 266
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
52-255 5.44e-09

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 57.31  E-value: 5.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKISGHDTGKLyAMKVLKKATIVQKAKtteHTRTERQVLEHIRQSPFLVTLHYAFQTETKLhLIL 131
Cdd:cd05087   2 LKEIGHGWFGKVFLGEVNSGLSSTQV-VVKELKASASVQDQM---QFLEEAQPYRALQHTNLLQCLAQCAEVTPYL-LVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 132 DYINGGELFTHLsQRERFTEH------EVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK-EFVA 204
Cdd:cd05087  77 EFCPLGDLKGYL-RSCRAAESmapdplTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHcKYKE 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 205 DETERAYSFCGTIEYMAPDIVrggDSGHD--------KAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05087 156 DYFVTADQLWVPLRWIAPELV---DEVHGnllvvdqtKQSNVWSLGVTIWELFElGNQPY 212
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
161-301 6.54e-09

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 57.01  E-value: 6.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 161 IVLALEHLHKLGIIYR-DIKLENILLDSNGHVVLTDFGLsKEFVADETERAYSfcGTIE-----YMAPDIVRGGDSGH-- 232
Cdd:cd13992 106 IVKGMNYLHSSSIGYHgRLKSSNCLVDSRWVVKLTDFGL-RNLLEEQTNHQLD--EDAQhkkllWTAPELLRGSLLEVrg 182
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 233 DKAVDWWSLGVLMYELLTGASPFtvDGEKNSQAEISRRILKSEPPYPQEMSALAK------DLIQRLLMKDPKKR 301
Cdd:cd13992 183 TQKGDVYSFAIILYEILFRSDPF--ALEREVAIVEKVISGGNKPFRPELAVLLDEfpprlvLLVKQCWAENPEKR 255
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
52-255 6.83e-09

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 57.38  E-value: 6.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  52 LKVLGTGAYGKVFLVRKISGHDTGKL-YAMKVLKKATivqKAKTTEHTRTERQVLEHIRQsPFLVTLHYAFQTETkLHLI 130
Cdd:cd05110  12 VKVLGSGAFGTVYKGIWVPEGETVKIpVAIKILNETT---GPKANVEFMDEALIMASMDH-PHLVRLLGVCLSPT-IQLV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 131 LDYINGGELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETEr 209
Cdd:cd05110  87 TQLMPHGCLLDYVHEhKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKE- 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 210 aYSFCG---TIEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLT-GASPF 255
Cdd:cd05110 166 -YNADGgkmPIKWMALECIHYRKFTHQS--DVWSYGVTIWELMTfGGKPY 212
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
432-548 6.88e-09

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 57.05  E-value: 6.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK-----EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd07846   9 VGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKkiamrEIKMLKQLR-HENLVNLIEVFRRKKRWYLVFEFVDHTVL 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07846  88 DDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPE 129
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
25-255 6.91e-09

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 57.71  E-value: 6.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  25 LLTVKHELRTANLTGHAEKVGienFELLKVLGTGAYGKV--FLVRKISGHDTGKLYAMKvlkkATIVQKAKTTEHTRTER 102
Cdd:cd14207  64 LIHIGHHLNVVNLLGACTKSG---GPLMVIVEYCKYGNLsnYLKSKRDFFVTNKDTSLQ----EELIKEKKEAEPTGGKK 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 103 QVLEHIRQSPFLVTlhYAFQTETKLHLIL-DYINGGELFthlsqRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLE 181
Cdd:cd14207 137 KRLESVTSSESFAS--SGFQEDKSLSDVEeEEEDSGDFY-----KRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAAR 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 182 NILLDSNGHVVLTDFGLSKEFvadeteraysfcgtieYMAPDIVRGGD-----------SGHDKAV----DWWSLGVLMY 246
Cdd:cd14207 210 NILLSENNVVKICDFGLARDI----------------YKNPDYVRKGDarlplkwmapeSIFDKIYstksDVWSYGVLLW 273
                       250
                ....*....|
gi 32528297 247 ELLT-GASPF 255
Cdd:cd14207 274 EIFSlGASPY 283
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
430-548 6.93e-09

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 57.73  E-value: 6.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKrmEANTQKEITALKLCEG-------HPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd05594  31 KLLGKGTFGKVILVKEKATGRYYAMKILKK--EVIVAKDEVAHTLTENrvlqnsrHPFLTALKYSFQTHDRLCFVMEYAN 108
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMH-DVGVVHRDLKPE 548
Cdd:cd05594 109 GGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLE 155
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
432-547 7.00e-09

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 57.05  E-value: 7.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK----EITALKLCEgHPNIVKLHEVFHDQLHT--FLVMELLNGGE 505
Cdd:cd06621   9 LGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKqilrELEINKSCA-SPYIVKYYGAFLDEQDSsiGIAMEYCEGGS 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 506 L---FERIKKKK-HFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd06621  88 LdsiYKKVKKKGgRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKP 133
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
428-545 7.82e-09

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 56.74  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   428 KDKPLGEGSF-SICR---KCVHKKSNQAFAVKIISKRMEANTQKEI--TALKLCE-GHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:pfam07714   3 LGEKLGEGAFgEVYKgtlKGEGENTKIKVAVKTLKEGADEEEREDFleEASIMKKlDHPNIVKLLGVCTQGEPLYIVTEY 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 32528297   501 LNGGELFERIKKKK-HFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:pfam07714  83 MPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDL 128
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
47-255 8.74e-09

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 57.30  E-value: 8.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKV-----FLVRKISghdTGKLYAMKVLKKAtivqkAKTTEHT--RTERQVLEHIRQSPFLVTLHY 119
Cdd:cd05103   7 DRLKLGKPLGRGAFGQVieadaFGIDKTA---TCRTVAVKMLKEG-----ATHSEHRalMSELKILIHIGHHLNVVNLLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 AFqteTK----LHLILDYINGGELFTHL-SQRERFTEHEVQI--------YVGEI------------------------- 161
Cdd:cd05103  79 AC---TKpggpLMVIVEFCKFGNLSAYLrSKRSEFVPYKTKGarfrqgkdYVGDIsvdlkrrldsitssqssassgfvee 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 162 -------------------VLALEHL--------------HKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVAD-ET 207
Cdd:cd05103 156 kslsdveeeeagqedlykdFLTLEDLicysfqvakgmeflASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDpDY 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 208 ERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05103 236 VRKGDARLPLKWMAPETIF--DRVYTIQSDVWSFGVLLWEIFSlGASPY 282
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
51-302 9.41e-09

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 56.71  E-value: 9.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFL--VRKISGHDTGKLYAMKVLKKATIVQKAKTTEHtrtERQVLEHIrQSPFLVTLhYAFQTETK-L 127
Cdd:cd05049   9 LKRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASSPDARKDFER---EAELLTNL-QHENIVKF-YGVCTEGDpL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGGELFTHLSQ-------------------RERFTEHEVQIYVGEIVLALEHLhklgiIYRDIKLENILLDSN 188
Cdd:cd05049  84 LMVFEYMEHGDLNKFLRShgpdaaflasedsapgeltLSQLLHIAVQIASGMVYLASQHF-----VHRDLATRNCLVGTN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 189 GHVVLTDFGLSKEFVadeTERAYSFCGT----IEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLT-GASP-FTVDGEKN 262
Cdd:cd05049 159 LVVKIGDFGMSRDIY---STDYYRVGGHtmlpIRWMPPESILYRKFTTES--DVWSFGVVLWEIFTyGKQPwFQLSNTEV 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 32528297 263 SQAEISRRILKSEPPYPQEMSAL-----AKDLIQRLLMKDPKKRL 302
Cdd:cd05049 234 IECITQGRLLQRPRTCPSEVYAVmlgcwKREPQQRLNIKDIHKRL 278
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
430-548 9.54e-09

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 56.61  E-value: 9.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK----EITAL-KLceGHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd14046  12 QVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSrilrEVMLLsRL--NHQHVVRYYQAWIERANLYIQMEYCEKS 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14046  90 TLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPV 133
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
433-548 9.97e-09

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 57.35  E-value: 9.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 433 GEGSFSICRKcvhKKSNQAFAVKIISKRM-----EAN---TQKEI-TALKlcegHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05600  23 GYGSVFLARK---KDTGEICALKIMKKKVlfklnEVNhvlTERDIlTTTN----SPWLVKLLYAFQDPENVYLAMEYVPG 95
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05600  96 GDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPE 140
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
47-255 9.98e-09

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 56.57  E-value: 9.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLvrkiSGHDTGKLYAMKVLKKATIVQKAKTTEHTRTerQVLEHIRqspfLVTLHyAFQTETK 126
Cdd:cd05073  11 ESLKLEKKLGAGQFGEVWM----ATYNKHTKVAVKTMKPGSMSVEAFLAEANVM--KTLQHDK----LVKLH-AVVTKEP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 LHLILDYINGGELFTHLSQRE--RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK---- 200
Cdd:cd05073  80 IYIITEFMAKGSLLDFLKSDEgsKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARvied 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 201 -EFVADETERAysfcgTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05073 160 nEYTAREGAKF-----PIKWTAPEAINFGS--FTIKSDVWSFGILLMEIVTyGRIPY 209
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
432-546 1.14e-08

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 56.65  E-value: 1.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKI--ISKRMEANTQKEITALKLCEGHPNIVKLHEVF--------HDQLhtFLVMELL 501
Cdd:cd06637  14 VGNGTYGQVYKGRHVKTGQLAAIKVmdVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFikknppgmDDQL--WLVMEFC 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 NGGELFERIKKKK--HFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06637  92 GAGSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHKVIHRDIK 138
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
442-546 1.15e-08

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 55.90  E-value: 1.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 442 KCVHKKSNQAFAVKIISkrmEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELlNGGELFERIKKKKHFSETEA 521
Cdd:cd13976  11 RCVDIHTGEELVCKVVP---VPECHAVLRAYFRLPSHPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSRKRLREPEA 86
                        90       100
                ....*....|....*....|....*
gi 32528297 522 SYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd13976  87 ARLFRQIASAVAHCHRNGIVLRDLK 111
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
432-547 1.30e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 56.18  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM-----EANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd14138  13 IGSGEFGSVFKCVKRLDGCIYAIKRSKKPLagsvdEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQNEYCNGGSL 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 507 FERI----KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14138  93 ADAIsenyRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKP 137
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
432-547 1.38e-08

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 56.76  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELf 507
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRrqicREIEILRDVN-HPNVVKCHDMFDHNGEIQVLLEFMDGGSL- 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 32528297  508 erikKKKHF-SETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:PLN00034 160 ----EGTHIaDEQFLADVARQILSGIAYLHRRHIVHRDIKP 196
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
426-547 1.42e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 56.22  E-value: 1.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKDK-PLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK----EITALKLCEGHPNIVKLH-EVFHDQlHTFLVME 499
Cdd:cd06616   7 DLKDLgEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKrllmDLDVVMRSSDCPYIVKFYgALFREG-DCWICME 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 500 LLNGG-ELFERI---KKKKHFSETEASYIMRKLVSAVSHM-HDVGVVHRDLKP 547
Cdd:cd06616  86 LMDISlDKFYKYvyeVLDSVIPEEILGKIAVATVKALNYLkEELKIIHRDVKP 138
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
49-255 1.46e-08

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 56.00  E-value: 1.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVrKISGHDTGKLyamKVlkkatIVQKAKTTEHTRTERQ--VLEHIRQSPF-----LVTLHYAF 121
Cdd:cd05035   1 LKLGKILGEGEFGSVMEA-QLKQDDGSQL---KV-----AVKTMKVDIHTYSEIEefLSEAACMKDFdhpnvMRLIGVCF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 122 QTETKLHL-----ILDYINGGELFTHL------SQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGH 190
Cdd:cd05035  72 TASDLNKPpspmvILPFMKHGDLHSYLlysrlgGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMT 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 191 VVLTDFGLSKEFVADETERAYSFCGT-IEYMApdIVRGGDSGHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05035 152 VCVADFGLSRKIYSGDYYRQGRISKMpVKWIA--LESLADNVYTSKSDVWSFGVTMWEIATrGQTPY 216
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
432-548 1.54e-08

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 55.95  E-value: 1.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGgELF 507
Cdd:cd07836   8 LGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPstaiREISLMKELK-HENIVRLHDVIHTENKLMLVFEYMDK-DLK 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 508 ERIKKKKHFSETEAS---YIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07836  86 KYMDTHGVRGALDPNtvkSFTYQLLKGIAFCHENRVLHRDLKPQ 129
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
425-547 1.56e-08

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 55.74  E-value: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 425 LDLKDKPLGEGSfsiCRKCVHKKS--NQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd13982   2 LTFSPKVLGYGS---EGTIVFRGTfdGRPVAVKRLLPEFFDFADREVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCA 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 503 GgELFERIKKKKHFSETEASY-----IMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd13982  79 A-SLQDLVESPRESKLFLRPGlepvrLLRQIASGLAHLHSLNIVHRDLKP 127
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
427-547 1.67e-08

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 55.68  E-value: 1.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSIcrkcVHK---KSNQAFAVKIIS-KRMEANT----QKEITALKLCEGHPNIVKL--HEVFHDQLHTFL 496
Cdd:cd14131   4 EILKQLGKGGSSK----VYKvlnPKKKIYALKRVDlEGADEQTlqsyKNEIELLKKLKGSDRIIQLydYEVTDEDDYLYM 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 497 VMELlngGEL-FERIKKKKHFSETEASYIM---RKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14131  80 VMEC---GEIdLATILKKKRPKPIDPNFIRyywKQMLEAVHTIHEEGIVHSDLKP 131
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
430-547 1.71e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 56.27  E-value: 1.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ-----KEITALKLCEgHPNIVKLHEVFHDQ--LHTF----LVM 498
Cdd:cd07850   6 KPIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHakrayRELVLMKLVN-HKNIIGLLNVFTPQksLEEFqdvyLVM 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 499 ELLNGgELFERIKKKkhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07850  85 ELMDA-NLCQVIQMD--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKP 130
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
53-301 1.71e-08

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 55.40  E-value: 1.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVF---------LVRKISGHDTGKLYAMKVLKKATIVqkaKTTEHtrterqvlehirqsPFLVTLHYAFQT 123
Cdd:cd05085   2 ELLGKGNFGEVYkgtlkdktpVAVKTCKEDLPQELKIKFLSEARIL---KQYDH--------------PNIVKLIGVCTQ 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGELFTHLSQR--ERFTEHEVQIYVgEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKE 201
Cdd:cd05085  65 RQPIYIVMELVPGGDFLSFLRKKkdELKTKQLVKFSL-DAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 202 fvadETERAYSFCG----TIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFTvdGEKNSQA--EISRRILKS 274
Cdd:cd05085 144 ----EDDGVYSSSGlkqiPIKWTAPEALNYGR--YSSESDVWSFGILLWETFSlGVCPYP--GMTNQQAreQVEKGYRMS 215
                       250       260
                ....*....|....*....|....*...
gi 32528297 275 EPPY-PQEMSalakDLIQRLLMKDPKKR 301
Cdd:cd05085 216 APQRcPEDIY----KIMQRCWDYNPENR 239
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
47-255 1.79e-08

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 55.88  E-value: 1.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrkiSG--HDTGKLyAMKVLKKATivqkAKTTEHTRtERQVLEHIRQsPFLVTLhYAFQT- 123
Cdd:cd05068   8 KSLKLLRKLGSGQFGEVW-----EGlwNNTTPV-AVKTLKPGT----MDPEDFLR-EAQIMKKLRH-PKLIQL-YAVCTl 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLA-LEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEF 202
Cdd:cd05068  75 EEPIYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASgMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVI 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 203 VADETERAYSfcGT---IEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05068 155 KVEDEYEARE--GAkfpIKWTAPEAANY--NRFSIKSDVWSFGILLTEIVTyGRIPY 207
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
151-255 1.92e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 56.59  E-value: 1.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 151 EHEVQIYV-GEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKefVADETERAYSFCGTIEYMAPDIVRGgd 229
Cdd:cd07875 124 DHERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR--TAGTSFMMTPYVVTRYYRAPEVILG-- 199
                        90       100
                ....*....|....*....|....*.
gi 32528297 230 SGHDKAVDWWSLGVLMYELLTGASPF 255
Cdd:cd07875 200 MGYKENVDIWSVGCIMGEMIKGGVLF 225
Pkinase_C pfam00433
Protein kinase C terminal domain;
339-377 2.07e-08

Protein kinase C terminal domain;


Pssm-ID: 459809 [Multi-domain]  Cd Length: 42  Bit Score: 50.28  E-value: 2.07e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 32528297   339 IRDELDVSNFAEEFTEMDPTYSPA---ALPQSSEKLFQGYSF 377
Cdd:pfam00433   1 VKSETDTSNFDPEFTEEPPVLTPPdssILSSNDQEEFRGFSY 42
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
430-547 2.18e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 56.25  E-value: 2.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ-----KEITALKlCEGHPNIVKLHEVFHDQ------LHTFLVM 498
Cdd:cd07874  23 KPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHakrayRELVLMK-CVNHKNIISLLNVFTPQksleefQDVYLVM 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 499 ELLNGgELFERIKKKkhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07874 102 ELMDA-NLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKP 147
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
432-547 2.30e-08

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 55.73  E-value: 2.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISK---------------RMEANTQ--------------KEITALKLCEgHPNIV 482
Cdd:cd14200   8 IGKGSYGVVKLAYNESDDKYYAMKVLSKkkllkqygfprrpppRGSKAAQgeqakplaplervyQEIAILKKLD-HVNIV 86
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 483 KLHEVFHD--QLHTFLVMELLNGGELFErIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14200  87 KLIEVLDDpaEDNLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKP 152
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
104-321 2.30e-08

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 56.03  E-value: 2.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 104 VLEHIRQSPFLVTLHYAFQTETKLHLILDYINGGELFTHLsqRERFTEHEVQIYVGEI----VLALEHLHKLGIIYRDIK 179
Cdd:cd08226  51 VLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLL--KTYFPEGMNEALIGNIlygaIKALNYLHQNGCIHRSVK 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 180 LENILLDSNGHVVLTdfGLSKEF-VADETERA---YSF----CGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd08226 129 ASHILISGDGLVSLS--GLSHLYsMVTNGQRSkvvYDFpqfsTSVLPWLSPELLRQDLHGYNVKSDIYSVGITACELARG 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 252 ASPF-----------TVDGE-----------------KNSQAEISRRILKS---------------EPPYPQEMSALAKD 288
Cdd:cd08226 207 QVPFqdmrrtqmllqKLKGPpyspldifpfpelesrmKNSQSGMDSGIGESvatssmtrtmtserlQTPSSKTFSPAFHN 286
                       250       260       270
                ....*....|....*....|....*....|...
gi 32528297 289 LIQRLLMKDPKKRlgcgpRDADEIKEHLFFQKI 321
Cdd:cd08226 287 LVELCLQQDPEKR-----PSASSLLSHSFFKQV 314
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
432-548 2.75e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 55.81  E-value: 2.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCE------GHPNIVKLHEVFHDQLHTFLVMELLNGgE 505
Cdd:cd14229   8 LGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARlsnenaDEFNFVRAYECFQHRNHTCLVFEMLEQ-N 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 506 LFERIKKKKhFSETEASYI---MRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14229  87 LYDFLKQNK-FSPLPLKVIrpiLQQVATALKKLKSLGLIHADLKPE 131
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
420-546 2.81e-08

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 55.42  E-value: 2.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 420 YQHY--DLDLKD-----KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK---EITALKLCEgHPNIVKLHEVFH 489
Cdd:cd06644   1 YEHVrrDLDPNEvweiiGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDymvEIEILATCN-HPYIVKLLGAFY 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32528297 490 DQLHTFLVMELLNGGELFE-RIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06644  80 WDGKLWIMIEFCPGGAVDAiMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLK 137
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
427-546 2.91e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 55.13  E-value: 2.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIIS----------KRMEAnTQKEITALKLCEgHPNIVKLHEVFHDQLHTFL 496
Cdd:cd06630   3 LKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSfcrnssseqeEVVEA-IREEIRMMARLN-HPNIVRMLGATQHKSHFNI 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 497 VMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06630  81 FVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLK 130
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
432-547 2.95e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 55.84  E-value: 2.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALK-------LCEGH-PNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05633  13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNerimlslVSTGDcPFIVCMTYAFHTPDKLCFILDLMNG 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd05633  93 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKP 136
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
49-251 2.95e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 55.81  E-value: 2.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFlVTLHYAFQTETKLH 128
Cdd:cd14229   2 YEVLDFLGRGTFGQVV---KCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENADEFNF-VRAYECFQHRNHTC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGgELFTHLSQrERFTEHEVQIY---VGEIVLALEHLHKLGIIYRDIKLENILL----DSNGHVVLTDFG---- 197
Cdd:cd14229  78 LVFEMLEQ-NLYDFLKQ-NKFSPLPLKVIrpiLQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGsash 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 198 LSKEFVADETERAYsfcgtieYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14229 156 VSKTVCSTYLQSRY-------YRAPEIILG--LPFCEAIDMWSLGCVIAELFLG 200
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
99-318 3.23e-08

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 55.08  E-value: 3.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  99 RTERQVLEHIrQSPFLVTLHYAFQTETK----LHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLG-- 172
Cdd:cd14032  48 KEEAEMLKGL-QHPNIVRFYDFWESCAKgkrcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTpp 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 173 IIYRDIKLENILLDS-NGHVVLTDFGLSkefVADETERAYSFCGTIEYMAPDIVrggDSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14032 127 IIHRDLKCDNIFITGpTGSVKIGDLGLA---TLKRASFAKSVIGTPEFMAPEMY---EEHYDESVDVYAFGMCMLEMATS 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 252 ASPFTvdgEKNSQAEISRRILKSEPP--YPQEMSALAKDLIQRLLMKDPKKRLgcgprDADEIKEHLFF 318
Cdd:cd14032 201 EYPYS---ECQNAAQIYRKVTCGIKPasFEKVTDPEIKEIIGECICKNKEERY-----EIKDLLSHAFF 261
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
53-255 3.27e-08

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 54.88  E-value: 3.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRkisghdtgklyaMKVLKKATIVQKAKTTEHTRTERQVLEHIRQS--------PFLVTLHYAFQTE 124
Cdd:cd05065  10 EVIGAGEFGEVCRGR------------LKLPGKREIFVAIKTLKSGYTEKQRRDFLSEAsimgqfdhPNIIHLEGVVTKS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRE-RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFV 203
Cdd:cd05065  78 RPVMIITEFMENGALDSFLRQNDgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLE 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 204 ADETERAYSFC--GTI--EYMAPDIV--RGGDSghdkAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05065 158 DDTSDPTYTSSlgGKIpiRWTAPEAIayRKFTS----ASDVWSYGIVMWEVMSyGERPY 212
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
430-547 3.42e-08

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 55.27  E-value: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR-----MEANTQKEITALKLCEgHPNIVKLHEVFHDQLH-TFLVMELLng 503
Cdd:cd07856  16 QPVGMGAFGLVCSARDQLTGQNVAVKKIMKPfstpvLAKRTYRELKLLKHLR-HENIISLSDIFISPLEdIYFVTELL-- 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07856  93 GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKP 136
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
157-248 3.55e-08

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 55.05  E-value: 3.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 157 YVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETE-RAYSFCGTIEYMAPDIVRGGDSGHDKA 235
Cdd:cd14141 107 YLHEDIPGLKDGHKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAgDTHGQVGTRRYMAPEVLEGAINFQRDA 186
                        90
                ....*....|....*.
gi 32528297 236 ---VDWWSLGVLMYEL 248
Cdd:cd14141 187 flrIDMYAMGLVLWEL 202
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
430-548 3.69e-08

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 55.78  E-value: 3.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEAN---TQKEITALKlceGHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd05622  79 KVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemikRSDSAffwEERDIMAFA---NSPWVVQLFYAFQDDRYLYMVMEYM 155
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 NGGELFErIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05622 156 PGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPD 201
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
432-548 3.89e-08

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 54.76  E-value: 3.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVK---IISKRMEANTQK---EITALKLCEgHPNIVKLHEVF-HDQLHT-----FLVME 499
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKkcrQELSPSDKNRERwclEVQIMKKLN-HPNVVSARDVPpELEKLSpndlpLLAME 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 500 LLNGGELFERIKKKKHFS---ETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd13989  80 YCSGGDLRKVLNQPENCCglkESEVRTLLSDISSAISYLHENRIIHRDLKPE 131
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
416-548 3.91e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 54.80  E-value: 3.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 416 DSPFYQHYDldlKDKPLGEGSFSICRKCVHKKSNQAFAVKIIsKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHT- 494
Cdd:cd14047   1 DERFRQDFK---EIELIGSGGFGQVFKAKHRIDGKTYAIKRV-KLNNEKAEREVKALAKLD-HPNIVRYNGCWDGFDYDp 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 495 ---------------FLVMELLNGGELFERIKK--KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14047  76 etsssnssrsktkclFIQMEFCEKGTLESWIEKrnGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPS 146
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
432-545 3.99e-08

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 54.40  E-value: 3.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM-EANTQKEITAL-KLCegHPNIVKLHEV-FHD-QLHTflVMELLNGGELF 507
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSnRANMLREVQLMnRLS--HPNILRFMGVcVHQgQLHA--LTEYINGGNLE 76
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 32528297 508 ERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd14155  77 QLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDL 114
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
53-186 4.29e-08

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 54.67  E-value: 4.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIvqkakttehtrTE----RQVLEHIRQSPFL---VTLHYA--FQT 123
Cdd:cd13981   6 KELGEGGYASVYLAKDDDEQSDGSLVALKVEKPPSI-----------WEfyicDQLHSRLKNSRLResiSGAHSAhlFQD 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 124 ETKLHL-------ILDYINGgelfTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLD 186
Cdd:cd13981  75 ESILVMdyssqgtLLDVVNK----MKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLR 140
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
445-548 4.61e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 54.72  E-value: 4.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 445 HKKSNQAFAVKIISKR--------MEANTQKEItaLKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHF 516
Cdd:cd05609  21 HRETRQRFAMKKINKQnlilrnqiQQVFVERDI--LTFAE-NPFVVSMYCSFETKRHLCMVMEYVEGGDCATLLKNIGPL 97
                        90       100       110
                ....*....|....*....|....*....|..
gi 32528297 517 SETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05609  98 PVDMARMYFAETVLALEYLHSYGIVHRDLKPD 129
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
433-548 4.67e-08

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 54.44  E-value: 4.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 433 GEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ--KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFERI 510
Cdd:cd14111  12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGvlQEYEILKSLH-HERIMALHEAYITPRYLVLIAEFCSGKELLHSL 90
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 32528297 511 KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14111  91 IDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPD 128
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
432-547 4.80e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 55.05  E-value: 4.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALK-------LCEGH-PNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd14223   8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNerimlslVSTGDcPFIVCMSYAFHTPDKLSFILDLMNG 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14223  88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKP 131
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
123-248 5.04e-08

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 54.37  E-value: 5.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGGELFTHLsQRERFTEHEVQIYVGEIVLALEHLH--------KLGIIYRDIKLENILLDSNGHVVLT 194
Cdd:cd14143  64 TWTQLWLVSDYHEHGSLFDYL-NRYTVTVEGMIKLALSIASGLAHLHmeivgtqgKPAIAHRDLKSKNILVKKNGTCCIA 142
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 195 DFGLS--KEFVADETERAYSF-CGTIEYMAPDI------VRGGDSGhdKAVDWWSLGVLMYEL 248
Cdd:cd14143 143 DLGLAvrHDSATDTIDIAPNHrVGTKRYMAPEVlddtinMKHFESF--KRADIYALGLVFWEI 203
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
427-548 5.18e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 55.02  E-value: 5.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSF-SICRKCvHKKSNQAFAVKIISKR--MEANTQKEITALK--LCEGHPN-IVKLHEVFHDQLHTFLVMEL 500
Cdd:cd05626   4 VKIKTLGIGAFgEVCLAC-KVDTHALYAMKTLRKKdvLNRNQVAHVKAERdiLAEADNEwVVKLYYSFQDKDNLYFVMDY 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05626  83 IPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPD 130
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
432-546 5.25e-08

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 54.61  E-value: 5.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEANT---QKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd05589   7 LGRGHFGKVLLAEYKPTGELFAIKALKKgdiiaRDEVESlmcEKRIFETVNSARHPFLVNLFACFQTPEHVCFVMEYAAG 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 504 GELFERIkkkkH---FSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd05589  87 GDLMMHI----HedvFSEPRAVFYAACVVLGLQFLHEHKIVYRDLK 128
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
53-255 5.26e-08

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 54.13  E-value: 5.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  53 KVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERqVLEHirqSPFLVTLHYAFQTETKLhLILD 132
Cdd:cd05042   1 QEIGNGWFGKVLLGEIYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYR-ILQH---PNILQCLGQCVEAIPYL-LVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 133 YINGGELFTHL-SQRErfteHE--------VQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLS-KEF 202
Cdd:cd05042  76 FCDLGDLKAYLrSERE----HErgdsdtrtLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAhSRY 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 203 VADETERAYSFCGTIEYMAPDIVrggDSGHD--------KAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05042 152 KEDYIETDDKLWFPLRWTAPELV---TEFHDrllvvdqtKYSNIWSLGVTLWELFEnGAQPY 210
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
125-248 5.96e-08

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 54.40  E-value: 5.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGGELFTHLSQRERFTEhEVQIYVGEIVLALEHLH--------KLGIIYRDIKLENILLDSNGHVVLTDF 196
Cdd:cd14144  66 TQLYLITDYHENGSLYDFLRGNTLDTQ-SMLKLAYSAACGLAHLHteifgtqgKPAIAHRDIKSKNILVKKNGTCCIADL 144
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 197 GLSKEFVADETE---RAYSFCGTIEYMAPDIVrggDSGHD-------KAVDWWSLGVLMYEL 248
Cdd:cd14144 145 GLAVKFISETNEvdlPPNTRVGTKRYMAPEVL---DESLNrnhfdayKMADMYSFGLVLWEI 203
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
430-547 6.06e-08

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 54.19  E-value: 6.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK-EITALKLCEGHPNIVKL-----HEVFhdqlhTFLVMELLnG 503
Cdd:cd14017   6 KKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKmEVAVLKKLQGKPHFCRLigcgrTERY-----NYIVMTLL-G 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 504 GELFE--RIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14017  80 PNLAElrRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKP 125
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
430-548 6.42e-08

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 55.01  E-value: 6.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd05624  78 KVIGRGAFGEVAVVKMKNTERIYAMKILNKwemlkRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGG 157
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 505 ELFERIKK-KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05624 158 DLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPD 202
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
430-547 6.52e-08

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 54.72  E-value: 6.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSI-CR----------KCVHKKSNQAFAVKIISKRmeanTQKEITALKLCEGHPNIVKLHE---VFHDQLH-T 494
Cdd:cd07857   6 KELGQGAYGIvCSarnaetseeeTVAIKKITNVFSKKILAKR----ALRELKLLRHFRGHKNITCLYDmdiVFPGNFNeL 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 495 FLVMELLNGgELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07857  82 YLYEELMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKP 133
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
432-548 7.04e-08

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 54.12  E-value: 7.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRM--------EANTQKEItalkLCEGHPN-IVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd05608   9 LGKGGFGEVSACQMRATGKLYACKKLNKKRlkkrkgyeGAMVEKRI----LAKVHSRfIVSLAYAFQTKTDLCLVMTIMN 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 503 GGELFERI----KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05608  85 GGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPE 134
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
432-548 7.42e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 54.71  E-value: 7.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCE------GHPNIVKLHEVFHDQLHTFLVMELLNGgE 505
Cdd:cd14227  23 LGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARlstesaDDYNFVRAYECFQHKNHTCLVFEMLEQ-N 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 506 LFERIKKKKhFSETEASYI---MRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14227 102 LYDFLKQNK-FSPLPLKYIrpiLQQVATALMKLKSLGLIHADLKPE 146
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
429-547 7.67e-08

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 53.88  E-value: 7.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSFSICRKCVHKKSNQAFAVK------IISKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd08229  29 EKKIGRGQFSEVYRATCLLDGVPVALKkvqifdLMDAKARADCIKEIDLLKQLN-HPNVIKYYASFIEDNELNIVLELAD 107
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 503 GGELFERI----KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd08229 108 AGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKP 156
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
430-548 7.89e-08

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 54.64  E-value: 7.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd05623  78 KVIGRGAFGEVAVVKLKNADKVFAMKILNKwemlkRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGG 157
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 505 ELFERIKK-KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05623 158 DLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPD 202
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
432-547 8.53e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 53.78  E-value: 8.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIiSKRMEANTQKEITALK------LCEGHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd14139   8 IGVGEFGSVYKCIKRLDGCVYAIKR-SMRPFAGSSNEQLALHevyahaVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGGS 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 506 L----FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14139  87 LqdaiSENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKP 132
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
432-546 8.91e-08

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 53.60  E-value: 8.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKiiskRMEANTQK-------EITALKLCEgHPNIVKLHEVF--HDQLhtFLVMELLN 502
Cdd:cd06648  15 IGEGSTGIVCIATDKSTGRQVAVK----KMDLRKQQrrellfnEVVIMRDYQ-HPNIVEMYSSYlvGDEL--WVVMEFLE 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 503 GGELFErIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06648  88 GGALTD-IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIK 130
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
160-256 8.98e-08

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 53.84  E-value: 8.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 160 EIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIE------YMAPDIVRGGDSGHD 233
Cdd:cd08216 109 DVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRVVHDFPKSseknlpWLSPEVLQQNLLGYN 188
                        90       100
                ....*....|....*....|...
gi 32528297 234 KAVDWWSLGVLMYELLTGASPFT 256
Cdd:cd08216 189 EKSDIYSVGITACELANGVVPFS 211
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
51-255 1.12e-07

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 53.14  E-value: 1.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFlvrkiSGHdtgklyaMKVLKKATIVQKAKTTEHTRTERQVLEHIRQS--------PFLVTLhYAFQ 122
Cdd:cd05033   8 IEKVIGGGEFGEVC-----SGS-------LKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEAsimgqfdhPNVIRL-EGVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLIL-DYINGGELFTHLSQ-RERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSK 200
Cdd:cd05033  75 TKSRPVMIVtEYMENGSLDKFLREnDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSR 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 201 EFvaDETERAYSFCG---TIEYMAPDIVrggdsGHDK---AVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05033 155 RL--EDSEATYTTKGgkiPIRWTAPEAI-----AYRKftsASDVWSFGIVMWEVMSyGERPY 209
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
432-545 1.19e-07

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 52.88  E-value: 1.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ-KEITALKlCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERI 510
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFlKEVKLMR-RLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELL 79
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 32528297 511 KK-KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd14065  80 KSmDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDL 115
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
47-255 1.22e-07

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 53.58  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFLVRKIsGHDTGKLYAMKVlkkATIVQKAKTTEHTR----TERQVLEHIRQSPFLVTLHYAFQ 122
Cdd:cd05053  12 DRLTLGKPLGEGAFGQVVKAEAV-GLDNKPNEVVTV---AVKMLKDDATEKDLsdlvSEMEMMKMIGKHKNIINLLGACT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 123 TETKLHLILDYINGGELFTHLSQR----------------ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLd 186
Cdd:cd05053  88 QDGPLYVVVEYASKGNLREFLRARrppgeeaspddprvpeEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLV- 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 187 SNGHVV-LTDFGLSKEFvadETERAYSFCGT----IEYMAPDIVrgGDSGHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05053 167 TEDNVMkIADFGLARDI---HHIDYYRKTTNgrlpVKWMAPEAL--FDRVYTHQSDVWSFGVLLWEIFTlGGSPY 236
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
143-256 1.43e-07

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 53.44  E-value: 1.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 143 LSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG---HVVLTDFGLSKEFVADETERAY------SF 213
Cdd:cd14015 118 EKNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLGFGKnkdQVYLVDYGLASRYCPNGKHKEYkedprkAH 197
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 214 CGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFT 256
Cdd:cd14015 198 NGTIEFTSRDAHKG--VAPSRRGDLEILGYNMLQWLCGKLPWE 238
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
432-548 1.46e-07

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 53.18  E-value: 1.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIiSKRMEANTQKEITALK------LCEGHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd14051   8 IGSGEFGSVYKCINRLDGCVYAIKK-SKKPVAGSVDEQNALNevyahaVLGKHPHVVRYYSAWAEDDHMIIQNEYCNGGS 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 506 LFERI----KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14051  87 LADAIseneKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPG 133
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
137-292 1.48e-07

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 405254 [Multi-domain]  Cd Length: 288  Bit Score: 53.27  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   137 GELFTHLSQRERFTEH--EVQIYVGEIVLAlEHLHKLGIIYRDIKLENILLDSNGHVVLTDFG----LSKEFVADETERA 210
Cdd:pfam14531 128 GEVLLSHSSTHKSLVHhaRLQLTLQLIRLA-ANLQHYGLVHGQFTVDNFFLDQRGGVFLGGFEhlvrDGTKVVASEVPRG 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   211 YS---FCGTieymapdivRGGDSGHDK-----AVDWWSLGVLMYELLTGASPFTVDGEKNsqaeISRRILKSEPPYPQEM 282
Cdd:pfam14531 207 FAppeLLGS---------RGGYTMKNTtlmthAFDAWQLGLVIYWIWCLDLPNTLDAEEG----GIEWKFRLCKNIPEPV 273
                         170
                  ....*....|
gi 32528297   283 SALAKDLIQR 292
Cdd:pfam14531 274 RALLKGFLNY 283
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
430-546 1.61e-07

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 52.82  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKII-----SKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQL-HTFLVMELLNG 503
Cdd:cd08223   6 RVIGKGSYGEVWLVRHKRDRKQYVIKKLnlknaSKRERKAAEQEAKLLSKLK-HPNIVSYKESFEGEDgFLYIVMGFCEG 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKH--FSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd08223  85 GDLYTRLKEQKGvlLEERQVVEWFVQIAMALQYMHERNILHRDLK 129
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
430-547 1.82e-07

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 53.13  E-value: 1.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSF-SICrKCVHKKSNQAFAVKIISKRMEA-----NTQKEITALKLCEgHPNIVKLHEVF------HDQLHTFLV 497
Cdd:cd07878  21 TPVGSGAYgSVC-SAYDTRLRQKVAVKKLSRPFQSliharRTYRELRLLKHMK-HENVIGLLDVFtpatsiENFNEVYLV 98
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 498 MELLnGGELfERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07878  99 TNLM-GADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKP 146
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
430-548 1.88e-07

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 52.66  E-value: 1.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISkrMEANTQKEITALK---LCEG--HPNIVKLHEVFHDQLHTFLVMELLNGG 504
Cdd:cd07870   6 EKLGEGSYATVYKGISRINGQLVALKVIS--MKTEEGVPFTAIReasLLKGlkHANIVLLHDIIHTKETLTFVFEYMHTD 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 505 ELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07870  84 LAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQ 127
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
42-255 1.88e-07

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 52.71  E-value: 1.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  42 EKVGIENFELLKVLGTGAYGKVF---LVRKISGHDTgKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHirqsPFLVTLH 118
Cdd:cd05091   1 KEINLSAVRFMEELGEDRFGKVYkghLFGTAPGEQT-QAVAIKTLKDKAEGPLREEFRHEAMLRSRLQH----PNIVCLL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 119 YAFQTETKLHLILDYINGGELFTHLSQRERF-----TEHEVQI-----------YVGEIVLALEHLHKLGIIYRDIKLEN 182
Cdd:cd05091  76 GVVTKEQPMSMIFSYCSHGDLHEFLVMRSPHsdvgsTDDDKTVkstlepadflhIVTQIAAGMEYLSSHHVVHKDLATRN 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 183 ILLDSNGHVVLTDFGLSKE-FVADeterAYSFCGT----IEYMAPDIVRGGDSGHDKavDWWSLGVLMYELLT-GASPF 255
Cdd:cd05091 156 VLVFDKLNVKISDLGLFREvYAAD----YYKLMGNsllpIRWMSPEAIMYGKFSIDS--DIWSYGVVLWEVFSyGLQPY 228
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
51-255 2.06e-07

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 53.10  E-value: 2.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  51 LLKVLGTGAYGKVFLVRKIsGHDTGK-----LYAMKVLKKATivqKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTET 125
Cdd:cd05100  16 LGKPLGEGCFGQVVMAEAI-GIDKDKpnkpvTVAVKMLKDDA---TDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 126 KLHLILDYINGGELFTHLSQR----------------ERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG 189
Cdd:cd05100  92 PLYVLVEYASKGNLREYLRARrppgmdysfdtcklpeEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32528297 190 HVVLTDFGLSKEF-VADETERAYSFCGTIEYMAPDIVRggDSGHDKAVDWWSLGVLMYELLT-GASPF 255
Cdd:cd05100 172 VMKIADFGLARDVhNIDYYKKTTNGRLPVKWMAPEALF--DRVYTHQSDVWSFGVLLWEIFTlGGSPY 237
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
428-546 2.14e-07

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 52.38  E-value: 2.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKII----SKRMEANTQKEITALKLCEGhPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd06641   8 KLEKIGKGSFGEVFKGIDNRTQKVVAIKIIdleeAEDEIEDIQQEITVLSQCDS-PYVTKYYGSYLKDTKLWIIMEYLGG 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 504 GELFERIKKKKhFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06641  87 GSALDLLEPGP-LDETQIATILREILKGLDYLHSEKKIHRDIK 128
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
430-547 2.16e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 53.11  E-value: 2.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ-----KEITALKlCEGHPNIVKLHEVFHDQ------LHTFLVM 498
Cdd:cd07876  27 KPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHakrayRELVLLK-CVNHKNIISLLNVFTPQksleefQDVYLVM 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 499 ELLNGgELFERIKKKkhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07876 106 ELMDA-NLCQVIHME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKP 151
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
428-548 2.30e-07

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 52.51  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQ-------KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMEL 500
Cdd:PLN00009   6 KVEKIGEGTYGVVYKARDRVTNETIALKKI--RLEQEDEgvpstaiREISLLKEMQ-HGNIVRLQDVVHSEKRLYLVFEY 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297  501 LNggelferIKKKKHFSETE---------ASYiMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:PLN00009  83 LD-------LDLKKHMDSSPdfaknprliKTY-LYQILRGIAYCHSHRVLHRDLKPQ 131
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
430-547 2.33e-07

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 52.42  E-value: 2.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKK-SNQAFAVKIISK----------RM-EANTQKEITAlklcEGHPNIVKLHEVFHDQLHTFLV 497
Cdd:cd14052   6 ELIGSGEFSQVYKVSERVpTGKVYAVKKLKPnyagakdrlrRLeEVSILRELTL----DGHDNIVQLIDSWEYHGHLYIQ 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 498 MELLNGGEL---FERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14052  82 TELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKP 134
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
417-547 3.07e-07

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 52.31  E-value: 3.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 417 SPFYQHYDLdlkdkpLGEGSFSICRKCVHKKSNQAFAVKIIS---KRMEA-NTQKEITALKLCEgHPNIVKLHEV----- 487
Cdd:cd07849   4 GPRYQNLSY------IGEGAYGMVCSAVHKPTGQKVAIKKISpfeHQTYClRTLREIKILLRFK-HENIIGILDIqrppt 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 488 ---FHDqlhTFLVMELLNGgELFeRIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07849  77 fesFKD---VYIVQELMET-DLY-KLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKP 134
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
432-547 3.17e-07

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 52.18  E-value: 3.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII--SKRMEANTQ--KEITALKLCEgHPNIVKLHEVFH-----------DQLHTFL 496
Cdd:cd14048  14 LGRGGFGVVFEAKNKVDDCNYAVKRIrlPNNELAREKvlREVRALAKLD-HPGIVRYFNAWLerppegwqekmDEVYLYI 92
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 497 VMELLNGGELFERIKKKKHFSETEASY---IMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd14048  93 QMQLCRKENLKDWMNRRCTMESRELFVclnIFKQIASAVEYLHSKGLIHRDLKP 146
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
478-548 3.18e-07

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 52.29  E-value: 3.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297  478 HPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:PTZ00426  90 HPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPE 160
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
432-548 3.23e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 52.40  E-value: 3.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCE------GHPNIVKLHEVFHDQLHTFLVMELLNGgE 505
Cdd:cd14228  23 LGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRlssenaDEYNFVRSYECFQHKNHTCLVFEMLEQ-N 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 506 LFERIKKKKhFSETEASYI---MRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14228 102 LYDFLKQNK-FSPLPLKYIrpiLQQVATALMKLKSLGLIHADLKPE 146
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
429-548 3.24e-07

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 52.32  E-value: 3.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSFSICRKCVHKKSNQAFAVKII--SKRMEANTQKEITALKLCEGHP-----NIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd14226  18 DSLIGKGSFGQVVKAYDHVEQEWVAIKIIknKKAFLNQAQIEVRLLELMNKHDtenkyYIVRLKRHFMFRNHLCLVFELL 97
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 502 NgGELFERIkKKKHFSETEASYIMR---KLVSAVSHMH--DVGVVHRDLKPE 548
Cdd:cd14226  98 S-YNLYDLL-RNTNFRGVSLNLTRKfaqQLCTALLFLStpELSIIHCDLKPE 147
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
49-301 3.25e-07

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 52.02  E-value: 3.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvRKISGHDtGKLYAMKVLKKATivqkAKTTEHTRTERQVLEH--IRQSPFLVTLHYAFQTETk 126
Cdd:cd14051   2 FHEVEKIGSGEFGSVY--KCINRLD-GCVYAIKKSKKPV----AGSVDEQNALNEVYAHavLGKHPHVVRYYSAWAEDD- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 127 lHLIL--DYINGGELFTHLSQRE----RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDfGLSK 200
Cdd:cd14051  74 -HMIIqnEYCNGGSLADAISENEkageRFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSSE-EEEE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 201 EFVADETERAYSFC--------------------GTIEYMAPDIVRGGDSGHDKAvDWWSLGVLMYElLTGASPFTVDGE 260
Cdd:cd14051 152 DFEGEEDNPESNEVtykigdlghvtsisnpqveeGDCRFLANEILQENYSHLPKA-DIFALALTVYE-AAGGGPLPKNGD 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 32528297 261 KnsqaeiSRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKR 301
Cdd:cd14051 230 E------WHEIRQGNLPPLPQCSPEFNELLRSMIHPDPEKR 264
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
460-548 3.35e-07

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 53.31  E-value: 3.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297    460 RMEANTQKEITalkLCEG--HPNIVKLHE--VFHDQLhTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHM 535
Cdd:TIGR03903   20 HQRARFRRETA---LCARlyHPNIVALLDsgEAPPGL-LFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACA 95
                           90
                   ....*....|...
gi 32528297    536 HDVGVVHRDLKPE 548
Cdd:TIGR03903   96 HNQGIVHRDLKPQ 108
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
432-548 3.39e-07

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 51.83  E-value: 3.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSF-SICRKCVhKKSNQAFAVKIISKRMEANTQKEITAL---KLCE--GHPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd05607  10 LGKGGFgEVCAVQV-KNTGQMYACKKLDKKRLKKKSGEKMALlekEILEkvNSPFIVSLAYAFETKTHLCLVMSLMNGGD 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 506 LFERIKK--KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05607  89 LKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPE 133
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
430-547 3.76e-07

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 52.35  E-value: 3.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ-----KEITALKlCEGHPNIVKLHEVFHDQ------LHTFLVM 498
Cdd:cd07875  30 KPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHakrayRELVLMK-CVNHKNIIGLLNVFTPQksleefQDVYIVM 108
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 499 ELLNGgELFERIKKKkhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07875 109 ELMDA-NLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKP 154
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
367-546 4.02e-07

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 52.71  E-value: 4.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  367 SSEKLFQGYSFVAPSILF------KRNAAVIDPLQFHMGVERPGVTNVARSammkDSPFYQHYDLD-LKDKPLGEGSFSI 439
Cdd:PTZ00267  11 ASAELLNQYAKYFPHVLFtseeafEKYCADLDPEAYKKCVDLPEGEEVPES----NNPREHMYVLTtLVGRNPTTAAFVA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  440 CRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKK--KKH-- 515
Cdd:PTZ00267  87 TRGSDPKEKVVAKFVMLNDERQAAYARSELHCLAACD-HFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQrlKEHlp 165
                        170       180       190
                 ....*....|....*....|....*....|.
gi 32528297  516 FSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:PTZ00267 166 FQEYEVGLLFYQIVLALDEVHSRKMMHRDLK 196
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
432-548 4.41e-07

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 51.84  E-value: 4.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSicRKCVHKKSNQAFAVKIISKRMEANTQ------KEITALKLCEgHPNIVKLHEVFHDQLHT-----FLVMEL 500
Cdd:cd14039   1 LGTGGFG--NVCLYQNQETGEKIAIKSCRLELSVKnkdrwcHEIQIMKKLN-HPNVVKACDVPEEMNFLvndvpLLAMEY 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 501 LNGGELFERIKKKKH---FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14039  78 CSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPE 128
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
432-546 4.47e-07

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 51.60  E-value: 4.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII----SKRMEANTQKEITALKLCEGhPNIVKLHEVFHDQLHTFLVMELLNGGELF 507
Cdd:cd06642  12 IGKGSFGEVYKGIDNRTKEVVAIKIIdleeAEDEIEDIQQEITVLSQCDS-PYITRYYGSYLKGTKLWIIMEYLGGGSAL 90
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 508 ERIKKKKhFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06642  91 DLLKPGP-LEETYIATILREILKGLDYLHSERKIHRDIK 128
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
430-548 4.66e-07

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 51.34  E-value: 4.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEA-NTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELL--NGGEL 506
Cdd:cd14127   6 KKIGEGSFGVIFEGTNLLNGQQVAIKFEPRKSDApQLRDEYRTYKLLAGCPGIPNVYYFGQEGLHNILVIDLLgpSLEDL 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 507 FERIKKKkhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14127  86 FDLCGRK--FSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPD 125
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
427-548 5.25e-07

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 51.97  E-value: 5.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSicRKCVHKK--SNQAFAVKIISKR--MEANTQKEITALK--LCEGHPN-IVKLHEVFHDQLHTFLVME 499
Cdd:cd05625   4 VKIKTLGIGAFG--EVCLARKvdTKALYATKTLRKKdvLLRNQVAHVKAERdiLAEADNEwVVRLYYSFQDKDNLYFVMD 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05625  82 YIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPD 130
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
49-251 6.06e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 51.63  E-value: 6.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFlVTLHYAFQTETKLH 128
Cdd:cd14227  17 YEVLEFLGRGTFGQVV---KCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNF-VRAYECFQHKNHTC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 129 LILDYINGgELFTHLSQrERFTE---HEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG----HVVLTDFG---- 197
Cdd:cd14227  93 LVFEMLEQ-NLYDFLKQ-NKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSrqpyRVKVIDFGsash 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 198 LSKEFVADETERAYsfcgtieYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14227 171 VSKAVCSTYLQSRY-------YRAPEIILG--LPFCEAIDMWSLGCVIAELFLG 215
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
48-251 6.80e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 51.63  E-value: 6.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  48 NFELLKVLGTGAYGKVFLVRKISghdTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFlVTLHYAFQTETKL 127
Cdd:cd14228  16 SYEVLEFLGRGTFGQVAKCWKRS---TKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNF-VRSYECFQHKNHT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 128 HLILDYINGgELFTHLSQrERFTE---HEVQIYVGEIVLALEHLHKLGIIYRDIKLENILL----DSNGHVVLTDFG--- 197
Cdd:cd14228  92 CLVFEMLEQ-NLYDFLKQ-NKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGsas 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 198 -LSKEFVADETERAYsfcgtieYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14228 170 hVSKAVCSTYLQSRY-------YRAPEIILG--LPFCEAIDMWSLGCVIAELFLG 215
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
430-546 7.15e-07

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 50.81  E-value: 7.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEA-NTQKEITALKlCE-------GHPNIVKLHEVFHDQLHTFL--VME 499
Cdd:cd06652   8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESpETSKEVNALE-CEiqllknlLHERIVQYYGCLRDPQERTLsiFME 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06652  87 YMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIK 133
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
432-545 7.21e-07

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 50.97  E-value: 7.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISK---RMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIRfdeEAQRNFLKEVKVMRSLD-HPNVLKFIGVLYKDKKLNLITEYIPGGTLKD 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 32528297 509 RIK-KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd14154  80 VLKdMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDL 117
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
430-547 7.22e-07

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 51.22  E-value: 7.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISK----RMEA-NTQKEITALKLCEgHPNIVKLHEV--------FHDqlhTFL 496
Cdd:cd07858  11 KPIGRGAYGIVCSAKNSETNEKVAIKKIANafdnRIDAkRTLREIKLLRHLD-HENVIAIKDImppphreaFND---VYI 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 497 VMELLNGgELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07858  87 VYELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKP 136
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
430-545 9.10e-07

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 50.43  E-value: 9.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHK-KSNQ--AFAVKIISKRMEANTQKEI--TALKLCE-GHPNIVKLHEV-FHDQLhtFLVMELLN 502
Cdd:cd05060   1 KELGHGNFGSVRKGVYLmKSGKevEVAVKTLKQEHEKAGKKEFlrEASVMAQlDHPCIVRLIGVcKGEPL--MLVMELAP 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd05060  79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDL 121
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
435-548 9.69e-07

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 50.22  E-value: 9.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 435 GSFSICRKCVHKKS--NQAFAVKIISKRMEA-NTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGgELFERIK 511
Cdd:cd14112  14 GRFSVIVKAVDSTTetDAHCAVKIFEVSDEAsEAVREFESLRTLQ-HENVQRLIAAFKPSNFAYLVMEKLQE-DVFTRFS 91
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 32528297 512 KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14112  92 SNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPD 128
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
477-548 1.24e-06

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 49.85  E-value: 1.24e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 477 GHPNIVKLHEVFHDQLHTFLVMEL-LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14101  65 GHRGVIRLLDWFEIPEGFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDE 137
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
430-548 1.32e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 51.28  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297   430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKR-----------MEANTQKEITalklcegHPNIVKLHEVFHDQLHT--FL 496
Cdd:PTZ00266   19 KKIGNGRFGEVFLVKHKRTQEFFCWKAISYRglkereksqlvIEVNVMRELK-------HKNIVRYIDRFLNKANQklYI 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297   497 VMELLNGGELFERIKK-KKHFSETEASYIM---RKLVSAVSHMHDVG-------VVHRDLKPE 548
Cdd:PTZ00266   92 LMEFCDAGDLSRNIQKcYKMFGKIEEHAIVditRQLLHALAYCHNLKdgpngerVLHRDLKPQ 154
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
430-547 1.35e-06

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 50.67  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSF-SICrKCVHKKSNQAFAVKIISKRMEAN-----TQKEITALKLCEgHPNIVKLHEVF-----HDQLHTF-LV 497
Cdd:cd07879  21 KQVGSGAYgSVC-SAIDKRTGEKVAIKKLSRPFQSEifakrAYRELTLLKHMQ-HENVIGLLDVFtsavsGDEFQDFyLV 98
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 498 MEllnggelFERIKKKK----HFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07879  99 MP-------YMQTDLQKimghPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKP 145
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
49-251 1.41e-06

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 50.52  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  49 FELLKVLGTGAYGKVFLVRKisgHDTGKLYAMKVLKkativQKAKTTEHTRTERQVLEHIRQSPF----LVTLHYAFQTE 124
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWK---RGTNEIVAIKILK-----NHPSYARQGQIEVSILSRLSQENAdefnFVRAYECFQHK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 125 TKLHLILDYINGgELFTHLSQRE--RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG----HVVLTDFGl 198
Cdd:cd14211  73 NHTCLVFEMLEQ-NLYDFLKQNKfsPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFG- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 199 SKEFVADETERAYsfCGTIEYMAPDIVRGgdSGHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14211 151 SASHVSKAVCSTY--LQSRYYRAPEIILG--LPFCEAIDMWSLGCVIAELFLG 199
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
432-545 1.45e-06

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 49.95  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISkRMEANTQ----KEITALKlCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELF 507
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELI-RFDEETQrtflKEVKVMR-CLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLR 78
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 508 ERIKK-KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd14221  79 GIIKSmDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDL 117
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
432-547 1.45e-06

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 50.13  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALK---------LCEGHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd05606   2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNerimlslvsTGGDCPFIVCMTYAFQTPDKLCFILDLMN 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 503 GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd05606  82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKP 126
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
404-548 1.74e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 50.46  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  404 GVTNVARSAMMKDSPFYQHYDLdLKDKPLGE-GSFSIC------------RKCVHKKSNQAFAVKIISKRMEANT----- 465
Cdd:PHA03210 131 GPVPLAQAKLKHDDEFLAHFRV-IDDLPAGAfGKIFICalrasteeaearRGVNSTNQGKPKCERLIAKRVKAGSraaiq 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  466 -QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVME--------LLNGGELfeRIKKKKHFSETEAsyIMRKLVSAVSHMH 536
Cdd:PHA03210 210 lENEILALGRLN-HENILKIEEILRSEANTYMITQkydfdlysFMYDEAF--DWKDRPLLKQTRA--IMKQLLCAVEYIH 284
                        170
                 ....*....|..
gi 32528297  537 DVGVVHRDLKPE 548
Cdd:PHA03210 285 DKKLIHRDIKLE 296
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
424-547 1.88e-06

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 49.75  E-value: 1.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKD----KPLGEGSFSICRKCVHKKSNQAFAVKII---SKR-MEANTQKEITALKLCEgHPNIVKLHEVFHDQL-HT 494
Cdd:cd06620   1 DLKNQDletlKDLGAGNGGSVSKVLHIPTGTIMAKKVIhidAKSsVRKQILRELQILHECH-SPYIVSFYGAFLNENnNI 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 495 FLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDV-GVVHRDLKP 547
Cdd:cd06620  80 IICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKP 133
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
432-547 1.93e-06

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 49.58  E-value: 1.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVhKKSNQAFAVKIISKrMEANT-----QKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd14066   1 IGSGGFGTVYKGV-LENGTVVAVKRLNE-MNCAAskkefLTELEMLGRLR-HPNLVRLLGYCLESDEKLLVYEYMPNGSL 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 507 FERIKKkkHFSETEASYIMR-----KLVSAVSHMH---DVGVVHRDLKP 547
Cdd:cd14066  78 EDRLHC--HKGSPPLPWPQRlkiakGIARGLEYLHeecPPPIIHGDIKS 124
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
430-547 2.02e-06

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 49.95  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN-----TQKEITALKLCEgHPNIVKLHEVFH-----DQLHTF-LVM 498
Cdd:cd07880  21 KQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSElfakrAYRELRLLKHMK-HENVIGLLDVFTpdlslDRFHDFyLVM 99
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 499 ELLngGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07880 100 PFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKP 146
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
427-548 2.59e-06

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 49.30  E-value: 2.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQKEITALK---LCEG--HPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd07844   3 KKLDKLGEGSYATVYKGRSKLTGQLVALKEI--RLEHEEGAPFTAIReasLLKDlkHANIVTLHDIIHTKKTLTLVFEYL 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 502 NggelferiKKKKHFSETEASYI--------MRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07844  81 D--------TDLKQYMDDCGGGLsmhnvrlfLFQLLRGLAYCHQRRVLHRDLKPQ 127
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
428-547 2.95e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 49.37  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  428 KDKPLGEGSFSICRKCVHKKSNQAFAVKI-----ISKRMEANTQK------------EITALKLCEgHPNIVKLHEVFHD 490
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAYDTLTGKIVAIKKvkiieISNDVTKDRQLvgmcgihfttlrELKIMNEIK-HENIMGLVDVYVE 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297  491 QLHTFLVMELLNGgELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:PTZ00024  92 GDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSP 147
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
432-546 3.89e-06

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 48.51  E-value: 3.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII----SKRMEANTQKEITALKLCEGhPNIVKLHEVFHDQLHTFLVMELLNGGELF 507
Cdd:cd06640  12 IGKGSFGEVFKGIDNRTQQVVAIKIIdleeAEDEIEDIQQEITVLSQCDS-PYVTKYYGSYLKGTKLWIIMEYLGGGSAL 90
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 508 ERIKKKKhFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06640  91 DLLRAGP-FDEFQIATMLKEILKGLDYLHSEKKIHRDIK 128
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
410-546 4.72e-06

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 48.49  E-value: 4.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 410 RSAMMKDSpfyQHYDLDLKDKP---------LGEGSFSICRKCVHKKSNQAFAVKIIS---KRMEANTQKEITALKLCE- 476
Cdd:cd06633   1 RKGVLKDP---EIADLFYKDDPeeifvdlheIGHGSFGAVYFATNSHTNEVVAIKKMSysgKQTNEKWQDIIKEVKFLQq 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 477 -GHPNIVKLHEVFHDQLHTFLVME--LLNGGELFEriKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06633  78 lKHPNTIEYKGCYLKDHTAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIK 148
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
432-548 5.16e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 48.20  E-value: 5.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIS-----KRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGgel 506
Cdd:cd07839   8 IGEGTYGTVFKAKNRETHEIVALKRVRlddddEGVPSSALREICLLKELK-HKNIVRLYDVLHSDKKLTLVFEYCDQ--- 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 507 feriKKKKHFS----ETEASYI---MRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07839  84 ----DLKKYFDscngDIDPEIVksfMFQLLKGLAFCHSHNVLHRDLKPQ 128
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
432-545 5.19e-06

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 48.40  E-value: 5.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISkRMEANTQKE-ITALKLCEG--HPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELI-RCDEETQKTfLTEVKVMRSldHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKD 79
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 32528297 509 RIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd14222  80 FLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDL 116
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
432-548 5.58e-06

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 48.55  E-value: 5.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII--SKRMEANTQKEITAL-----KLCEGHPNIVKLHEVFHDQLHTFLVMELLnGG 504
Cdd:cd14225  51 IGKGSFGQVVKALDHKTNEHVAIKIIrnKKRFHHQALVEVKILdalrrKDRDNSHNVIHMKEYFYFRNHLCITFELL-GM 129
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 505 ELFERIkKKKHFSETEASYIMRKLVSAVSHM---HDVGVVHRDLKPE 548
Cdd:cd14225 130 NLYELI-KKNNFQGFSLSLIRRFAISLLQCLrllYRERIIHCDLKPE 175
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
429-546 7.30e-06

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 48.71  E-value: 7.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  429 DKPLGEGSFS--ICRKCVhkKSNQAFAVKIISkrMEANT-------QKEITALKLCEgHPNIVKLHEVF--------HDQ 491
Cdd:PTZ00283  37 SRVLGSGATGtvLCAKRV--SDGEPFAVKVVD--MEGMSeadknraQAEVCCLLNCD-FFSIVKCHEDFakkdprnpENV 111
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297  492 LHTFLVMELLNGGELFERIKKK----KHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:PTZ00283 112 LMIALVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIK 170
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
422-546 7.65e-06

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 48.08  E-value: 7.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 422 HYDLDLKdkpLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN-----TQKEITALKLCEgHPNIVKLHEVF---HDQLH 493
Cdd:cd07866   9 DYEILGK---LGEGTFGEVYKARQIKTGRVVALKKILMHNEKDgfpitALREIKILKKLK-HPNVVPLIDMAverPDKSK 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 494 -----TFLVMEL----LNGgeLFE--RIkkkkHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd07866  85 rkrgsVYMVTPYmdhdLSG--LLEnpSV----KLTESQIKCYMLQLLEGINYLHENHILHRDIK 142
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
432-548 1.02e-05

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 47.31  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGgELF 507
Cdd:cd07871  13 LGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPctaiREVSLLKNLK-HANIVTLHDIIHTERCLTLVFEYLDS-DLK 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 32528297 508 ERIKKKKHF-SETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07871  91 QYLDNCGNLmSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQ 132
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
445-546 1.02e-05

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 47.67  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 445 HKKSNQAFAVKIISkrMEANTQKEITAL--------KLCegHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKkkHF 516
Cdd:cd08216  21 HKPTNTLVAVKKIN--LESDSKEDLKFLqqeiltsrQLQ--HPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLLKT--HF 94
                        90       100       110
                ....*....|....*....|....*....|....
gi 32528297 517 S----ETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd08216  95 PeglpELAIAFILRDVLNALEYIHSKGYIHRSVK 128
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
421-547 1.16e-05

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 47.37  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 421 QHYDLDLKD----KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEI----TALKLCEGHPNIVKLHEVFHDQL 492
Cdd:cd06618   8 KKYKADLNDlenlGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRIlmdlDVVLKSHDCPYIVKCYGYFITDS 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32528297 493 HTFLVMELLngGELFERIKK--KKHFSEteasYIMRKL-VSAVSHMHDV----GVVHRDLKP 547
Cdd:cd06618  88 DVFICMELM--STCLDKLLKriQGPIPE----DILGKMtVSIVKALHYLkekhGVIHRDVKP 143
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
428-548 1.17e-05

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 47.38  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNG 503
Cdd:cd07869   9 KLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPftaiREASLLKGLK-HANIVLLHDIIHTKETLTLVFEYVHT 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 504 GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07869  88 DLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQ 132
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
442-546 1.38e-05

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 46.80  E-value: 1.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 442 KCVHKKSNQAFAVKIISKRmeaNTQKEITALKLCEGHPNIVKLHEVF--HDQLHTFLVMellNGGELFERIKKKKHFSET 519
Cdd:cd14024  11 RAEHYQTEKEYTCKVLSLR---SYQECLAPYDRLGPHEGVCSVLEVVigQDRAYAFFSR---HYGDMHSHVRRRRRLSED 84
                        90       100
                ....*....|....*....|....*..
gi 32528297 520 EASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd14024  85 EARGLFTQMARAVAHCHQHGVILRDLK 111
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
423-546 1.40e-05

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 47.02  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 423 YDLDLKDKP--LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ---KEItAL--KLCegHPNIVKLHEVFHDQLHTF 495
Cdd:cd06624   5 YEYDESGERvvLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQplhEEI-ALhsRLS--HKNIVQYLGSVSEDGFFK 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 496 LVMELLNGGELFERIKKK---KHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06624  82 IFMEQVPGGSLSALLRSKwgpLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIK 135
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
432-547 1.53e-05

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 46.97  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIS-KRMEANTQKEITALKLCE--------GHPNIVKLHEVFHDQLHTF-LVMELL 501
Cdd:cd14040  14 LGRGGFSEVYKAFDLYEQRYAAVKIHQlNKSWRDEKKENYHKHACReyrihkelDHPRIVKLYDYFSLDTDTFcTVLEYC 93
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 502 NGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVG--VVHRDLKP 547
Cdd:cd14040  94 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKP 141
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
421-546 1.66e-05

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 46.56  E-value: 1.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 421 QHyDLDLKDKpLGEGSFSICRKCVHKKSNQAFAVKIIskRMEAN-----TQKEITALKLCEgHPNIVKLHEVFHDQLHTF 495
Cdd:cd06646   8 QH-DYELIQR-VGSGTYGDVYKARNLHTGELAAVKII--KLEPGddfslIQQEIFMVKECK-HCNIVAYFGSYLSREKLW 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32528297 496 LVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06646  83 ICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIK 133
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
428-546 1.96e-05

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 46.61  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEA-NTQKEITALKlCE-------GHPNIVKLHEVFHDQLHTFLV-- 497
Cdd:cd06651  11 RGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESpETSKEVSALE-CEiqllknlQHERIVQYYGCLRDRAEKTLTif 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 498 MELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06651  90 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIK 138
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
432-547 1.97e-05

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 46.59  E-value: 1.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKI--ISKRMEaNTQKEITALKLCE--------GHPNIVKLHEVFHDQLHTF-LVMEL 500
Cdd:cd14041  14 LGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNWR-DEKKENYHKHACReyrihkelDHPRIVKLYDYFSLDTDSFcTVLEY 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVG--VVHRDLKP 547
Cdd:cd14041  93 CEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKP 141
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
47-251 2.02e-05

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 46.93  E-value: 2.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  47 ENFELLKVLGTGAYGKVFlvrKISGHDTGKLYAMKVLKKativqKAKTTEHTRTERQVLEHIRQSP-----FLVTL--HY 119
Cdd:cd14226  13 DRYEIDSLIGKGSFGQVV---KAYDHVEQEWVAIKIIKN-----KKAFLNQAQIEVRLLELMNKHDtenkyYIVRLkrHF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 120 AFqtetKLHLILDYinggELFTH-LSQRERFTE-HEVQI-----YVGEIVLALEHLHK--LGIIYRDIKLENILLDS--N 188
Cdd:cd14226  85 MF----RNHLCLVF----ELLSYnLYDLLRNTNfRGVSLnltrkFAQQLCTALLFLSTpeLSIIHCDLKPENILLCNpkR 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32528297 189 GHVVLTDFGLSKEFvadeTERAYSFCGTIEYMAPDIVRGGDsgHDKAVDWWSLGVLMYELLTG 251
Cdd:cd14226 157 SAIKIIDFGSSCQL----GQRIYQYIQSRFYRSPEVLLGLP--YDLAIDMWSLGCILVEMHTG 213
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
432-548 2.08e-05

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 46.57  E-value: 2.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ---KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd06658  30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRREllfNEVVIMRDYH-HENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 509 rIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd06658 109 -IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSD 147
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
430-546 2.17e-05

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 46.17  E-value: 2.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEAN-TQKEITALKlCE-------GHPNIVKLHEVFHD--QLHTFLVME 499
Cdd:cd06653   8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQeTSKEVNALE-CEiqllknlRHDRIVQYYGCLRDpeEKKLSIFVE 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06653  87 YMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIK 133
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
442-546 2.41e-05

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 45.80  E-value: 2.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 442 KCVHKKSNQAFAVKIiskrMEANTQKEITALKLCEG-HPNIVKLHEVFHDQLHTFLVMELlNGGELFERIKKKKHFSETE 520
Cdd:cd14022  11 RAVHLHSGEELVCKV----FDIGCYQESLAPCFCLPaHSNINQITEIILGETKAYVFFER-SYGDMHSFVRTCKKLREEE 85
                        90       100
                ....*....|....*....|....*.
gi 32528297 521 ASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd14022  86 AARLFYQIASAVAHCHDGGLVLRDLK 111
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
431-547 2.48e-05

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 46.57  E-value: 2.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 431 PLGEGSF-SICrKCVHKKSNQAFAVKIISKRMEA-----NTQKEITALKLCEgHPNIVKLHEVFH-----DQLHTFLVME 499
Cdd:cd07877  24 PVGSGAYgSVC-AAFDTKTGLRVAVKKLSRPFQSiihakRTYRELRLLKHMK-HENVIGLLDVFTparslEEFNDVYLVT 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 500 LLNGGELFERIKKKKhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07877 102 HLMGADLNNIVKCQK-LTDDHVQFLIYQILRGLKYIHSADIIHRDLKP 148
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
427-548 2.61e-05

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 46.15  E-value: 2.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd07873   5 IKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPctaiREVSLLKDLK-HANIVTLHDIIHTEKSLTLVFEYLD 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 503 ggelferiKKKKHFSETEASYI--------MRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07873  84 --------KDLKQYLDDCGNSInmhnvklfLFQLLRGLAYCHRRKVLHRDLKPQ 129
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
432-546 2.79e-05

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 46.13  E-value: 2.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ---KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd06659  29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRREllfNEVVIMRDYQ-HPNVVEMYKSYLVGEELWVLMEYLQGGALTD 107
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 32528297 509 rIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06659 108 -IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIK 144
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
424-545 2.93e-05

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 45.88  E-value: 2.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 424 DLDLKDKpLGEGSFSICRKCV-HKKSNQAFAVKIisKRMEANTQKEITALKLCEG-------HPNIVKLHEVFHDQlHTF 495
Cdd:cd05056   7 DITLGRC-IGEGQFGDVYQGVyMSPENEKIAVAV--KTCKNCTSPSVREKFLQEAyimrqfdHPHIVKLIGVITEN-PVW 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 32528297 496 LVMELLNGGELFERIKKKKHfSETEASYIM--RKLVSAVSHMHDVGVVHRDL 545
Cdd:cd05056  83 IVMELAPLGELRSYLQVNKY-SLDLASLILyaYQLSTALAYLESKRFVHRDI 133
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
443-546 3.20e-05

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 45.42  E-value: 3.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 443 CVHKKSNQAFAVKIISkrmeaNTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELlNGGELFERIKKKKHFSETEAS 522
Cdd:cd14023  14 QLHSGAELQCKVFPLK-----HYQDKIRPYIQLPSHRNITGIVEVILGDTKAYVFFEK-DFGDMHSYVRSCKRLREEEAA 87
                        90       100
                ....*....|....*....|....
gi 32528297 523 YIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd14023  88 RLFKQIVSAVAHCHQSAIVLGDLK 111
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
432-546 3.37e-05

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 45.60  E-value: 3.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKII------------SKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVME 499
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKQVelpsvsaenkdrKKSMLDALQREIALLRELQ-HENIVQYLGSSSDANHLNIFLE 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06628  87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIK 133
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
426-546 3.51e-05

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 45.52  E-value: 3.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 426 DLKDkpLGEGSFSICRKCVHKKSNQAFAVKIIS---KRMEANTQ---KEITALKLCEgHPNIVKLHEVFHDQLHTFLVME 499
Cdd:cd06607   5 DLRE--IGHGSFGAVYYARNKRTSEVVAIKKMSysgKQSTEKWQdiiKEVKFLRQLR-HPNTIEYKGCYLREHTAWLVME 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 500 --LLNGGELFERIKKKKHfsETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06607  82 ycLGSASDIVEVHKKPLQ--EVEIAAICHGALQGLAYLHSHNRIHRDVK 128
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
432-548 3.59e-05

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 45.72  E-value: 3.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK----EITALKLCEgHPNIVKLHEVfHDQLHTF-------LVMEL 500
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRErwclEIQIMKRLN-HPNVVAARDV-PEGLQKLapndlplLAMEY 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 501 LNGGELferikkKKHFSETEASYIMRK---------LVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14038  80 CQGGDL------RKYLNQFENCCGLREgailtllsdISSALRYLHENRIIHRDLKPE 130
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
431-547 3.60e-05

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 46.06  E-value: 3.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 431 PLGEGSFS-ICRKCVHKKSNQAFAVKIISKR--MEANTQKEITAL-KLCEGHPN----IVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd14135   7 YLGKGVFSnVVRARDLARGNQEVAIKIIRNNelMHKAGLKELEILkKLNDADPDdkkhCIRLLRHFEHKNHLCLVFESLS 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 503 GgELFERIKK--KKHFSETEA--SYIMRKLVsAVSHMHDVGVVHRDLKP 547
Cdd:cd14135  87 M-NLREVLKKygKNVGLNIKAvrSYAQQLFL-ALKHLKKCNILHADIKP 133
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
432-548 4.60e-05

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 45.54  E-value: 4.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRME-----ANTQKEITALKLCEgHPNIVKLHEV--------FHDqlhTFLVM 498
Cdd:cd07859   8 IGKGSYGVVCSAIDTHTGEKVAIKKINDVFEhvsdaTRILREIKLLRLLR-HPDIVEIKHImlppsrreFKD---IYVVF 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 499 ELLnGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07859  84 ELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPK 132
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
428-546 4.95e-05

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 45.07  E-value: 4.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIIS-------------KRMEANTQKEITALKLCEgHPNIVKL--HEVFHDQL 492
Cdd:cd06629   5 KGELIGKGTYGRVYLAMNATTGEMLAVKQVElpktssdradsrqKTVVDALKSEIDTLKDLD-HPNIVQYlgFEETEDYF 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 493 HTFLvmELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06629  84 SIFL--EYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLK 135
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
433-547 5.78e-05

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 45.35  E-value: 5.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 433 GEGSFSICRKCVHK--KSNQAFAVKII---SKRMEANTQ---KEITALKLCEgHPNIVKLHEVF--HDQLHTFLVME--- 499
Cdd:cd07842   9 GRGTYGRVYKAKRKngKDGKEYAIKKFkgdKEQYTGISQsacREIALLRELK-HENVVSLVEVFleHADKSVYLLFDyae 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 500 -----LLNggelFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd07842  88 hdlwqIIK----FHRQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKP 136
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
432-546 8.60e-05

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 44.79  E-value: 8.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKiiskRMEANTQKE---ITALKLCE-----GHPNIVKLHEVFHDQLHT--------- 494
Cdd:cd07864  15 IGEGTYGQVYKAKDKDTGELVALK----KVRLDNEKEgfpITAIREIKilrqlNHRSVVNLKEIVTDKQDAldfkkdkga 90
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 495 -FLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd07864  91 fYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIK 143
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
427-548 8.83e-05

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 44.55  E-value: 8.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKksNQAFAVKIISKRMEANTQKEI-TALKLC----EGHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd13980   3 LYDKSLGSTRFLKVARARHD--EGLVVVKVFVKPDPALPLRSYkQRLEEIrdrlLELPNVLPFQKVIETDKAAYLIRQYV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 502 nGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd13980  81 -KYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTE 126
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
432-548 9.06e-05

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 44.63  E-value: 9.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITAL---KLCEGHPN--IVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALnekQILEKVNSrfVVSLAYAYETKDALCLVLTLMNGGDL 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 507 FERIKK--KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05630  88 KFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPE 131
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
432-548 1.24e-04

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 44.04  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQKEITAlklCEG--HPNIVKLHEVFHDQLHTFLVMELLNGGELFER 509
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKV--RLEVFRAEELMA---CAGltSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQL 88
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32528297 510 IKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd13991  89 IKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKAD 127
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
432-548 1.37e-04

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 43.80  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISK-RME--------ANTQKEITALK-LCEGHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd14100   8 LGSGGFGSVYSGIRVADGAPVAIKHVEKdRVSewgelpngTRVPMEIVLLKkVGSGFRGVIRLLDWFERPDSFVLVLERP 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 502 NG-GELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14100  88 EPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDE 135
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
432-547 1.58e-04

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 43.57  E-value: 1.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITA-LKLC--EGH-PNIVKLHEVFHDQLHTFLVMELLNGG--E 505
Cdd:cd06617   9 LGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLLMdLDISmrSVDcPYTVTFYGALFREGDVWICMEVMDTSldK 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 506 LFERI-KKKKHFSETEASYIMRKLVSAVSHMHD-VGVVHRDLKP 547
Cdd:cd06617  89 FYKKVyDKGLTIPEDILGKIAVSIVKALEYLHSkLSVIHRDVKP 132
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
478-545 1.90e-04

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 43.46  E-value: 1.90e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 478 HPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKhfSETEASYIMRKLVSAVSHM---HDVGVVHRDL 545
Cdd:cd05085  52 HPNIVKLIGVCTQRQPIYIVMELVPGGDFLSFLRKKK--DELKTKQLVKFSLDAAAGMaylESKNCIHRDL 120
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
432-548 2.32e-04

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 43.47  E-value: 2.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ---KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd06657  28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRREllfNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 509 rIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd06657 107 -IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSD 145
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
428-548 2.45e-04

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 43.29  E-value: 2.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRME-----ANTQKEITALKLCEGHPNIVKLHEVFH----DQLHTFLVM 498
Cdd:cd07837   5 KLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEeegvpSTALREVSLLQMLSQSIYIVRLLDVEHveenGKPLLYLVF 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 499 ELLNGG-----ELFERIKKKKHFSETEASYiMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07837  85 EYLDTDlkkfiDSYGRGPHNPLPAKTIQSF-MYQLCKGVAHCHSHGVMHRDLKPQ 138
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
432-548 2.75e-04

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 43.04  E-value: 2.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITAL---KLCE--GHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd05632  10 LGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALnekQILEkvNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 32528297 507 FERIKKKKH--FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05632  90 KFHIYNMGNpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPE 133
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
431-547 4.35e-04

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 42.37  E-value: 4.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 431 PLGEGSFSICRKCVHKksNQAFAVKIISKR--MEANTQK---EITALKLceGHPNIV---KLHEVFHDQLHTFLVMELLN 502
Cdd:cd13979  10 PLGSGGFGSVYKATYK--GETVAVKIVRRRrkNRASRQSfwaELNAARL--RHENIVrvlAAETGTDFASLGLIIMEYCG 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 503 GGELFERI-KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd13979  86 NGTLQQLIyEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKP 131
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
431-548 5.03e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 42.52  E-value: 5.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297  431 PLGEGSFSICRKcVHKKSNQAFAVKIISKrmEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGgELFERI 510
Cdd:PHA03207 102 PGSEGEVFVCTK-HGDEQRKKVIVKAVTG--GKTPGREIDILKTIS-HRAIINLIHAYRWKSTVCMVMPKYKC-DLFTYV 176
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 32528297  511 KKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:PHA03207 177 DRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTE 214
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
432-547 6.32e-04

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 42.04  E-value: 6.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEIT----ALKLCEGhPNIVKLHEVFHDQLHTFLVMELLNGGELF 507
Cdd:cd06615   9 LGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAIRNQIIrelkVLHECNS-PYIVGFYGAFYSDGEISICMEHMDGGSLD 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32528297 508 ERIKKKKHFSETEASYIMRKLVSAVSHMHDV-GVVHRDLKP 547
Cdd:cd06615  88 QVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKP 128
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
468-548 6.73e-04

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 41.48  E-value: 6.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 468 EITAL-KLCEGHPNIVKLHEVFHDQLHTFLVMELLN-GGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd14102  52 EIVLLkKVGSGFRGVIKLLDWYERPDGFLIVMERPEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDI 131

                ...
gi 32528297 546 KPE 548
Cdd:cd14102 132 KDE 134
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
478-548 7.92e-04

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 41.33  E-value: 7.92e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 478 HPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMrKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd14027  50 HSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPE 119
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
427-547 9.02e-04

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 41.15  E-value: 9.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLG-----EGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITAlklCEGHPNIVKLHE--VFHDQLHTFlvME 499
Cdd:cd13995   2 LTYRNIGsdfipRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVEIQA---CFRHENIAELYGalLWEETVHLF--ME 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32528297 500 LLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKP 547
Cdd:cd13995  77 AGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKP 124
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
420-548 1.07e-03

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 41.13  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 420 YQHYdldlkdKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITAL---KLCEGHPN--IVKLHEVFHDQLHT 494
Cdd:cd05631   2 FRHY------RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALnekRILEKVNSrfVVSLAYAYETKDAL 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32528297 495 FLVMELLNGGELFERIKKKKH--FSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05631  76 CLVLTIMNGGDLKFHIYNMGNpgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPE 131
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
458-548 1.11e-03

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 40.81  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 458 SKRMEANTQKEITALKLCEgHPNIVKLHEV------FHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSA 531
Cdd:cd14012  38 GKKQIQLLEKELESLKKLR-HPNLVSYLAFsierrgRSDGWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEA 116
                        90
                ....*....|....*..
gi 32528297 532 VSHMHDVGVVHRDLKPE 548
Cdd:cd14012 117 LEYLHRNGVVHKSLHAG 133
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
432-545 1.24e-03

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 40.89  E-value: 1.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK----EITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELF 507
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRkflqEARILKQYD-HPNIVKLIGVCVQKQPIMIVMELVPGGSLL 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 508 ERIKKKK---------HFSEtEASYIMRKLVSAvshmhdvGVVHRDL 545
Cdd:cd05041  82 TFLRKKGarltvkqllQMCL-DAAAGMEYLESK-------NCIHRDL 120
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
432-548 1.31e-03

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 40.90  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISK-----RMEANTQKEITALKLcEGHPNIVKLHEVFHDQLHTFLVMELLNGGEL 506
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSspnciEERKALLKEAEKMER-ARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 507 FERIKKKKHFSETEASY-IMRKLVSAVSHMH--DVGVVHRDLKPE 548
Cdd:cd13978  80 KSLLEREIQDVPWSLRFrIIHEIALGMNFLHnmDPPLLHHDLKPE 124
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
478-548 1.38e-03

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 40.68  E-value: 1.38e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32528297 478 HPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKhFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd06647  63 NPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSD 132
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
430-545 1.44e-03

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 40.72  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVH--KKSNQAFAVKIIskRMEANTQ-------KEITALKLCEgHPNIVKLHEVFHDQlHTFLVMEL 500
Cdd:cd05116   1 GELGSGNFGTVKKGYYqmKKVVKTVAVKIL--KNEANDPalkdellREANVMQQLD-NPYIVRMIGICEAE-SWMLVMEM 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32528297 501 LNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd05116  77 AELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDL 121
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
415-546 1.61e-03

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 40.78  E-value: 1.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 415 KDSPFYQHYDLdlkdKPLGEGSFSICRKCVHKKSNQAFAVKIIS---KRMEANTQKEITALKLCEG--HPNIVKLHEVFH 489
Cdd:cd06634  10 KDDPEKLFSDL----REIGHGSFGAVYFARDVRNNEVVAIKKMSysgKQSNEKWQDIIKEVKFLQKlrHPNTIEYRGCYL 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 490 DQLHTFLVME--LLNGGELFEriKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06634  86 REHTAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVK 142
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
478-545 1.78e-03

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 40.23  E-value: 1.78e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 478 HPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKK-HFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd05066  64 HPNIIHLEGVVTRSKPVMIVTEYMENGSLDAFLRKHDgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDL 132
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
432-547 1.81e-03

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 40.60  E-value: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIIskRMEANTQK------EITALKLCEGhPNIVKLHEVFHDQLHTFLVMELLNGGE 505
Cdd:cd06622   9 LGKGNYGSVYKVLHRPTGVTMAMKEI--RLELDESKfnqiimELDILHKAVS-PYIVDFYGAFFIEGAVYMCMEYMDAGS 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 32528297 506 LfERIKKKKHFSETEASYIMRKLVSAVSH-----MHDVGVVHRDLKP 547
Cdd:cd06622  86 L-DKLYAGGVATEGIPEDVLRRITYAVVKglkflKEEHNIIHRDVKP 131
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
427-548 1.91e-03

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 40.36  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 427 LKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ----KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLN 502
Cdd:cd07872   9 IKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPctaiREVSLLKDLK-HANIVTLHDIVHTDKSLTLVFEYLD 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 32528297 503 ggelferiKKKKHF--------SETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd07872  88 --------KDLKQYmddcgnimSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQ 133
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
432-546 1.91e-03

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 40.29  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFsicrKCVHKKSNQAFAVKI------ISKRMEANTQK---EITALKLCEgHPNIVKLHEVFHDQLHTFLVM--EL 500
Cdd:cd13983   9 LGRGSF----KTVYRAFDTEEGIEVawneikLRKLPKAERQRfkqEIEILKSLK-HPNIIKFYDSWESKSKKEVIFitEL 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 32528297 501 LNGGELFERIKKKKHFSE----TEASYIMRKLVSAvsHMHDVGVVHRDLK 546
Cdd:cd13983  84 MTSGTLKQYLKRFKRLKLkvikSWCRQILEGLNYL--HTRDPPIIHRDLK 131
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
478-545 2.36e-03

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 40.09  E-value: 2.36e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 478 HPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVS-------AVSHMHDVGVVHRDL 545
Cdd:cd05044  58 HPNILKLLGVCLDNDPQYIILELMEGGDLLSYLRAARPTAFTPPLLTLKDLLSicvdvakGCVYLEDMHFVHRDL 132
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
429-545 2.86e-03

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 39.63  E-value: 2.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSFSICRKCVHK--KSNQAF---AVKIISKR----------MEANTQKEITAlklceghPNIVKLHEVFHDQLH 493
Cdd:cd05032  11 IRELGQGSFGMVYEGLAKgvVKGEPEtrvAIKTVNENasmrerieflNEASVMKEFNC-------HHVVRLLGVVSTGQP 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32528297 494 TFLVMELLNGGELfeRIKKKKHFSETE---------ASYIMR---KLVSAVSHMHDVGVVHRDL 545
Cdd:cd05032  84 TLVVMELMAKGDL--KSYLRSRRPEAEnnpglgpptLQKFIQmaaEIADGMAYLAAKKFVHRDL 145
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
496-548 3.88e-03

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 39.26  E-value: 3.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32528297 496 LVMELLNGGELFERIKK--KKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd05605  77 LVLTIMNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPE 131
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
467-547 3.90e-03

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 39.53  E-value: 3.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 467 KEITALKLCEGHPNIVKLHEVF--HDQLHT---FLVMELLN--GGELFERIKKKKHfSETEASYIMRKLVSAVSHMHDVG 539
Cdd:cd14020  52 KERAALEQLQGHRNIVTLYGVFtnHYSANVpsrCLLLELLDvsVSELLLRSSNQGC-SMWMIQHCARDVLEALAFLHHEG 130

                ....*...
gi 32528297 540 VVHRDLKP 547
Cdd:cd14020 131 YVHADLKP 138
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
407-546 4.17e-03

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 39.65  E-value: 4.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 407 NVARSAMMKDSPFYqhyDLDLKDKP---------LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQK------EITA 471
Cdd:cd06635   2 STSRAGSLKDPDIA---ELFFKEDPeklfsdlreIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwqdiikEVKF 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32528297 472 LKLCEgHPNIVKLHEVFHDQLHTFLVME--LLNGGELFEriKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd06635  79 LQRIK-HPNSIEYKGCYLREHTAWLVMEycLGSASDLLE--VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIK 152
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
432-548 4.20e-03

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 39.32  E-value: 4.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 432 LGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQ---KEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELLNGGELFE 508
Cdd:cd06655  27 IGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKEliiNEILVMKELK-NPNIVNFLDSFLVGDELFVVMEYLAGGSLTD 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32528297 509 rIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPE 548
Cdd:cd06655 106 -VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSD 144
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
429-545 4.50e-03

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 39.28  E-value: 4.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 429 DKPLGEGSF-SICRKCVHKKSNQAFAVKI------ISKRMEANTQKEITALKLCEgHPNIVKLHEVFHDQLHTFLVMELL 501
Cdd:cd05033   9 EKVIGGGEFgEVCSGSLKLPGKKEIDVAIktlksgYSDKQRLDFLTEASIMGQFD-HPNVIRLEGVVTKSRPVMIVTEYM 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 32528297 502 NGGEL--FERiKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDL 545
Cdd:cd05033  88 ENGSLdkFLR-ENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDL 132
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
512-546 4.71e-03

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 39.31  E-value: 4.71e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 32528297 512 KKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLK 546
Cdd:cd13974 125 REKRLSEREALVIFYDVVRVVEALHKKNIVHRDLK 159
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
148-255 5.20e-03

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 39.01  E-value: 5.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 148 RFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNG-------HVVltDFGLSKEFVADETER------AYSFC 214
Cdd:cd14127  92 KFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGRPGtknanviHVV--DFGMAKQYRDPKTKQhipyreKKSLS 169
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 32528297 215 GTIEYMAPDIVRGGD-SGHDkavDWWSLG-VLMYeLLTGASPF 255
Cdd:cd14127 170 GTARYMSINTHLGREqSRRD---DLEALGhVFMY-FLRGSLPW 208
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
430-545 6.41e-03

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 38.90  E-value: 6.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 430 KPLGEGSFSICRKCVHK----KSNQAFAVKIISKRMEANT----QKEITALKLCEgHPNIVKLHEVFHDQ--LHTFLVME 499
Cdd:cd05038  10 KQLGEGHFGSVELCRYDplgdNTGEQVAVKSLQPSGEEQHmsdfKREIEILRTLD-HEYIVKYKGVCESPgrRSLRLIME 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32528297 500 LLNGGELFERIKKKKHFSETeasyimRKLVSAVS-------HMHDVGVVHRDL 545
Cdd:cd05038  89 YLPSGSLRDYLQRHRDQIDL------KRLLLFASqickgmeYLGSQRYIHRDL 135
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
428-545 6.73e-03

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 38.55  E-value: 6.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32528297 428 KDKPLGEGSFSICRKCVHKKSNQ----AFAVKIISKRMEANTQKEIT---ALKLCEGHPNIVKLHEVFHDQLHTfLVMEL 500
Cdd:cd05057  11 KGKVLGSGAFGTVYKGVWIPEGEkvkiPVAIKVLREETGPKANEEILdeaYVMASVDHPHLVRLLGICLSSQVQ-LITQL 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 32528297 501 LNGGELFERIKKKKhfsETEASYIM----RKLVSAVSHMHDVGVVHRDL 545
Cdd:cd05057  90 MPLGCLLDYVRNHR---DNIGSQLLlnwcVQIAKGMSYLEEKRLVHRDL 135
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
478-545 8.44e-03

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 38.20  E-value: 8.44e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32528297 478 HPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLV-SAVSHMHDVGVVHRDL 545
Cdd:cd05059  58 HPKLVQLYGVCTKQRPIFIVTEYMANGCLLNYLRERRGKFQTEQLLEMCKDVcEAMEYLESNGFIHRDL 126
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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