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Conserved domains on  [gi|21359873|ref|NP_005021|]
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serine/threonine-protein kinase PLK1 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase PLK1( domain architecture ID 10197709)

serine/threonine-protein kinase PLK1 (Polo-like kinase 1) 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_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
45-309 0e+00

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: 552.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  45 VDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDND 124
Cdd:cd14187   1 VDPRTRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDND 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 FVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD 204
Cdd:cd14187  81 FVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQK 284
Cdd:cd14187 161 GERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQK 240
                       250       260
                ....*....|....*....|....*
gi 21359873 285 MLQTDPTARPTINELLNDEFFTSGY 309
Cdd:cd14187 241 MLQTDPTARPTINELLNDEFFTSGY 265
POLO_box_1 cd13118
First polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like Ser ...
407-494 1.15e-46

First polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.


:

Pssm-ID: 240561  Cd Length: 91  Bit Score: 159.02  E-value: 1.15e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 407 PIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVS--SHPNSLMKKITLLKYFRN 484
Cdd:cd13118   1 PPVWVSKWVDYSNKYGLGYQLSDGSVGVLFNDSTKMVLSPDGKHVQYIERNGEESELTRSddSYPPDLAKKVTLLKYFRN 80
                        90
                ....*....|
gi 21359873 485 YMSEHLLKAG 494
Cdd:cd13118  81 YMEEHLSKGG 90
POLO_box_2 cd13117
Second polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like ...
509-590 3.42e-38

Second polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.


:

Pssm-ID: 240560  Cd Length: 81  Bit Score: 135.40  E-value: 3.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 509 PYLRTWFRTRSAIILHLSNGSVQINFFqDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVD 588
Cdd:cd13117   1 PFVKKWLRTKSAIVFRLSNGTVQVNFF-DHTKIILSPLGKLVTYIDKKRESRTYPLSELLKSGCSSELAKRLKYAKEILK 79

                ..
gi 21359873 589 KL 590
Cdd:cd13117  80 EL 81
 
Name Accession Description Interval E-value
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
45-309 0e+00

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: 552.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  45 VDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDND 124
Cdd:cd14187   1 VDPRTRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDND 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 FVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD 204
Cdd:cd14187  81 FVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQK 284
Cdd:cd14187 161 GERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQK 240
                       250       260
                ....*....|....*....|....*
gi 21359873 285 MLQTDPTARPTINELLNDEFFTSGY 309
Cdd:cd14187 241 MLQTDPTARPTINELLNDEFFTSGY 265
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
58-305 8.88e-96

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 293.67  E-value: 8.88e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873     58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:smart00220   6 KLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNY 217
Cdd:smart00220  84 LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLD-PGEKLTTFVGTPEY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSC-LKETYLRIKKNEYSIPKH---INPVAASLIQKMLQTDPTAR 293
Cdd:smart00220 163 MAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVKDPEKR 242
                          250
                   ....*....|..
gi 21359873    294 PTINELLNDEFF 305
Cdd:smart00220 243 LTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
59-305 1.80e-57

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 192.46  E-value: 1.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:pfam00069   7 LGSGSFGTVYKAKHRDTGKIVAIKKIKKEKI-KKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   139 LELHKRRKALTEPEARYYLRQIVLGcqylhrnrvihrdlklgnlflnedlevkigdfgLATKVEYDgerkkTLCGTPNYI 218
Cdd:pfam00069  86 FDLLSEKGAFSEREAKFIMKQILEG---------------------------------LESGSSLT-----TFVGTPWYM 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSI---PKHINPVAASLIQKMLQTDPTARPT 295
Cdd:pfam00069 128 APEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFpelPSNLSEEAKDLLKKLLKKDPSKRLT 207
                         250
                  ....*....|
gi 21359873   296 INELLNDEFF 305
Cdd:pfam00069 208 ATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
59-302 3.72e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 186.37  E-value: 3.72e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:COG0515  15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKT--LCGTPN 216
Cdd:COG0515  95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALG-GATLTQTgtVVGTPG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINP-VAASL---IQKMLQTDPTA 292
Cdd:COG0515 174 YMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPdLPPALdaiVLRALAKDPEE 253
                       250
                ....*....|.
gi 21359873 293 RP-TINELLND 302
Cdd:COG0515 254 RYqSAAELAAA 264
POLO_box_1 cd13118
First polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like Ser ...
407-494 1.15e-46

First polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.


Pssm-ID: 240561  Cd Length: 91  Bit Score: 159.02  E-value: 1.15e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 407 PIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVS--SHPNSLMKKITLLKYFRN 484
Cdd:cd13118   1 PPVWVSKWVDYSNKYGLGYQLSDGSVGVLFNDSTKMVLSPDGKHVQYIERNGEESELTRSddSYPPDLAKKVTLLKYFRN 80
                        90
                ....*....|
gi 21359873 485 YMSEHLLKAG 494
Cdd:cd13118  81 YMEEHLSKGG 90
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
59-293 1.03e-42

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 156.13  E-value: 1.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  139 LElhKRRKALTEPE--ARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydgERKKTLCGTPN 216
Cdd:PTZ00263 106 FT--HLRKAGRFPNdvAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP---DRTFTLCGTPE 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873  217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:PTZ00263 181 YLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHTKR 257
POLO_box_2 cd13117
Second polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like ...
509-590 3.42e-38

Second polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.


Pssm-ID: 240560  Cd Length: 81  Bit Score: 135.40  E-value: 3.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 509 PYLRTWFRTRSAIILHLSNGSVQINFFqDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVD 588
Cdd:cd13117   1 PFVKKWLRTKSAIVFRLSNGTVQVNFF-DHTKIILSPLGKLVTYIDKKRESRTYPLSELLKSGCSSELAKRLKYAKEILK 79

                ..
gi 21359873 589 KL 590
Cdd:cd13117  80 EL 81
POLO_box pfam00659
POLO box duplicated region;
517-580 4.71e-21

POLO box duplicated region;


Pssm-ID: 459894  Cd Length: 61  Bit Score: 86.79  E-value: 4.71e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21359873   517 TRSAIILHLSNGSVQINFfQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLeeYGCCKELASRL 580
Cdd:pfam00659   1 TKYGIGYQLSNGTVQVNF-NDHTKIILSPDGKAVTYIDKEGERRTYTLSTL--SGCPEDLKKKL 61
POLO_box pfam00659
POLO box duplicated region;
419-476 2.31e-20

POLO box duplicated region;


Pssm-ID: 459894  Cd Length: 61  Bit Score: 84.86  E-value: 2.31e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21359873   419 DKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVS---SHPNSLMKKI 476
Cdd:pfam00659   1 TKYGIGYQLSNGTVQVNFNDHTKIILSPDGKAVTYIDKEGERRTYTLStlsGCPEDLKKKL 61
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
107-302 1.56e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 89.08  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  107 SLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE 186
Cdd:NF033483  63 SLSHPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITK 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  187 DLEVKIGDFGLA-----TKVEYDGerkkTLCGTPNYIAPE-----VLSKKghsfeVDVWSIGCIMYTLLVGKPPF--ETS 254
Cdd:NF033483 143 DGRVKVTDFGIAralssTTMTQTN----SVLGTVHYLSPEqarggTVDAR-----SDIYSLGIVLYEMLTGRPPFdgDSP 213
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21359873  255 clketylrikkneYSI-----------PKHINP-VAASL---IQKMLQTDPTARP-TINELLND 302
Cdd:NF033483 214 -------------VSVaykhvqedpppPSELNPgIPQSLdavVLKATAKDPDDRYqSAAEMRAD 264
 
Name Accession Description Interval E-value
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
45-309 0e+00

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: 552.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  45 VDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDND 124
Cdd:cd14187   1 VDPRTRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDND 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 FVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD 204
Cdd:cd14187  81 FVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQK 284
Cdd:cd14187 161 GERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQK 240
                       250       260
                ....*....|....*....|....*
gi 21359873 285 MLQTDPTARPTINELLNDEFFTSGY 309
Cdd:cd14187 241 MLQTDPTARPTINELLNDEFFTSGY 265
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
58-305 4.47e-169

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: 480.90  E-value: 4.47e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14099   8 FLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNGS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd14099  88 LMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGTPNY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKK-GHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKH--INPVAASLIQKMLQTDPTARP 294
Cdd:cd14099 168 IAPEVLEKKkGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHlsISDEAKDLIRSMLQPDPTKRP 247
                       250
                ....*....|.
gi 21359873 295 TINELLNDEFF 305
Cdd:cd14099 248 SLDEILSHPFF 258
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
58-305 6.24e-108

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: 324.96  E-value: 6.24e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14189   8 LLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd14189  88 LAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICGTPNY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd14189 168 LAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLTLD 247

                ....*...
gi 21359873 298 ELLNDEFF 305
Cdd:cd14189 248 QILEHEFF 255
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
59-305 1.18e-105

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: 319.26  E-value: 1.18e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14188   9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd14188  89 AHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGTPNYL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINE 298
Cdd:cd14188 169 SPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPEDRPSLDE 248

                ....*..
gi 21359873 299 LLNDEFF 305
Cdd:cd14188 249 IIRHDFF 255
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
58-305 8.88e-96

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 293.67  E-value: 8.88e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873     58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:smart00220   6 KLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNY 217
Cdd:smart00220  84 LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLD-PGEKLTTFVGTPEY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSC-LKETYLRIKKNEYSIPKH---INPVAASLIQKMLQTDPTAR 293
Cdd:smart00220 163 MAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLLVKDPEKR 242
                          250
                   ....*....|..
gi 21359873    294 PTINELLNDEFF 305
Cdd:smart00220 243 LTAEEALQHPFF 254
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
59-304 7.94e-87

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: 270.50  E-value: 7.94e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05117   8 LGRGSFGVVRLAVHKKTGEEYAVKIIDKKKL-KSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTGGEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd05117  87 FDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFE-EGEKLKTVCGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTDPT 291
Cdd:cd05117 166 YYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDspewKNVSEEAKDLIKRLLVVDPK 245
                       250
                ....*....|...
gi 21359873 292 ARPTINELLNDEF 304
Cdd:cd05117 246 KRLTAAEALNHPW 258
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
59-304 1.50e-86

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: 269.39  E-value: 1.50e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14003   8 LGEGSFGKVKLARHKLTGEKVAIKIIDKSKL-KEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNYI 218
Cdd:cd14003  87 FDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFR-GGSLLKTFCGTPAYA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKG-HSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd14003 166 APEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSKRITIE 245

                ....*..
gi 21359873 298 ELLNDEF 304
Cdd:cd14003 246 EILNHPW 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
58-306 4.68e-80

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: 252.78  E-value: 4.68e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14007   7 PLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNGE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtkVEYDGERKKTLCGTPNY 217
Cdd:cd14007  87 LYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWS--VHAPSNRRKTFCGTLDY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd14007 165 LPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDPSKRLSLE 244

                ....*....
gi 21359873 298 ELLNDEFFT 306
Cdd:cd14007 245 QVLNHPWIK 253
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
59-305 3.12e-72

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: 232.41  E-value: 3.12e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd05123  81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTPEYL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPT--- 295
Cdd:cd05123 161 APEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGsgg 240
                       250
                ....*....|
gi 21359873 296 INELLNDEFF 305
Cdd:cd05123 241 AEEIKAHPFF 250
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
58-305 4.84e-70

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: 227.02  E-value: 4.84e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAgkiVpKSLLLKPHQREKMS---MEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd06606   7 LLGKGSFGSVYLALNLDTGELMA---V-KEVELSGDSEEELEaleREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE--YDGERKKTLC 212
Cdd:cd06606  83 GGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAeiATGEGTKSLR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 213 GTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFetSCLKETY---LRIKKNEYS--IPKHINPVAASLIQKMLQ 287
Cdd:cd06606 163 GTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPW--SELGNPVaalFKIGSSGEPppIPEHLSEEAKDFLRKCLQ 240
                       250
                ....*....|....*...
gi 21359873 288 TDPTARPTINELLNDEFF 305
Cdd:cd06606 241 RDPKKRPTADELLQHPFL 258
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
58-304 3.15e-68

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: 222.04  E-value: 3.15e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14186   8 LLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd14186  88 MSRyLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFTMCGTPN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTI 296
Cdd:cd14186 168 YISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKNPADRLSL 247

                ....*...
gi 21359873 297 NELLNDEF 304
Cdd:cd14186 248 SSVLDHPF 255
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
59-303 2.89e-67

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: 217.91  E-value: 2.89e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKK--LLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKA-LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN- 216
Cdd:cd00180  79 KDLLKENKGpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPp 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 -YIAPEVLSKKGHSFEVDVWSIGCIMYTLlvgkppfetsclketylrikkneysipkhinPVAASLIQKMLQTDPTARPT 295
Cdd:cd00180 159 yYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKRPS 207

                ....*...
gi 21359873 296 INELLNDE 303
Cdd:cd00180 208 AKELLEHL 215
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
59-305 2.96e-63

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: 208.86  E-value: 2.96e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd08215   8 IGKGSFGSAYLVRRKSDGKLYVLKEIDLSNM-SEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGGDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKA----LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd08215  87 AQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLAKTVVGT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd08215 167 PYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVNSMLQKDPEKR 246
                       250
                ....*....|..
gi 21359873 294 PTINELLNDEFF 305
Cdd:cd08215 247 PSANEILSSPFI 258
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
59-305 1.98e-62

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: 206.74  E-value: 1.98e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14079  10 LGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGGEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATkVEYDGERKKTLCGTPNYI 218
Cdd:cd14079  90 FDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSN-IMRDGEFLKTSCGSPNYA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSkkGHSF---EVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPT 295
Cdd:cd14079 169 APEVIS--GKLYagpEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLKRIT 246
                       250
                ....*....|
gi 21359873 296 INELLNDEFF 305
Cdd:cd14079 247 IPEIRQHPWF 256
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
59-305 7.87e-62

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: 205.13  E-value: 7.87e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPkslLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05122   8 IGKGGFGVVYKARHKKTGQIVAIKKIN---LESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSGGSL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNY 217
Cdd:cd05122  85 KDlLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLS-DGKTRNTFVGTPYW 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEysIPKHINPVAASL-----IQKMLQTDPTA 292
Cdd:cd05122 164 MAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNG--PPGLRNPKKWSKefkdfLKKCLQKDPEK 241
                       250
                ....*....|...
gi 21359873 293 RPTINELLNDEFF 305
Cdd:cd05122 242 RPTAEQLLKHPFI 254
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
59-305 1.87e-60

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: 202.01  E-value: 1.87e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSM-----------EISIHRSLAHQHVVGFHGFFED--NDF 125
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREGKNDRGkiknalddvrrEIAIMKKLDHPNIVRLYEVIDDpeSDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 126 VFVVLELCRRRSLLELH--KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEY 203
Cdd:cd14008  81 LYLVLEYCEGGPVMELDsgDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFED 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 204 DGERKKTLCGTPNYIAPEVLSKKG---HSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKK--NEYSIPKHINPVA 278
Cdd:cd14008 161 GNDTLQKTAGTPAFLAPELCDGDSktySGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNqnDEFPIPPELSPEL 240
                       250       260
                ....*....|....*....|....*..
gi 21359873 279 ASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14008 241 KDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
59-305 2.52e-59

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: 199.36  E-value: 2.52e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05581   9 LGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAPNGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA-----------------TKV 201
Cdd:cd05581  89 LEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAkvlgpdsspestkgdadSQI 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 202 EYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASL 281
Cdd:cd05581 169 AYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPENFPPDAKDL 248
                       250       260       270
                ....*....|....*....|....*....|
gi 21359873 282 IQKMLQTDPTARPTIN------ELLNDEFF 305
Cdd:cd05581 249 IQKLLVLDPSKRLGVNenggydELKAHPFF 278
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
59-305 3.39e-58

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: 195.55  E-value: 3.39e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14081   9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATkVEYDGERKKTLCGTPNYI 218
Cdd:cd14081  89 FDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS-LQPEGSLLETSCGSPHYA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKG-HSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd14081 168 CPEVIKGEKyDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPEKRITIE 247

                ....*...
gi 21359873 298 ELLNDEFF 305
Cdd:cd14081 248 EIKKHPWF 255
Pkinase pfam00069
Protein kinase domain;
59-305 1.80e-57

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 192.46  E-value: 1.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:pfam00069   7 LGSGSFGTVYKAKHRDTGKIVAIKKIKKEKI-KKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   139 LELHKRRKALTEPEARYYLRQIVLGcqylhrnrvihrdlklgnlflnedlevkigdfgLATKVEYDgerkkTLCGTPNYI 218
Cdd:pfam00069  86 FDLLSEKGAFSEREAKFIMKQILEG---------------------------------LESGSSLT-----TFVGTPWYM 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSI---PKHINPVAASLIQKMLQTDPTARPT 295
Cdd:pfam00069 128 APEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFpelPSNLSEEAKDLLKKLLKKDPSKRLT 207
                         250
                  ....*....|
gi 21359873   296 INELLNDEFF 305
Cdd:pfam00069 208 ATQALQHPWF 217
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
58-304 6.65e-56

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: 189.54  E-value: 6.65e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14663   7 TLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGGE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEY--DGERKKTLCGTP 215
Cdd:cd14663  87 LFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQfrQDGLLHTTCGTP 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGH-SFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARP 294
Cdd:cd14663 167 NYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDPNPSTRI 246
                       250
                ....*....|
gi 21359873 295 TINELLNDEF 304
Cdd:cd14663 247 TVEQIMASPW 256
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
59-305 1.13e-55

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: 188.93  E-value: 1.13e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEI--SDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd14080   8 IGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAEHG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERK--KTLCGT 214
Cdd:cd14080  88 DLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDVlsKTFCGS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLskKG---HSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP---KHINPVAASLIQKMLQT 288
Cdd:cd14080 168 AAYAAPEIL--QGipyDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPssvKKLSPECKDLIDQLLEP 245
                       250
                ....*....|....*..
gi 21359873 289 DPTARPTINELLNDEFF 305
Cdd:cd14080 246 DPTKRATIEEILNHPWL 262
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
59-305 1.68e-55

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: 188.20  E-value: 1.68e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06627   8 IGRGAFGSVYKGLNLNTGEFVAIKQI-SLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd06627  87 ASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSVVGTPYWM 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF----ETSCLketyLRIKKNEYS-IPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd06627 167 APEVIEMSGVTTASDIWSVGCTVIELLTGNPPYydlqPMAAL----FRIVQDDHPpLPENISPELRDFLLQCFQKDPTLR 242
                       250
                ....*....|..
gi 21359873 294 PTINELLNDEFF 305
Cdd:cd06627 243 PSAKELLKHPWL 254
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
59-309 3.20e-55

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: 187.43  E-value: 3.20e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQrEKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQ-ENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKVEYDGErKKTLCGTP 215
Cdd:cd14009  80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARSLQPASM-AETLCGSP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNE----YSIPKHINPVAASLIQKMLQTDPT 291
Cdd:cd14009 159 LYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDavipFPIAAQLSPDCKDLLRRLLRRDPA 238
                       250
                ....*....|....*...
gi 21359873 292 ARPTInellnDEFFTSGY 309
Cdd:cd14009 239 ERISF-----EEFFAHPF 251
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
59-302 8.79e-55

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: 186.64  E-value: 8.79e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14014   8 LGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE-RKKTLCGTPNY 217
Cdd:cd14014  88 ADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLtQTGSVLGTPAY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVA----ASLIQKMLQTDPTAR 293
Cdd:cd14014 168 MAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVppalDAIILRALAKDPEER 247
                       250
                ....*....|
gi 21359873 294 P-TINELLND 302
Cdd:cd14014 248 PqSAAELLAA 257
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
59-301 1.68e-54

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: 186.44  E-value: 1.68e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQRE-----KMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd14084  14 LGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREinkprNIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLELM 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLAtKVEYDGERKKT 210
Cdd:cd14084  94 EGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLS-KILGETSLMKT 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVL---SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYL-RIKKNEYS-IP---KHINPVAASLI 282
Cdd:cd14084 173 LCGTPTYLAPEVLrsfGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKeQILSGKYTfIPkawKNVSEEAKDLV 252
                       250
                ....*....|....*....
gi 21359873 283 QKMLQTDPTARPTINELLN 301
Cdd:cd14084 253 KKMLVVDPSRRPSIEEALE 271
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
74-305 3.57e-53

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: 182.94  E-value: 3.57e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  74 DTKEVFAGKIV-----PKSLLLKPHQREKMSMEISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKA 147
Cdd:cd14093  26 ETGQEFAVKIIditgeKSSENEAEELREATRREIEILRQVSgHPNIIELHDVFESPTFIFLVFELCRKGELFDYLTEVVT 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 148 LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNYIAPEVL---- 223
Cdd:cd14093 106 LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLD-EGEKLRELCGTPGYLAPEVLkcsm 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 224 --SKKGHSFEVDVWSIGCIMYTLLVGKPPF----ETSCLKetylRIKKNEYSIPK----HINPVAASLIQKMLQTDPTAR 293
Cdd:cd14093 185 ydNAPGYGKEVDMWACGVIMYTLLAGCPPFwhrkQMVMLR----NIMEGKYEFGSpewdDISDTAKDLISKLLVVDPKKR 260
                       250
                ....*....|..
gi 21359873 294 PTINELLNDEFF 305
Cdd:cd14093 261 LTAEEALEHPFF 272
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
59-305 4.23e-53

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: 183.16  E-value: 4.23e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05580   9 LGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydgERKKTLCGTPNYI 218
Cdd:cd05580  89 FSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK---DRTYTLCGTPEYL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR----- 293
Cdd:cd05580 166 APEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVDLTKRlgnlk 245
                       250
                ....*....|..
gi 21359873 294 PTINELLNDEFF 305
Cdd:cd05580 246 NGVEDIKNHPWF 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
59-302 3.72e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 186.37  E-value: 3.72e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:COG0515  15 LGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKT--LCGTPN 216
Cdd:COG0515  95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALG-GATLTQTgtVVGTPG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINP-VAASL---IQKMLQTDPTA 292
Cdd:COG0515 174 YMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPdLPPALdaiVLRALAKDPEE 253
                       250
                ....*....|.
gi 21359873 293 RP-TINELLND 302
Cdd:COG0515 254 RYqSAAELAAA 264
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
59-293 3.93e-52

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: 179.73  E-value: 3.93e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeYDGERKKTLCGTPNYI 218
Cdd:cd05572  81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKL-GSGRKTWTFCGTPEYV 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK--ETYLRIKKNEYSI--PKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05572 160 APEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGIDKIefPKYIDKNAKNLIKQLLRRNPEER 238
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
59-303 1.32e-50

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: 175.59  E-value: 1.32e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKM-SMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14095   8 IGDGNFAVVKECRDKATDKEYALKIIDKA---KCKGKEHMiENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKGGD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED----LEVKIGDFGLATKVEydgERKKTLCG 213
Cdd:cd14095  85 LFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHedgsKSLKLADFGLATEVK---EPLFTVCG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYL--RIKKNEYSIPK----HINPVAASLIQKMLQ 287
Cdd:cd14095 162 TPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQEELfdLILAGEFEFLSpywdNISDSAKDLISRMLV 241
                       250
                ....*....|....*.
gi 21359873 288 TDPTARPTINELLNDE 303
Cdd:cd14095 242 VDPEKRYSAGQVLDHP 257
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
61-306 1.40e-50

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: 175.87  E-value: 1.40e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  61 KGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLE 140
Cdd:cd05579   3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 141 LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGL--------------ATKVEYDGE 206
Cdd:cd05579  83 LLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLskvglvrrqiklsiQKKSNGAPE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 RK-KTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK--HINPVAASLIQ 283
Cdd:cd05579 163 KEdRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEdpEVSDEAKDLIS 242
                       250       260
                ....*....|....*....|....*.
gi 21359873 284 KMLQTDPTARP---TINELLNDEFFT 306
Cdd:cd05579 243 KLLTPDPEKRLgakGIEEIKNHPFFK 268
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
59-302 1.40e-50

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: 175.27  E-value: 1.40e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14073   9 LGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNYI 218
Cdd:cd14073  89 YDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYS-KDKLLQTFCGSPLYA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLskKGHSF---EVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINpVAASLIQKMLQTDPTARPT 295
Cdd:cd14073 168 SPEIV--NGTPYqgpEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPS-DASGLIRWMLTVNPKRRAT 244

                ....*..
gi 21359873 296 INELLND 302
Cdd:cd14073 245 IEDIANH 251
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
59-301 1.52e-50

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: 175.26  E-value: 1.52e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlkPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14078  11 IGSGGFAKVKLATHILTGEKVAIKIMDKKAL--GDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDG--ERKKTLCGTPN 216
Cdd:cd14078  89 FDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPK-GGmdHHLETCCGSPA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGH-SFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPT 295
Cdd:cd14078 168 YAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKRIT 247

                ....*.
gi 21359873 296 INELLN 301
Cdd:cd14078 248 VKELLN 253
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
59-305 1.75e-50

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: 175.21  E-value: 1.75e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKslllKPHQ---REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14069   9 LGEGAFGEVFLAVNRNTEEAVAVKFVDM----KRAPgdcPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDG-ERKKT-LCG 213
Cdd:cd14069  85 GELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGkERLLNkMCG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFE-VDVWSIGCIMYTLLVGKPPFE---TSCLK-ETYLRIKKNEYSIPKHINPVAASLIQKMLQT 288
Cdd:cd14069 165 TLPYVAPELLAKKKYRAEpVDVWSCGIVLFAMLAGELPWDqpsDSCQEySDWKENKKTYLTPWKKIDTAALSLLRKILTE 244
                       250
                ....*....|....*..
gi 21359873 289 DPTARPTINELLNDEFF 305
Cdd:cd14069 245 NPNKRITIEDIKKHPWY 261
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
59-301 6.10e-50

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: 173.11  E-value: 6.10e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFeisdadtKEVFAGKIVP-KSLLLKPHQREKMSM---EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd13999   1 IGSGSFGEVY-------KGKWRGTDVAiKKLKVEDDNDELLKEfrrEVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd13999  74 GGSLYDlLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFET-SCLKETYLRIKKNEYS-IPKHINPVAASLIQKMLQTDPT 291
Cdd:cd13999 154 TPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKElSPIQIAAAVVQKGLRPpIPPDCPPELSKLIKRCWNEDPE 233
                       250
                ....*....|
gi 21359873 292 ARPTINELLN 301
Cdd:cd13999 234 KRPSFSEIVK 243
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
59-293 3.60e-49

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: 173.55  E-value: 3.60e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHrSLAHQH--VVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd05570   3 LGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVL-ALANRHpfLTGLHACFQTEDRLYFVMEYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLL-ELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd05570  82 DLMfHIQRARR-FTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCGTP 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05570 161 DYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARR 238
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
59-300 7.71e-49

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: 170.91  E-value: 7.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14116  13 LGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtkVEYDGERKKTLCGTPNYI 218
Cdd:cd14116  93 YRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS--VHAPSSRRTTLCGTLDYL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINE 298
Cdd:cd14116 171 PPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLRE 250

                ..
gi 21359873 299 LL 300
Cdd:cd14116 251 VL 252
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
59-304 1.39e-48

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: 170.35  E-value: 1.39e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKS-LLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14098   8 LGSGTFAEVKKAVEVETGKMRAIKQIVKRkVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEGGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED--LEVKIGDFGLAtKVEYDGERKKTLCGTP 215
Cdd:cd14098  88 LMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDdpVIVKISDFGLA-KVIHTGTFLVTFCGTM 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKK------GHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKM 285
Cdd:cd14098 167 AYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPlvdfNISEEAIDFILRL 246
                       250
                ....*....|....*....
gi 21359873 286 LQTDPTARPTINELLNDEF 304
Cdd:cd14098 247 LDVDPEKRMTAAQALDHPW 265
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
58-347 1.41e-48

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: 171.71  E-value: 1.41e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLllkPHQREkmsmeISIHRSL-AHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd14092  13 ALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL---DTSRE-----VQLLRLCqGHPNIVKLHEVFQDELHTYLVMELLRGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLAtKVEYDGERKKTLCG 213
Cdd:cd14092  85 ELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFA-RLKPENQPLKTPCF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVL----SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK----ETYLRIKKNEYSIP----KHINPVAASL 281
Cdd:cd14092 164 TLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSGDFSFDgeewKNVSSEAKSL 243
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 282 IQKMLQTDPTARPTINELLNDEFFTSGYIPARLPItcLTipprfsiaPSSLDPSNRKPLTVLNKGL 347
Cdd:cd14092 244 IQGLLTVDPSKRLTMSELRNHPWLQGSSSPSSTPL--MT--------PGVLSSSAAAVSTALRATF 299
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
60-305 1.65e-48

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: 169.74  E-value: 1.65e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  60 GKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELcrrrsL- 138
Cdd:cd05578   9 GKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL-----Ll 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 ---LELH-KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGT 214
Cdd:cd05578  84 ggdLRYHlQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLT-DGTLATSTSGT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFE--TSCLKETYLRI-KKNEYSIPKHINPVAASLIQKMLQTDPT 291
Cdd:cd05578 163 KPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEihSRTSIEEIRAKfETASVLYPAGWSEEAIDLINKLLERDPQ 242
                       250
                ....*....|....*
gi 21359873 292 AR-PTINELLNDEFF 305
Cdd:cd05578 243 KRlGDLSDLKNHPYF 257
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-301 2.24e-48

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: 170.68  E-value: 2.24e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFA---KCFEISdadTKEVFAGKIV-PKSLLLKPHQreKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd14086   9 LGKGAFSvvrRCVQKS---TGQEFAAKIInTKKLSARDHQ--KLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKVEYDGERKKTL 211
Cdd:cd14086  84 GGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQAWFGF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKH----INPVAASLIQKMLQ 287
Cdd:cd14086 164 AGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPewdtVTPEAKDLINQMLT 243
                       250
                ....*....|....
gi 21359873 288 TDPTARPTINELLN 301
Cdd:cd14086 244 VNPAKRITAAEALK 257
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
59-300 3.06e-48

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: 168.60  E-value: 3.06e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFA---KCFEISdadTKEVFAGKIVPKslllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14006   1 LGRGRFGvvkRCIEKA---TGREFAAKFIPK----RDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE--DLEVKIGDFGLATKVEyDGERKKTLCG 213
Cdd:cd14006  74 GELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKIIDFGLARKLN-PGEELKEIFG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSI----PKHINPVAASLIQKMLQTD 289
Cdd:cd14006 153 TPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFseeyFSSVSQEAKDFIRKLLVKE 232
                       250
                ....*....|.
gi 21359873 290 PTARPTINELL 300
Cdd:cd14006 233 PRKRPTAQEAL 243
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
58-304 3.70e-48

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: 168.73  E-value: 3.70e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPksLLLKPHQR----EKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd06632   7 LLGSGSFGSVYEGFNGDTGDFFAVKEVS--LVDDDKKSresvKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGeRKKTLCG 213
Cdd:cd06632  85 PGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFS-FAKSFKG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKK--GHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY--SIPKHINPVAASLIQKMLQTD 289
Cdd:cd06632 164 SPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGElpPIPDHLSPDAKDFIRLCLQRD 243
                       250
                ....*....|....*
gi 21359873 290 PTARPTINELLNDEF 304
Cdd:cd06632 244 PEDRPTASQLLEHPF 258
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
59-306 5.61e-47

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: 165.46  E-value: 5.61e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAgkivPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06614   8 IGEGASGEVYKATDRATGKEVA----IKKMRLRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd06614  84 TDiITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNSVVGTPYW 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYLrIKKNEYSIPKHINPVAASL---IQKMLQTDPTAR 293
Cdd:cd06614 164 MAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPyLEEPPLRALFL-ITTKGIPPLKNPEKWSPEFkdfLNKCLVKDPEKR 242
                       250
                ....*....|...
gi 21359873 294 PTINELLNDEFFT 306
Cdd:cd06614 243 PSAEELLQHPFLK 255
POLO_box_1 cd13118
First polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like Ser ...
407-494 1.15e-46

First polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.


Pssm-ID: 240561  Cd Length: 91  Bit Score: 159.02  E-value: 1.15e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 407 PIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVS--SHPNSLMKKITLLKYFRN 484
Cdd:cd13118   1 PPVWVSKWVDYSNKYGLGYQLSDGSVGVLFNDSTKMVLSPDGKHVQYIERNGEESELTRSddSYPPDLAKKVTLLKYFRN 80
                        90
                ....*....|
gi 21359873 485 YMSEHLLKAG 494
Cdd:cd13118  81 YMEEHLSKGG 90
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
59-305 1.72e-46

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: 164.64  E-value: 1.72e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFED--NDFVFVVLELCRRR 136
Cdd:cd08217   8 IGKGSFGTVRKVRRKSDGKILVWKEI-DYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIVDraNTTLYIVMEYCEGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKA----LTEPEARYYLRQIVLGCQYLHR-----NRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGER 207
Cdd:cd08217  87 DLAQLIKKCKKenqyIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFLDSDNNVKLGDFGLARVLSHDSSF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 KKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHINPVAASLIQKML 286
Cdd:cd08217 167 AKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPrIPSRYSSELNEVIKSML 246
                       250
                ....*....|....*....
gi 21359873 287 QTDPTARPTINELLNDEFF 305
Cdd:cd08217 247 NVDPDKRPSVEELLQLPLI 265
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-302 3.63e-46

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: 163.70  E-value: 3.63e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14083  11 LGTGAFSEVVLAEDKATGKLVAIKCIDKKALKG--KEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLF---LNEDLEVKIGDFGLaTKVEyDGERKKTLCGTP 215
Cdd:cd14083  89 FDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGL-SKME-DSGVMSTACGTP 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQTDPT 291
Cdd:cd14083 167 GYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSpywdDISDSAKDFIRHLMEKDPN 246
                       250
                ....*....|.
gi 21359873 292 ARPTINELLND 302
Cdd:cd14083 247 KRYTCEQALEH 257
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
59-304 1.37e-45

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: 162.33  E-value: 1.37e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPK----SLLLKPHQREkmsmeISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd14097   9 LGQGSFGVVIEATHKETQTKWAIKKINRekagSSAVKLLERE-----VDILKHVNHAHIIHLEEVFETPKRMYLVMELCE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL------NED-LEVKIGDFGLATKVEYDGER 207
Cdd:cd14097  84 DGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidNNDkLNIKVTDFGLSVQKYGLGED 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 K-KTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNE----YSIPKHINPVAASLI 282
Cdd:cd14097 164 MlQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDltftQSVWQSVSDAAKNVL 243
                       250       260
                ....*....|....*....|..
gi 21359873 283 QKMLQTDPTARPTINELLNDEF 304
Cdd:cd14097 244 QQLLKVDPAHRMTASELLDNPW 265
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
59-304 1.45e-45

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: 161.53  E-value: 1.45e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14072   8 IGKGNFAKVKLARHVLTGREVAIKIIDKTQL-NPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 ---LELHKRRKaltEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYdGERKKTLCGTP 215
Cdd:cd14072  87 fdyLVAHGRMK---EKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTP-GNKLDTFCGSP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLS-KKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARP 294
Cdd:cd14072 163 PYAAPELFQgKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSKRG 242
                       250
                ....*....|
gi 21359873 295 TINELLNDEF 304
Cdd:cd14072 243 TLEQIMKDRW 252
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
59-293 4.04e-45

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: 163.61  E-value: 4.04e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIhrsLAHQH---VVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd05573   9 IGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDI---LADADspwIVRLHYAFQDEDHLYLVMEYMPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERK------- 208
Cdd:cd05573  86 GDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGDREsylndsv 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 ----------------------KTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIK-- 264
Cdd:cd05573 166 ntlfqdnvlarrrphkqrrvraYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYSKIMnw 245
                       250       260       270
                ....*....|....*....|....*....|.
gi 21359873 265 KNEYSIPKH--INPVAASLIQKMLqTDPTAR 293
Cdd:cd05573 246 KESLVFPDDpdVSPEAIDLIRRLL-CDPEDR 275
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
58-301 5.82e-45

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: 160.25  E-value: 5.82e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLlkpHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd08530   7 KLGKGSYGSVYKVKRLSDNQVYALKEVNLGSL---SQKEREDSvnEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKA----LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydGERKKTL 211
Cdd:cd08530  84 GDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLK--KNLAKTQ 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPV-AASLIQKMLQTDP 290
Cdd:cd08530 162 IGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPPIPPVYSQdLQQIIRSLLQVNP 241
                       250
                ....*....|.
gi 21359873 291 TARPTINELLN 301
Cdd:cd08530 242 KKRPSCDKLLQ 252
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
59-305 1.16e-44

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: 159.35  E-value: 1.16e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPhqrekMSMEISIHRSLAHQHVVGFHG-FFEDNDfVFVVLELCRRRS 137
Cdd:cd06612  11 LGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQE-----IIKEISILKQCDSPYIVKYYGsYFKNTD-LWIVMEYCGAGS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHK-RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd06612  85 VSDIMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVIGTPF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYLrIKKN---EYSIPKHINPVAASLIQKMLQTDPTA 292
Cdd:cd06612 165 WMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPySDIHPMRAIFM-IPNKpppTLSDPEKWSPEFNDFVKKCLVKDPEE 243
                       250
                ....*....|...
gi 21359873 293 RPTINELLNDEFF 305
Cdd:cd06612 244 RPSAIQLLQHPFI 256
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
59-304 1.55e-44

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: 158.99  E-value: 1.55e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFA---KCFEISDadTKEVFAGKIVPKSLLLKPhQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14121   3 LGSGTYAtvyKAYRKSG--AREVVAVKCVSKSSLNKA-STENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL--NEDLEVKIGDFGLATKVEyDGERKKTLCG 213
Cdd:cd14121  80 GDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLssRYNPVLKLADFGFAQHLK-PNDEAHSLRG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNE-YSIPK--HINPVAASLIQKMLQTDP 290
Cdd:cd14121 159 SPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTrpELSADCRDLLLRLLQRDP 238
                       250
                ....*....|....
gi 21359873 291 TARPTINELLNDEF 304
Cdd:cd14121 239 DRRISFEEFFAHPF 252
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
58-304 4.91e-44

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: 157.75  E-value: 4.91e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPksLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd06623   8 VLGQGSSGVVYKVRHKPTGKIYALKKIH--VDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR-VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd06623  86 LADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTFVGTVT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF---ETSCLKETYLRIKKNE-YSIP-KHINPVAASLIQKMLQTDPT 291
Cdd:cd06623 166 YMSPERIQGESYSYAADIWSLGLTLLECALGKFPFlppGQPSFFELMQAICDGPpPSLPaEEFSPEFRDFISACLQKDPK 245
                       250
                ....*....|...
gi 21359873 292 ARPTINELLNDEF 304
Cdd:cd06623 246 KRPSAAELLQHPF 258
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
59-304 5.28e-44

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: 157.67  E-value: 5.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLK-PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14070  10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKdSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAT--KVEYDGERKKTLCGTP 215
Cdd:cd14070  90 LMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNcaGILGYSDPFSTQCGSP 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF--ETSCLKETYLRIKKNEYS-IPKHINPVAASLIQKMLQTDPTA 292
Cdd:cd14070 170 AYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFtvEPFSLRALHQKMVDKEMNpLPTDLSPGAISFLRSLLEPDPLK 249
                       250
                ....*....|..
gi 21359873 293 RPTINELLNDEF 304
Cdd:cd14070 250 RPNIKQALANRW 261
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
59-299 5.53e-44

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: 157.42  E-value: 5.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVfAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14161  11 LGKGTYGRVKKARDSSGRLV-AIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKveYDGER-KKTLCGTPNY 217
Cdd:cd14161  90 YDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNL--YNQDKfLQTYCGSPLY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSF-EVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPvAASLIQKMLQTDPTARPTI 296
Cdd:cd14161 168 ASPEIVNGRPYIGpEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSD-ACGLIRWLLMVNPERRATL 246

                ...
gi 21359873 297 NEL 299
Cdd:cd14161 247 EDV 249
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
59-305 1.01e-43

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: 156.65  E-value: 1.01e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLK-PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDF--VFVVLELCRR 135
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRiPNGEANVKREIQILRRLNHRNVIKLVDVLYNEEKqkLYMVMEYCVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 rSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEY--DGERKKTL 211
Cdd:cd14119  81 -GLQEMLDSApdKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLfaEDDTCTTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPEVLSKKG--HSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTD 289
Cdd:cd14119 160 QGSPAFQPPEIANGQDsfSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLEKD 239
                       250
                ....*....|....*.
gi 21359873 290 PTARPTINELLNDEFF 305
Cdd:cd14119 240 PEKRFTIEQIRQHPWF 255
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
59-293 1.44e-43

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: 157.57  E-value: 1.44e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14209   9 LGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEYVPGGEM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydgERKKTLCGTPNYI 218
Cdd:cd14209  89 FSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVK---GRTWTLCGTPEYL 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd14209 166 APEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
59-322 1.79e-43

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: 157.02  E-value: 1.79e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREkmsmEISI-HRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14091   8 IGKGSYSVCKRCIHKATGKEYAVKIIDKS---KRDPSE----EIEIlLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNEDLE---VKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd14091  81 LLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNiLYADESGDpesLRICDFGFAKQLRAENGLLMTPCY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETS---CLKETYLRIkkNEYSIP------KHINPVAASLIQK 284
Cdd:cd14091 161 TANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGpndTPEVILARI--GSGKIDlsggnwDHVSDSAKDLVRK 238
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21359873 285 MLQTDPTARPTINELLNDEFFTSGyipARLPITCLTIP 322
Cdd:cd14091 239 MLHVDPSQRPTAAQVLQHPWIRNR---DSLPQRQLTDP 273
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
59-303 2.36e-43

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: 156.30  E-value: 2.36e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPksLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd13996  14 LGSGGFGSVYKVRNKVDGVTYAIKKIR--LTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGGTL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 ---LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL-NEDLEVKIGDFGLATKVEyDGERKKTL--- 211
Cdd:cd13996  92 rdwIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLdNDDLQVKIGDFGLATSIG-NQKRELNNlnn 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 ------------CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVgkpPFETSclKETYLRIKK------NEYSIPKH 273
Cdd:cd13996 171 nnngntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PFKTA--MERSTILTDlrngilPESFKAKH 245
                       250       260       270
                ....*....|....*....|....*....|
gi 21359873 274 inPVAASLIQKMLQTDPTARPTINELLNDE 303
Cdd:cd13996 246 --PKEADLIQSLLSKNPEERPSAEQLLRSL 273
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
59-301 3.12e-43

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: 155.24  E-value: 3.12e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14071   8 IGKGNFAVVKLARHRITKTEVAIKIIDKSQL-DEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNYI 218
Cdd:cd14071  87 FDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFK-PGELLKTWCGSPPYA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSF-EVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd14071 166 APEVFEGKEYEGpQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPSKRLTIE 245

                ....
gi 21359873 298 ELLN 301
Cdd:cd14071 246 QIKK 249
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
59-301 6.38e-43

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: 154.95  E-value: 6.38e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFA---KCFEISdadTKEVFAGKIVPKSLLLKPHQ---REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd14105  13 LGSGQFAvvkKCREKS---TGLEYAAKFIKKRRSKASRRgvsREDIEREVSILRQVLHPNIITLHDVFENKTDVVLILEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE----VKIGDFGLATKVEyDGERK 208
Cdd:cd14105  90 VAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIE-DGNEF 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS----IPKHINPVAASLIQK 284
Cdd:cd14105 169 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDfddeYFSNTSELAKDFIRQ 248
                       250
                ....*....|....*..
gi 21359873 285 MLQTDPTARPTINELLN 301
Cdd:cd14105 249 LLVKDPRKRMTIQESLR 265
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-300 8.51e-43

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: 155.15  E-value: 8.51e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKmsmEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14166  11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLEN---EIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLaTKVEYDGeRKKTLCGTP 215
Cdd:cd14166  88 FDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGL-SKMEQNG-IMSTACGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQTDPT 291
Cdd:cd14166 166 GYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESpfwdDISESAKDFIRHLLEKNPS 245

                ....*....
gi 21359873 292 ARPTINELL 300
Cdd:cd14166 246 KRYTCEKAL 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
59-293 1.03e-42

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 156.13  E-value: 1.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  139 LElhKRRKALTEPE--ARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydgERKKTLCGTPN 216
Cdd:PTZ00263 106 FT--HLRKAGRFPNdvAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP---DRTFTLCGTPE 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873  217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:PTZ00263 181 YLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHTKR 257
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
59-293 2.23e-42

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: 155.26  E-value: 2.23e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCF---EISDADTKEVFAGKIVPKSLLLKpHQREKM--SMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05584   4 LGKGGYGKVFqvrKTTGSDKGKIFAMKVLKKASIVR-NQKDTAhtKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd05584  83 SGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTHTFCG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05584 163 TIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNVSSR 242
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
59-305 3.83e-42

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: 153.41  E-value: 3.83e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKslllkPHQREKMSM----EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd07829   7 LGEGTYGVVYKAKDKKTGEIVALKKIRL-----DNEEEGIPStalrEISLLKELKHPNIVKLLDVIHTENKLYLVFEYCD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 R--RSLLelHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDgerKKTLc 212
Cdd:cd07829  82 QdlKKYL--DKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIP---LRTY- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 213 gTPN-----YIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI------------------KKNEY 268
Cdd:cd07829 156 -THEvvtlwYRAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIfqilgtpteeswpgvtklPDYKP 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 21359873 269 SIPKH-----------INPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07829 235 TFPKWpkndlekvlprLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
59-302 4.46e-42

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: 153.36  E-value: 4.46e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADT--KEVfAGKIVPK----SLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd14096   9 IGEGAFSNVYKAVPLRNtgKPV-AIKVVRKadlsSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLF---------------LNEDLE-------- 189
Cdd:cd14096  88 ADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkADDDETkvdegefi 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 190 ----------VKIGDFGLATKVeyDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKET 259
Cdd:cd14096 168 pgvggggigiVKLADFGLSKQV--WDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDESIETL 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 21359873 260 YLRIKKNEYSIPK----HINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd14096 246 TEKISRGDYTFLSpwwdEISKSAKDLISHLLTVDPAKRYDIDEFLAH 292
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
59-300 5.86e-42

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: 151.80  E-value: 5.86e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd08529   8 LGKGSFGVVYKVVRKVDGRVYALKQIDISRM-SRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAENGDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd08529  87 HSLIKSQrgRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQTIVGTPY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHINPVAASLIQKMLQTDPTARPT 295
Cdd:cd08529 167 YLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSCLTKDYRQRPD 246

                ....*
gi 21359873 296 INELL 300
Cdd:cd08529 247 TTELL 251
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
59-305 6.86e-42

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: 151.74  E-value: 6.86e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIH--RSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd06625   8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKALECEIQllKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE--YDGERKKTLCGT 214
Cdd:cd06625  88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQtiCSSTGMKSVTGT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPP---FETSClkeTYLRIKKN--EYSIPKHINPVAASLIQKMLQTD 289
Cdd:cd06625 168 PYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPwaeFEPMA---AIFKIATQptNPQLPPHVSEDARDFLSLIFVRN 244
                       250
                ....*....|....*.
gi 21359873 290 PTARPTINELLNDEFF 305
Cdd:cd06625 245 KKQRPSAEELLSHSFV 260
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
59-307 1.10e-41

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: 152.94  E-value: 1.10e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCF---EISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd05582   3 LGQGSFGKVFlvrKITGPDAGTLYAMKVLKKATL-KVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd05582  82 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGTV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR-- 293
Cdd:cd05582 162 EYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRlg 241
                       250
                ....*....|....*..
gi 21359873 294 ---PTINELLNDEFFTS 307
Cdd:cd05582 242 agpDGVEEIKRHPFFAT 258
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
59-304 1.91e-41

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: 151.06  E-value: 1.91e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVP---KSLLLKPHQ-REKMSM--------EISIHRSLAHQHVVGFHGFFEDNDFV 126
Cdd:cd14077   9 IGAGSMGKVKLAKHIRTGEKCAIKIIPrasNAGLKKEREkRLEKEIsrdirtirEAALSSLLNHPHICRLRDFLRTPNHY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 127 FVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKveYDGE 206
Cdd:cd14077  89 YMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNL--YDPR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 RK-KTLCGTPNYIAPEVLSKKGHSF-EVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQK 284
Cdd:cd14077 167 RLlRTFCGSLYFAAPELLQAQPYTGpEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSECKSLISR 246
                       250       260
                ....*....|....*....|
gi 21359873 285 MLQTDPTARPTINELLNDEF 304
Cdd:cd14077 247 MLVVDPKKRATLEQVLNHPW 266
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
59-305 1.92e-41

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: 150.92  E-value: 1.92e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFA--KCFEISDADTKEVFAGKIVPKSLL--LKPHQREKMSMEISIHRSLAHQHVV-------GFHGffednDFVF 127
Cdd:cd13994   1 IGKGATSvvRIVTKKNPRSGVLYAVKEYRRRDDesKRKDYVKRLTSEYIISSKLHHPNIVkvldlcqDLHG-----KWCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 128 VvLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE- 206
Cdd:cd13994  76 V-MEYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEk 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 ---RKKTLCGTPNYIAPEVLSKKGHS-FEVDVWSIGCIMYTLLVGKPPFETSC------------LKETYLRIKKNEYSI 270
Cdd:cd13994 155 espMSAGLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWRSAKksdsaykayeksGDFTNGPYEPIENLL 234
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21359873 271 PKHinpvAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd13994 235 PSE----CRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
59-305 2.44e-41

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: 150.53  E-value: 2.44e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIV-----PKSLLLKPHQREkmsmeISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd14162   8 LGHGSYAVVKKAYSTKHKCKVAIKIVskkkaPEDYLQKFLPRE-----IEVIKGLKHPNLICFYEAIETTSRVYIIMELA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA--TKVEYDGERK--K 209
Cdd:cd14162  83 ENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFArgVMKTKDGKPKlsE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TLCGTPNYIAPEVLSKKGHS-FEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI-KKNEYSIPKHINPVAASLIQKMLq 287
Cdd:cd14162 163 TYCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVqRRVVFPKNPTVSEECKDLILRML- 241
                       250
                ....*....|....*...
gi 21359873 288 TDPTARPTINELLNDEFF 305
Cdd:cd14162 242 SPVKKRITIEEIKRDPWF 259
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-300 3.39e-41

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: 150.18  E-value: 3.39e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlkPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14167  11 LGTGAFSEVVLAEEKRTQKLVAIKCIAKKAL--EGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLF---LNEDLEVKIGDFGLaTKVEYDGERKKTLCGTP 215
Cdd:cd14167  89 FDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL-SKIEGSGSVMSTACGTP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQTDPT 291
Cdd:cd14167 168 GYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSpywdDISDSAKDFIQHLMEKDPE 247

                ....*....
gi 21359873 292 ARPTINELL 300
Cdd:cd14167 248 KRFTCEQAL 256
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
59-304 3.71e-41

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: 149.80  E-value: 3.71e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQReKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14075  10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQR-LLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 L-ELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNY 217
Cdd:cd14075  89 YtKISTEGK-LSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAK-RGETLNTFCGSPPY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEvLSKKGHSF--EVDVWSIGCIMYTLLVGKPPFETsclkETYLRIKKN----EYSIPKHINPVAASLIQKMLQTDPT 291
Cdd:cd14075 167 AAPE-LFKDEHYIgiYVDIWALGVLLYFMVTGVMPFRA----ETVAKLKKCilegTYTIPSYVSEPCQELIRGILQPVPS 241
                       250
                ....*....|...
gi 21359873 292 ARPTINELLNDEF 304
Cdd:cd14075 242 DRYSIDEIKNSEW 254
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
59-293 4.95e-41

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: 151.35  E-value: 4.95e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05571   3 LGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd05571  83 FFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTPEYL 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05571 163 APEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKR 237
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
59-293 7.40e-41

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: 150.28  E-value: 7.40e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05612   9 IGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEYVPGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydgERKKTLCGTPNYI 218
Cdd:cd05612  89 FSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR---DRTWTLCGTPEYL 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05612 166 APEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDRTRR 240
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
59-305 1.03e-40

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: 148.61  E-value: 1.03e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQ-REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd06613   8 IGSGTYGDVYKARNIATGELAAVKVIK----LEPGDdFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGGGS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd06613  84 LQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSFIGTPYW 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLS---KKGHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYLrIKKNEYSIP----KHI-NPVAASLIQKMLQT 288
Cdd:cd06613 164 MAPEVAAverKGGYDGKCDIWALGITAIELAELQPPmFDLHPMRALFL-IPKSNFDPPklkdKEKwSPDFHDFIKKCLTK 242
                       250
                ....*....|....*..
gi 21359873 289 DPTARPTINELLNDEFF 305
Cdd:cd06613 243 NPKKRPTATKLLQHPFV 259
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
58-307 1.31e-40

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: 150.54  E-value: 1.31e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05595   2 LLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd05595  82 LFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGTPEY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR---- 293
Cdd:cd05595 162 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRlggg 241
                       250
                ....*....|....*
gi 21359873 294 PT-INELLNDEFFTS 307
Cdd:cd05595 242 PSdAKEVMEHRFFLS 256
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
59-308 2.04e-40

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: 149.42  E-value: 2.04e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPhQREKMSMEISihrsLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14179  15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANT-QREIAALKLC----EGHPNIVKLHEVYHDQLHTFLVMELLKGGEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd14179  90 LERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQPLKTPCFTL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFE--------TSCLkETYLRIKKNEYSIP----KHINPVAASLIQ 283
Cdd:cd14179 170 HYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQchdksltcTSAE-EIMKKIKQGDFSFEgeawKNVSQEAKDLIQ 248
                       250       260
                ....*....|....*....|....*
gi 21359873 284 KMLQTDPTARPTINELLNDEFFTSG 308
Cdd:cd14179 249 GLLTVDPNKRIKMSGLRYNEWLQDG 273
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
59-293 2.08e-40

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: 148.09  E-value: 2.08e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14117  14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtkVEYDGERKKTLCGTPNYI 218
Cdd:cd14117  94 YKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS--VHAPSLRRRTMCGTLDYL 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd14117 172 PPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHPSER 246
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
77-305 2.84e-40

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: 148.20  E-value: 2.84e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  77 EVFAGKIVPKSLllkPHQREKMSMEISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARY 155
Cdd:cd14181  44 EVTAERLSPEQL---EEVRSSTLKEIHILRQVSgHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRS 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 156 YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNYIAPEVL------SKKGHS 229
Cdd:cd14181 121 IMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLE-PGEKLRELCGTPGYLAPEILkcsmdeTHPGYG 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 230 FEVDVWSIGCIMYTLLVGKPPF--ETSCLKETYLRIKKNEYSIPK--HINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14181 200 KEVDLWACGVILFTLLAGSPPFwhRRQMLMLRMIMEGRYQFSSPEwdDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
60-305 2.88e-40

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: 149.30  E-value: 2.88e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  60 GKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLL 139
Cdd:cd05599  10 GRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEFLPGGDMM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 140 ELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLcGTPNYIA 219
Cdd:cd05599  90 TLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSHLAYSTV-GTPDYIA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 220 PEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIK--KNEYSIPK--HINPVAASLIQKMLqTDPTAR-- 293
Cdd:cd05599 169 PEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPevPISPEAKDLIERLL-CDAEHRlg 247
                       250
                ....*....|...
gi 21359873 294 -PTINELLNDEFF 305
Cdd:cd05599 248 aNGVEEIKSHPFF 260
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
59-305 6.35e-40

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: 146.23  E-value: 6.35e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkslLLKPHQREKMSMEISIHRSL----AHQHVVGFHGFFEDNDFVFV--VLEL 132
Cdd:cd05118   7 IGEGAFGTVWLARDKVTGEKVAIKKI----KNDFRHPKAALREIKLLKHLndveGHPNIVKLLDVFEHRGGNHLclVFEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRrSLLELHKRRKA-LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE-VKIGDFGLAtkVEYDGERKKT 210
Cdd:cd05118  83 MGM-NLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGqLKLADFGLA--RSFTSPPYTP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIkkneysIPKHINPVAASLIQKMLQTD 289
Cdd:cd05118 160 YVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKI------VRLLGTPEALDLLSKMLKYD 233
                       250
                ....*....|....*.
gi 21359873 290 PTARPTINELLNDEFF 305
Cdd:cd05118 234 PAKRITASQALAHPYF 249
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
59-302 8.91e-40

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: 146.02  E-value: 8.91e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPhQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14074  11 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDV-SKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGGDM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE-VKIGDFGLATKVEyDGERKKTLCGTPN 216
Cdd:cd14074  90 YDyIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFSNKFQ-PGEKLETSCGSLA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSkkGHSFE---VDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd14074 169 YSAPEILL--GDEYDapaVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIRDPKKR 246

                ....*....
gi 21359873 294 PTINELLND 302
Cdd:cd14074 247 ASLEEIENH 255
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
59-293 1.24e-39

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: 147.53  E-value: 1.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIhRSLAHQH--VVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRV-LALASQHpfLTHLFCTFQTESHLFFVMEYLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd05592  82 DLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCGTPD 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05592 162 YIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKR 238
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
96-305 1.39e-39

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: 145.96  E-value: 1.39e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  96 EKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHK---RRKALTEPEARYYLRQIVLGCQYLHRNRV 172
Cdd:cd06610  44 DELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLLDIMKssyPRGGLDEAIIATVLKEVLKGLEYLHSNGQ 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 173 IHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERK----KTLCGTPNYIAPEVLSK-KGHSFEVDVWSIGCIMYTLLVG 247
Cdd:cd06610 124 IHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRTrkvrKTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAIELATG 203
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21359873 248 KPPFET-SCLKETYLRIKKNEYSIPKHINPVAAS-----LIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd06610 204 AAPYSKyPPMKVLMLTLQNDPPSLETGADYKKYSksfrkMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
79-299 1.47e-39

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: 145.97  E-value: 1.47e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  79 FAGKIVPKSLLLKPHQR----EKMSMEISIHRSLAHQHVVGFHGFFED--NDFVFVVLELCRRRSLLELhKRRKALTEPE 152
Cdd:cd14118  38 FFRRPPPRRKPGALGKPldplDRVYREIAILKKLDHPNVVKLVEVLDDpnEDNLYMVFELVDKGAVMEV-PTDNPLSEET 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 153 ARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFE- 231
Cdd:cd14118 117 ARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKFSg 196
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21359873 232 --VDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKH--INPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd14118 197 kaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPDDpvVSEQLKDLILRMLDKNPSERITLPEI 268
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
59-305 2.05e-39

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: 145.31  E-value: 2.05e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDND-FVFVVLELCRRRS 137
Cdd:cd14165   9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILARLNHKSIIKTYEIFETSDgKVYIVMELGVQGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERK----KTLCG 213
Cdd:cd14165  89 LLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRivlsKTFCG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLskKGHSFE---VDVWSIGCIMYTLLVGKPPFETSCLKETyLRI-KKNEYSIP--KHINPVAASLIQKMLQ 287
Cdd:cd14165 169 SAAYAAPEVL--QGIPYDpriYDIWSLGVILYIMVCGSMPYDDSNVKKM-LKIqKEHRVRFPrsKNLTSECKDLIYRLLQ 245
                       250
                ....*....|....*...
gi 21359873 288 TDPTARPTINELLNDEFF 305
Cdd:cd14165 246 PDVSQRLCIDEVLSHPWL 263
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
59-300 2.16e-39

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: 145.55  E-value: 2.16e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQ---REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14194  13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRgvsREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNEDL---EVKIGDFGLATKVEYdGERKKTL 211
Cdd:cd14194  93 GELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDRNVpkpRIKIIDFGLAHKIDF-GNEFKNI 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQ 287
Cdd:cd14194 172 FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDeyfsNTSALAKDFIRRLLV 251
                       250
                ....*....|...
gi 21359873 288 TDPTARPTINELL 300
Cdd:cd14194 252 KDPKKRMTIQDSL 264
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
59-304 2.16e-39

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: 145.47  E-value: 2.16e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06609   9 IGKGSFGEVYKGIDKRTNQVVAIKVI--DLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGGSV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd06609  87 LDLLKPGP-LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNTFVGTPFWM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKKNEYSIPKH-INPVAASLIQKMLQTDPTARPTI 296
Cdd:cd06609 166 APEVIKQSGYDEKADIWSLGITAIELAKGEPPLsDLHPMRVLFLIPKNNPPSLEGNkFSKPFKDFVELCLNKDPKERPSA 245

                ....*...
gi 21359873 297 NELLNDEF 304
Cdd:cd06609 246 KELLKHKF 253
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
60-304 2.54e-39

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: 144.70  E-value: 2.54e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  60 GKGGFAKCFEISDADTKEVFAGKIVPKSlllkpHQREK----MSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14002  10 GEGSFGKVYKGRRKYTGQVVALKFIPKR-----GKSEKelrnLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 rSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd14002  85 -ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLTSIKGTP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPT 295
Cdd:cd14002 164 LYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKDPSKRLS 243

                ....*....
gi 21359873 296 INELLNDEF 304
Cdd:cd14002 244 WPDLLEHPF 252
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
59-304 8.27e-39

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: 143.33  E-value: 8.27e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADT---------KEVFAGKivpksllLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVV 129
Cdd:cd08222   8 LGSGNFGTVYLVSDLKAtadeelkvlKEISVGE-------LQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSL----LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLeVKIGDFGLATKVEYDG 205
Cdd:cd08222  81 TEYCEGGDLddkiSEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRILMGTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 ERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY-SIPKHINPVAASLIQK 284
Cdd:cd08222 160 DLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSR 239
                       250       260
                ....*....|....*....|
gi 21359873 285 MLQTDPTARPTINELLNDEF 304
Cdd:cd08222 240 MLNKDPALRPSAAEILKIPF 259
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
59-293 1.42e-38

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: 144.56  E-value: 1.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIhRSLAHQH--VVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd05591   3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRI-LALAAKHpfLTALHSCFQTKDRLFFVMEYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd05591  82 DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTPD 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05591 162 YIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKR 238
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
59-300 1.55e-38

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: 142.78  E-value: 1.55e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlkPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14185   8 IGDGNFAVVKECRHWNENQEYAMKIIDKSKL--KGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL--NED--LEVKIGDFGLATKVEydgERKKTLCGT 214
Cdd:cd14185  86 FDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhNPDksTTLKLADFGLAKYVT---GPIFTVCGT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETS--CLKETYLRIKKNEYS-IP---KHINPVAASLIQKMLQT 288
Cdd:cd14185 163 PTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQLGHYEfLPpywDNISEAAKDLISRLLVV 242
                       250
                ....*....|..
gi 21359873 289 DPTARPTINELL 300
Cdd:cd14185 243 DPEKRYTAKQVL 254
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
59-306 2.53e-38

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: 142.12  E-value: 2.53e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDAD-TKEVFAGKIVPKSLLLKPhqREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14120   1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKS--QNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLE-LHKRRkALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE---------DLEVKIGDFGLATKVEyDGER 207
Cdd:cd14120  79 LADyLQAKG-TLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHnsgrkpspnDIRLKIADFGFARFLQ-DGMM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 KKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSC---LKETYLRIKKNEYSIPKHINPVAASLIQK 284
Cdd:cd14120 157 AATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTpqeLKAFYEKNANLRPNIPSGTSPALKDLLLG 236
                       250       260
                ....*....|....*....|..
gi 21359873 285 MLQTDPTARptineLLNDEFFT 306
Cdd:cd14120 237 LLKRNPKDR-----IDFEDFFS 253
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
59-293 2.64e-38

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: 143.98  E-value: 2.64e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHR---SLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd05589   7 LGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFEtvnSARHPFLVNLFACFQTPEHVCFVMEYAAG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLeLHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd05589  87 GDLM-MHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTSTFCGTP 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05589 166 EFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNPERR 243
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
61-293 3.17e-38

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: 141.85  E-value: 3.17e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  61 KGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQ-HVVGFHGFFEDNDFVFVVLELCRRRSLL 139
Cdd:cd05611   6 KGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESpYVAKLYYSFQSKDYLYLVMEYLNGGDCA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 140 ELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLaTKVEYDGERKKTLCGTPNYIA 219
Cdd:cd05611  86 SLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGL-SRNGLEKRHNKKFVGTPDYLA 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 220 PEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHIN----PVAASLIQKMLQTDPTAR 293
Cdd:cd05611 165 PETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKefcsPEAVDLINRLLCMDPAKR 242
POLO_box_2 cd13117
Second polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like ...
509-590 3.42e-38

Second polo-box domain (PBD) of polo-like kinases Plk1, Plk2, Plk3, and Plk5; The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.


Pssm-ID: 240560  Cd Length: 81  Bit Score: 135.40  E-value: 3.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 509 PYLRTWFRTRSAIILHLSNGSVQINFFqDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVD 588
Cdd:cd13117   1 PFVKKWLRTKSAIVFRLSNGTVQVNFF-DHTKIILSPLGKLVTYIDKKRESRTYPLSELLKSGCSSELAKRLKYAKEILK 79

                ..
gi 21359873 589 KL 590
Cdd:cd13117  80 EL 81
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
59-300 4.14e-38

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: 141.21  E-value: 4.14e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCR---KAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LElhkrRKA-----LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNED-LEVKIGDFGLATKveYDGERK-KT 210
Cdd:cd14103  78 FE----RVVdddfeLTERDCILFMRQICEGVQYMHKQGILHLDLKPENiLCVSRTgNQIKIIDFGLARK--YDPDKKlKV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY----SIPKHINPVAASLIQKML 286
Cdd:cd14103 152 LFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWdfddEAFDDISDEAKDFISKLL 231
                       250
                ....*....|....
gi 21359873 287 QTDPTARPTINELL 300
Cdd:cd14103 232 VKDPRKRMSAAQCL 245
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
59-304 4.98e-38

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: 141.13  E-value: 4.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKslllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14087   9 IGRGSFSRVVRVEHRVTRQPYAIKMIET----KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGEL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLA-TKVEYDGERKKTLCGT 214
Cdd:cd14087  85 FDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLAsTRKKGPNCLMKTTCGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTDP 290
Cdd:cd14087 165 PEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSgepwPSVSNLAKDFIDRLLTVNP 244
                       250
                ....*....|....
gi 21359873 291 TARPTINELLNDEF 304
Cdd:cd14087 245 GERLSATQALKHPW 258
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
93-304 6.23e-38

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: 141.28  E-value: 6.23e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  93 HQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRV 172
Cdd:cd14010  36 SKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGI 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 173 IHRDLKLGNLFLNEDLEVKIGDFGLATKV----------------EYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWS 236
Cdd:cd14010 116 IYCDLKPSNILLDGNGTLKLSDFGLARREgeilkelfgqfsdegnVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWA 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21359873 237 IGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAAS-----LIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd14010 196 LGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKVSSKPSpdfksLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
101-318 7.58e-38

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: 142.66  E-value: 7.58e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDF-----VFVVLELCRrrslLELH---KRRKALTEPEARYYLRQIVLGCQYLHRNRV 172
Cdd:cd07834  49 EIKILRHLKHENIIGLLDILRPPSPeefndVYIVTELME----TDLHkviKSPQPLTDDHIQYFLYQILRGLKYLHSAGV 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 173 IHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDgERKKTLCG---TPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGK 248
Cdd:cd07834 125 IHRDLKPSNILVNSNCDLKICDFGLARGVDPD-EDKGFLTEyvvTRWYRAPELlLSSKKYTKAIDIWSVGCIFAELLTRK 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 249 PPFE-----------------------TSCLKET---YLRI-----KKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd07834 204 PLFPgrdyidqlnlivevlgtpseedlKFISSEKarnYLKSlpkkpKKPLSEVFPGASPEAIDLLEKMLVFNPKKRITAD 283
                       250       260
                ....*....|....*....|.
gi 21359873 298 ELLNDEFFTSGYIPARLPITC 318
Cdd:cd07834 284 EALAHPYLAQLHDPEDEPVAK 304
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
59-304 7.88e-38

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: 141.30  E-value: 7.88e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQR----EKMSMEISIHRSLAHQHVVGFHGFFE-DNDFVFVVLELC 133
Cdd:cd13990   8 LGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKqnyiKHALREYEIHKSLDHPRIVKLYDVFEiDTDSFCTVLEYC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYL--HRNRVIHRDLKLGNLFLNED---LEVKIGDFGLATKVEYDGERK 208
Cdd:cd13990  88 DGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGnvsGEIKITDFGLSKIMDDESYNS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTL------CGTPNYIAPEVLSKKGH----SFEVDVWSIGCIMYTLLVGKPPF-----ETSCLKE-TYLRIKKNEYSIPK 272
Cdd:cd13990 168 DGMeltsqgAGTYWYLPPECFVVGKTppkiSSKVDVWSVGVIFYQMLYGRKPFghnqsQEAILEEnTILKATEVEFPSKP 247
                       250       260       270
                ....*....|....*....|....*....|..
gi 21359873 273 HINPVAASLIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd13990 248 VVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
59-300 8.41e-38

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: 140.49  E-value: 8.41e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIV--PKSLllkpHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd08219   8 VGEGSFGRALLVQHVNSDQKYAMKEIrlPKSS----SAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHK--RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd08219  84 DLMQKIKlqRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACTYVGT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd08219 164 PYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFKRNPRSR 243

                ....*..
gi 21359873 294 PTINELL 300
Cdd:cd08219 244 PSATTIL 250
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
59-301 1.26e-37

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: 140.48  E-value: 1.26e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQ---REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14196  13 LGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVSG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNEDL---EVKIGDFGLATKVEyDGERKKTL 211
Cdd:cd14196  93 GELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIE-DGVEFKNI 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQ 287
Cdd:cd14196 172 FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEeffsHTSELAKDFIRKLLV 251
                       250
                ....*....|....
gi 21359873 288 TDPTARPTINELLN 301
Cdd:cd14196 252 KETRKRLTIQEALR 265
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
59-300 1.97e-37

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 139.59  E-value: 1.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873     59 LGKGGFAKCFE----ISDADTKEVFAGKIVPKSLllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:smart00219   7 LGEGAFGEVYKgklkGKGGKKKVEVAVKTLKEDA--SEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    135 RRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtKVEYDGERKKTLCG 213
Cdd:smart00219  85 GGDLLSyLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS-RDLYDDDYYRKRGG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    214 T-P-NYIAPEVLSKKGHSFEVDVWSIGCIMY---TLlvGKPPFETSCLKETYLRIKKNEY-SIPKHINPVAASLIQKMLQ 287
Cdd:smart00219 164 KlPiRWMAPESLKEGKFTSKSDVWSFGVLLWeifTL--GEQPYPGMSNEEVLEYLKNGYRlPQPPNCPPELYDLMLQCWA 241
                          250
                   ....*....|...
gi 21359873    288 TDPTARPTINELL 300
Cdd:smart00219 242 EDPEDRPTFSELV 254
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
59-307 3.34e-37

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: 140.87  E-value: 3.34e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLL-KPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05604   4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILnRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd05604  84 LFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGTPEY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPT----AR 293
Cdd:cd05604 164 LAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQlrlgAK 243
                       250
                ....*....|....
gi 21359873 294 PTINELLNDEFFTS 307
Cdd:cd05604 244 EDFLEIKNHPFFES 257
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
59-305 4.76e-37

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: 138.55  E-value: 4.76e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISD-ADTKEVFAGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd08225   8 IGEGSFGKIYLAKAkSDSEHCVIKEIDLTKMPVK--EKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKAL--TEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEV-KIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd08225  86 LMKRINRQRGVlfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAYTCVGT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd08225 166 PYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFApISPNFSRDLRSLISQLFKVSPRDR 245
                       250
                ....*....|..
gi 21359873 294 PTINELLNDEFF 305
Cdd:cd08225 246 PSITSILKRPFL 257
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
59-293 5.15e-37

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: 140.22  E-value: 5.15e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEisiHRSLAHQH----VVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd05587   4 LGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVE---KRVLALSGkppfLTQLHSCFQTMDRLYFVMEYVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd05587  81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGT 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05587 161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKR 239
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
59-307 5.17e-37

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: 139.11  E-value: 5.17e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPkslLLKPHQREKMSMEISIHRSLAHQHVVGFH-GFFEDNDfVFVVLELCRRRS 137
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFAAAKIIQ---IESEEELEDFMVEIDILSECKHPNIVGLYeAYFYENK-LWILIEFCDGGA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 L----LELHKrrkALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd06611  89 LdsimLELER---GLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVL-----SKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKeTYLRIKKNE---YSIPKHINPVAASLIQK 284
Cdd:cd06611 166 TPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHhELNPMR-VLLKILKSEpptLDQPSKWSSSFNDFLKS 244
                       250       260
                ....*....|....*....|...
gi 21359873 285 MLQTDPTARPTINELLNDEFFTS 307
Cdd:cd06611 245 CLVKDPDDRPTAAELLKHPFVSD 267
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
58-307 5.49e-37

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: 141.32  E-value: 5.49e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05594  32 LLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGE 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR-VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd05594 112 LFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPE 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR--- 293
Cdd:cd05594 192 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRlgg 271
                       250
                ....*....|....*.
gi 21359873 294 --PTINELLNDEFFTS 307
Cdd:cd05594 272 gpDDAKEIMQHKFFAG 287
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
59-293 5.53e-37

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: 140.25  E-value: 5.53e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPH-----QREKMSMEISIHrslaHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05588   3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEdidwvQTEKHVFETASN----HPFLVGLHSCFQTESRLFFVIEFV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd05588  79 NGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK-------ETYL--RIKKNEYSIPKHINPVAASLIQK 284
Cdd:cd05588 159 TPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDIVGSSdnpdqntEDYLfqVILEKPIRIPRSLSVKAASVLKG 238

                ....*....
gi 21359873 285 MLQTDPTAR 293
Cdd:cd05588 239 FLNKNPAER 247
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
59-304 5.93e-37

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: 138.34  E-value: 5.93e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFeISDADTKEVFAGKIV---PKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd06631   9 LGKGAYGTVY-CGLTSTGQLIAVKQVeldTSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDG------ERKK 209
Cdd:cd06631  88 GSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLssgsqsQLLK 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI---KKNEYSIPKHINPVAASLIQKML 286
Cdd:cd06631 168 SMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIgsgRKPVPRLPDKFSPEARDFVHACL 247
                       250
                ....*....|....*...
gi 21359873 287 QTDPTARPTINELLNDEF 304
Cdd:cd06631 248 TRDQDERPSAEQLLKHPF 265
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
59-301 8.38e-37

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: 137.80  E-value: 8.38e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkslllkpHQREKMSMEISIH-RSLAHQHVVG----FHGFFEDNDFVFVVLELC 133
Cdd:cd14089   9 LGLGINGKVLECFHKKTGEKFALKVL--------RDNPKARREVELHwRASGCPHIVRiidvYENTYQGRKCLLVVMECM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE---DLEVKIGDFGLATKVEydgeRK 208
Cdd:cd14089  81 EGGELFSRIQERadSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSkgpNAILKLTDFGFAKETT----TK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTL---CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETS-------CLKEtylRIKKNEYSIP----KHI 274
Cdd:cd14089 157 KSLqtpCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaispGMKK---RIRNGQYEFPnpewSNV 233
                       250       260
                ....*....|....*....|....*..
gi 21359873 275 NPVAASLIQKMLQTDPTARPTINELLN 301
Cdd:cd14089 234 SEEAKDLIRGLLKTDPSERLTIEEVMN 260
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
59-300 9.17e-37

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: 138.21  E-value: 9.17e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQ---REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14195  13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRgvsREEIEREVNILREIQHPNIITLHDIFENKTDVVLILELVSG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE----DLEVKIGDFGLATKVEyDGERKKTL 211
Cdd:cd14195  93 GELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDknvpNPRIKLIDFGIAHKIE-AGNEFKNI 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQ 287
Cdd:cd14195 172 FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEeyfsNTSELAKDFIRRLLV 251
                       250
                ....*....|...
gi 21359873 288 TDPTARPTINELL 300
Cdd:cd14195 252 KDPKKRMTIAQSL 264
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
59-307 1.02e-36

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: 137.91  E-value: 1.02e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCF---EISDADTKEVFAGKIVPKSLLLkphQREKMSMEISIHRSLAHQ-----HVVGFHGFFEDNDFVFVVL 130
Cdd:cd05583   2 LGTGAYGKVFlvrKVGGHDAGKLYAMKVLKKATIV---QKAKTAEHTMTERQVLEAvrqspFLVTLHYAFQTDAKLHLIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 131 ELCRRRSLL-ELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATK-VEYDGERK 208
Cdd:cd05583  79 DYVNGGELFtHLYQREH-FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEfLPGENDRA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTLCGTPNYIAPEVLSKK--GHSFEVDVWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSIPKHINPVAASLI 282
Cdd:cd05583 158 YSFCGTIEYMAPEVVRGGsdGHDKAVDWWSLGVLTYELLTGASPFtvdgERNSQSEISKRILKSHPPIPKTFSAEAKDFI 237
                       250       260       270
                ....*....|....*....|....*....|
gi 21359873 283 QKMLQTDPTAR-----PTINELLNDEFFTS 307
Cdd:cd05583 238 LKLLEKDPKKRlgagpRGAHEIKEHPFFKG 267
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-300 1.12e-36

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: 138.64  E-value: 1.12e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlkPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14168  18 LGTGAFSEVVLAEERATGKLFAVKCIPKKAL--KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGEL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNL-FLNEDLEVKI--GDFGLaTKVEYDGERKKTLCGTP 215
Cdd:cd14168  96 FDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLlYFSQDEESKImiSDFGL-SKMEGKGDVMSTACGTP 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQTDPT 291
Cdd:cd14168 175 GYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSpywdDISDSAKDFIRNLMEKDPN 254

                ....*....
gi 21359873 292 ARPTINELL 300
Cdd:cd14168 255 KRYTCEQAL 263
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
59-304 1.19e-36

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: 137.42  E-value: 1.19e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKphqrEKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14665   8 IGSGNFGVARLMRDKQTKELVAVKYIERGEKID----ENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGGEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL--EVKIGDFGLATKVEYDGERKKTLcGTPN 216
Cdd:cd14665  84 FERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQPKSTV-GTPA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEV-DVWSIGCIMYTLLVGKPPFET----SCLKETYLRIKKNEYSIPK--HINPVAASLIQKMLQTD 289
Cdd:cd14665 163 YIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQYSIPDyvHISPECRHLISRIFVAD 242
                       250
                ....*....|....*
gi 21359873 290 PTARPTINELLNDEF 304
Cdd:cd14665 243 PATRITIPEIRNHEW 257
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
59-293 1.24e-36

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: 139.67  E-value: 1.24e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCF---EISDADTKEVFAGKIVPKSLLLkphQREKMSMEISIHRSLAhQHV------VGFHGFFEDNDFVFVV 129
Cdd:cd05614   8 LGTGAYGKVFlvrKVSGHDANKLYAMKVLRKAALV---QKAKTVEHTRTERNVL-EHVrqspflVTLHYAFQTDAKLHLI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATK-VEYDGERK 208
Cdd:cd05614  84 LDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEfLTEEKERT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTLCGTPNYIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSIPKHINPVAASLIQ 283
Cdd:cd05614 164 YSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVARDLLQ 243
                       250
                ....*....|
gi 21359873 284 KMLQTDPTAR 293
Cdd:cd05614 244 KLLCKDPKKR 253
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
59-304 1.37e-36

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: 137.25  E-value: 1.37e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd08218   8 IGEGSFGKALLVKSKEDGKQYVIKEINISKM-SPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARY--YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd08218  87 YKRINAQRGVLFPEDQIldWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTCIGTPY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY-SIPKHINPVAASLIQKMLQTDPTARPT 295
Cdd:cd08218 167 YLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLFKRNPRDRPS 246

                ....*....
gi 21359873 296 INELLNDEF 304
Cdd:cd08218 247 INSILEKPF 255
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
59-307 2.33e-36

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: 138.60  E-value: 2.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISI-HRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05575   3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVlLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd05575  83 LFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGTPEY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR---- 293
Cdd:cd05575 163 LAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRlgsg 242
                       250
                ....*....|....
gi 21359873 294 PTINELLNDEFFTS 307
Cdd:cd05575 243 NDFLEIKNHSFFRP 256
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
59-293 2.44e-36

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: 138.59  E-value: 2.44e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEisiHRSLAHQ----HVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd05616   8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVE---KRVLALSgkppFLTQLHSCFQTMDRLYFVMEYVN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd05616  85 GGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGT 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05616 165 PDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKR 243
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
59-301 2.52e-36

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: 136.71  E-value: 2.52e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKivpkslLLKPHQREKMSMEISIHR------SLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd14106  16 LGRGKFAVVRKCIHKETGKEYAAK------FLRKRRRGQDCRNEILHEiavlelCKDCPRVVNLHEVYETRSELILILEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL---EVKIGDFGLATKVEyDGERKK 209
Cdd:cd14106  90 AAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFplgDIKLCDFGISRVIG-EGEEIR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKM 285
Cdd:cd14106 169 EILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPeelfKDVSPLAIDFIKRL 248
                       250
                ....*....|....*.
gi 21359873 286 LQTDPTARPTINELLN 301
Cdd:cd14106 249 LVKDPEKRLTAKECLE 264
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
75-305 2.73e-36

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: 136.97  E-value: 2.73e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  75 TKEVFAGKI--VPKSLLLKPHQ----REKMSMEISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKA 147
Cdd:cd14182  27 TRQEYAVKIidITGGGSFSPEEvqelREATLKEIDILRKVSgHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVT 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 148 LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTPNYIAPEVL---- 223
Cdd:cd14182 107 LSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLD-PGEKLREVCGTPGYLAPEIIecsm 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 224 --SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSI--PK--HINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd14182 186 ddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFgsPEwdDRSDTVKDLISRFLVVQPQKRYTAE 265

                ....*...
gi 21359873 298 ELLNDEFF 305
Cdd:cd14182 266 EALAHPFF 273
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
59-306 3.58e-36

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: 137.00  E-value: 3.58e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLK-------PHQR----------------EKMSMEISIHRSLAHQHVVG 115
Cdd:cd14200   8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKqygfprrPPPRgskaaqgeqakplaplERVYQEIAILKKLDHVNIVK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 116 FHGFFED--NDFVFVVLELCRRRSLLELhKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIG 193
Cdd:cd14200  88 LIEVLDDpaEDNLYMVFDLLRKGPVMEV-PSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 194 DFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFE---VDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSI 270
Cdd:cd14200 167 DFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSFSgkaLDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPVEF 246
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21359873 271 PK--HINPVAASLIQKMLQTDPTARPTINELLNDEFFT 306
Cdd:cd14200 247 PEepEISEELKDLILKMLDKNPETRITVPEIKVHPWVT 284
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
59-293 3.69e-36

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: 139.01  E-value: 3.69e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPH-----QREKMSMEisihRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05618  28 IGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEdidwvQTEKHVFE----QASNHPFLVGLHSCFQTESRLFFVIEYV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd05618 104 NGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCG 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK-------ETYL--RIKKNEYSIPKHINPVAASLIQK 284
Cdd:cd05618 184 TPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSdnpdqntEDYLfqVILEKQIRIPRSLSVKAASVLKS 263

                ....*....
gi 21359873 285 MLQTDPTAR 293
Cdd:cd05618 264 FLNKDPKER 272
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
59-293 4.78e-36

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: 137.37  E-value: 4.78e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05574   9 LGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA------------------ 198
Cdd:cd05574  89 FRLLQKQpgKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSkqssvtpppvrkslrkgs 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 199 -----------TKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNE 267
Cdd:cd05574 169 rrssvksiekeTFVAEPSARSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKE 248
                       250       260
                ....*....|....*....|....*...
gi 21359873 268 YSIPKHIN--PVAASLIQKMLQTDPTAR 293
Cdd:cd05574 249 LTFPESPPvsSEAKDLIRKLLVKDPSKR 276
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
59-305 5.93e-36

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: 135.59  E-value: 5.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKC-FEISDADTKEVFAGKIVPKSLLLKPHQREK----MSMEISIHRSL---AHQHVVGFHGFFEDNDFVFVVL 130
Cdd:cd14004   8 MGEGAYGQVnLAIYKSKGKEVVIKFIFKERILVDTWVRDRklgtVPLEIHILDTLnkrSHPNIVKLLDFFEDDEFYYLVM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 131 ElCRRRS--LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE---YDg 205
Cdd:cd14004  88 E-KHGSGmdLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIKsgpFD- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 erkkTLCGTPNYIAPEVLskKGHSF---EVDVWSIGCIMYTLLVGKPPFetSCLKETYlrikKNEYSIPKHINPVAASLI 282
Cdd:cd14004 166 ----TFVGTIDYAAPEVL--RGNPYggkEQDIWALGVLLYTLVFKENPF--YNIEEIL----EADLRIPYAVSEDLIDLI 233
                       250       260
                ....*....|....*....|...
gi 21359873 283 QKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14004 234 SRMLNRDVGDRPTIEELLTDPWL 256
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
59-304 6.22e-36

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: 135.97  E-value: 6.22e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIV--PKSLLLKPHQREK-----MSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLE 131
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEMLAVKQVelPKTSSDRADSRQKtvvdaLKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE--YDGERKK 209
Cdd:cd06629  89 YVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDdiYGNNGAT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TLCGTPNYIAPEVL--SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIPK--HINPVAASLIQ 283
Cdd:cd06629 169 SMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgnKRSAPPVPEdvNLSPEALDFLN 248
                       250       260
                ....*....|....*....|.
gi 21359873 284 KMLQTDPTARPTINELLNDEF 304
Cdd:cd06629 249 ACFAIDPRDRPTAAELLSHPF 269
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
59-302 6.37e-36

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: 135.32  E-value: 6.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    59 LGKGGF-----AKCFEISDADTKEVfAGKIVPKSLllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:pfam07714   7 LGEGAFgevykGTLKGEGENTKIKV-AVKTLKEGA--DEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   134 RRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE-RKKTL 211
Cdd:pfam07714  84 PGGDLLDfLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYyRKRGG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   212 CGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPFETSCLKETYLRIKKNEY-SIPKHINPVAASLIQKMLQT 288
Cdd:pfam07714 164 GKLPiKWMAPESLKDGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLEDGYRlPQPENCPDELYDLMKQCWAY 243
                         250
                  ....*....|....
gi 21359873   289 DPTARPTINELLND 302
Cdd:pfam07714 244 DPEDRPTFSELVED 257
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
59-304 8.23e-36

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: 135.23  E-value: 8.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlkpHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06624  16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDS---REVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRR---KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE-DLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd06624  93 SALLRSKwgpLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGINPCTETFTGT 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSK--KGHSFEVDVWSIGCIMYTLLVGKPPF------ETSCLKETYLRIKKNeysIPKHINPVAASLIQKML 286
Cdd:cd06624 173 LQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFielgepQAAMFKVGMFKIHPE---IPESLSEEAKSFILRCF 249
                       250
                ....*....|....*...
gi 21359873 287 QTDPTARPTINELLNDEF 304
Cdd:cd06624 250 EPDPDKRATASDLLQDPF 267
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
59-301 9.25e-36

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: 134.98  E-value: 9.25e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873     59 LGKGGFAKCFE----ISDADTKEVFAGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:smart00221   7 LGEGAFGEVYKgtlkGKGDGKEVEVAVKTLKEDASEQ--QIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    135 RRSLLE-LHKRR-KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtKVEYDGERKKTLC 212
Cdd:smart00221  85 GGDLLDyLRKNRpKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS-RDLYDDDYYKVKG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    213 GT-P-NYIAPEVLSKKGHSFEVDVWSIGCIMY---TLlvGKPPFETSCLKETYLRIKKNEY-SIPKHINPVAASLIQKML 286
Cdd:smart00221 164 GKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWeifTL--GEEPYPGMSNAEVLEYLKKGYRlPKPPNCPPELYKLMLQCW 241
                          250
                   ....*....|....*
gi 21359873    287 QTDPTARPTINELLN 301
Cdd:smart00221 242 AEDPEDRPTFSELVE 256
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
59-293 9.69e-36

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: 136.96  E-value: 9.69e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIhRSLAHQH--VVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRI-LSLARNHpfLTQLYCCFQTPDRLFFVMEFVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd05590  82 DLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGTPD 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05590 162 YIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMR 238
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-300 1.01e-35

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: 135.40  E-value: 1.01e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlkphqREKMSM---EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14169  11 LGEGAFSEVVLAQERGSQRLVALKCIPKKAL-----RGKEAMvenEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN---EDLEVKIGDFGLaTKVEYDGERKkTLC 212
Cdd:cd14169  86 GELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGL-SKIEAQGMLS-TAC 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 213 GTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQT 288
Cdd:cd14169 164 GTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSpywdDISESAKDFIRHLLER 243
                       250
                ....*....|..
gi 21359873 289 DPTARPTINELL 300
Cdd:cd14169 244 DPEKRFTCEQAL 255
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
59-293 1.05e-35

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: 137.05  E-value: 1.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEisiHRSLAHQHVVGF----HGFFEDNDFVFVVLELCR 134
Cdd:cd05615  18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVE---KRVLALQDKPPFltqlHSCFQTVDRLYFVMEYVN 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd05615  95 GGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTTRTFCGT 174
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05615 175 PDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKR 253
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
59-293 1.29e-35

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: 136.23  E-value: 1.29e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIhRSLAHQH--VVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRV-LALAWENpfLTHLYCTFQTKEHLFFVMEFLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLeLHKRRKALTEP-EARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd05620  82 DLM-FHIQDKGRFDLyRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFCGTP 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05620 161 DYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRR 238
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
59-305 1.50e-35

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: 134.72  E-value: 1.50e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlkphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14113  15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLM----KRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE---VKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd14113  91 LDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLN-TTYYIHQLLGSP 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTDPT 291
Cdd:cd14113 170 EFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFLLQMDPA 249
                       250
                ....*....|....
gi 21359873 292 ARPTINELLNDEFF 305
Cdd:cd14113 250 KRPSAALCLQEQWL 263
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
59-305 2.10e-35

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: 135.00  E-value: 2.10e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKivpKSLLlkphQREKMSM------EISIHRSLAHQHVVGFH------GFFEDNDFV 126
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVALK---KIRM----ENEKEGFpitairEIKLLQKLDHPNVVRLKeivtskGSAKYKGSI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 127 FVVLELCRR--RSLLELHKRRkaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD 204
Cdd:cd07840  80 YMVFEYMDHdlTGLLDNPEVK--FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKT-LCGTPNYIAPEVL--SKKgHSFEVDVWSIGCIMYTLLVGKPPF------------------------------ 251
Cdd:cd07840 158 NNADYTnRVITLWYRPPELLlgATR-YGPEVDMWSVGCILAELFTGKPIFqgkteleqlekifelcgspteenwpgvsdl 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 252 ---ETSCLKETYLRIKKNEYSipKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07840 237 pwfENLKPKKPYKRRLREVFK--NVIDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
59-301 2.24e-35

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: 133.94  E-value: 2.24e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd08224   8 IGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAGDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LEL----HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd08224  88 SRLikhfKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTTAAHSLVGT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSclketylriKKNEYSIPKHIN-----PVAA--------SL 281
Cdd:cd08224 168 PYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGE---------KMNLYSLCKKIEkceypPLPAdlysqelrDL 238
                       250       260
                ....*....|....*....|
gi 21359873 282 IQKMLQTDPTARPTINELLN 301
Cdd:cd08224 239 VAACIQPDPEKRPDISYVLD 258
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
59-307 2.35e-35

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: 135.91  E-value: 2.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05598   9 IGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVMDYIPGGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERK----KTLCGT 214
Cdd:cd05598  89 MSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKyylaHSLVGT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIK--KNEYSIPKHIN--PVAASLIQKMLqTDP 290
Cdd:cd05598 169 PNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHEANlsPEAKDLILRLC-CDA 247
                       250       260
                ....*....|....*....|
gi 21359873 291 TARPTIN---ELLNDEFFTS 307
Cdd:cd05598 248 EDRLGRNgadEIKAHPFFAG 267
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
59-301 2.81e-35

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: 133.74  E-value: 2.81e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPH-QREKMSmeisiHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14662   8 IGSGNFGVARLMRNKETKELVAVKYIERGLKIDENvQREIIN-----HRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL--NEDLEVKIGDFGLaTKVEYDGERKKTLCGTP 215
Cdd:cd14662  83 LFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGY-SKSSVLHSQPKSTVGTP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEV-DVWSIGCIMYTLLVGKPPFE----TSCLKETYLRIKKNEYSIPK--HINPVAASLIQKMLQT 288
Cdd:cd14662 162 AYIAPEVLSRKEYDGKVaDVWSCGVTLYVMLVGAYPFEdpddPKNFRKTIQRIMSVQYKIPDyvRVSQDCRHLLSRIFVA 241
                       250
                ....*....|...
gi 21359873 289 DPTARPTINELLN 301
Cdd:cd14662 242 NPAKRITIPEIKN 254
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
59-305 3.41e-35

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: 133.48  E-value: 3.41e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14107  10 IGRGTFGFVKRVTHKGNGECCAAKFIP----LRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELCSSEEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL----NEDLevKIGDFGLATKVEyDGERKKTLCGT 214
Cdd:cd14107  86 LDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsptREDI--KICDFGFAQEIT-PSEHQFSKYGS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNE--YSIPK--HINPVAASLIQKMLQTDP 290
Cdd:cd14107 163 PEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVvsWDTPEitHLSEDAKDFIKRVLQPDP 242
                       250
                ....*....|....*
gi 21359873 291 TARPTINELLNDEFF 305
Cdd:cd14107 243 EKRPSASECLSHEWF 257
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
59-301 6.11e-35

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: 132.66  E-value: 6.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCF--EISDADTKEVF-AGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd00192   3 LGEGAFGEVYkgKLKGGDGKTVDvAVKTLKEDASES--ERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLE-LHKRR--------KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE-YDG 205
Cdd:cd00192  81 GDLLDfLRKSRpvfpspepSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYdDDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 ERKKTLCGTPN-YIAPEVLSKKGHSFEVDVWSIGCIMY---TLlvGKPPFETSCLKETYLRIKK-NEYSIPKHINPVAAS 280
Cdd:cd00192 161 YRKKTGGKLPIrWMAPESLKDGIFTSKSDVWSFGVLLWeifTL--GATPYPGLSNEEVLEYLRKgYRLPKPENCPDELYE 238
                       250       260
                ....*....|....*....|.
gi 21359873 281 LIQKMLQTDPTARPTINELLN 301
Cdd:cd00192 239 LMLSCWQLDPEDRPTFSELVE 259
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
58-304 7.31e-35

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: 132.81  E-value: 7.31e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREKMSM---EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd06626   7 KIGEGTFGKVYTAVNLDTGELMAMKEIR----FQDNDPKTIKEiadEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE-----YDGERKK 209
Cdd:cd06626  83 EGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKnntttMAPGEVN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TLCGTPNYIAPEVL---SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSclketylrikKNEYSIPKHI------------ 274
Cdd:cd06626 163 SLVGTPAYMAPEVItgnKGEGHGRAADIWSLGCVVLEMATGKRPWSEL----------DNEWAIMYHVgmghkppipdsl 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 21359873 275 --NPVAASLIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd06626 233 qlSPEGKDFLSRCLESDPKKRPTASELLDHPF 264
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
59-293 7.71e-35

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: 135.15  E-value: 7.71e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISI-HRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05617  23 IGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVfEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGD 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd05617 103 LMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNY 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFET-----SCLKETYL--RIKKNEYSIPKHINPVAASLIQKMLQTDP 290
Cdd:cd05617 183 IAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIitdnpDMNTEDYLfqVILEKPIRIPRFLSVKASHVLKGFLNKDP 262

                ...
gi 21359873 291 TAR 293
Cdd:cd05617 263 KER 265
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
59-306 7.96e-35

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: 132.55  E-value: 7.96e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQR---EKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEevvEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED-LEVKIGDFG----LATKVEYDGERKKT 210
Cdd:cd06630  88 GSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGaaarLASKGTGAGEFQGQ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKK-----NEYSIPKHINPVAASLIQKM 285
Cdd:cd06630 168 LLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKiasatTPPPIPEHLSPGLRDVTLRC 247
                       250       260
                ....*....|....*....|.
gi 21359873 286 LQTDPTARPTINELLNDEFFT 306
Cdd:cd06630 248 LELQPEDRPPARELLKHPVFT 268
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
84-305 1.38e-34

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: 131.80  E-value: 1.38e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  84 VPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLEL--HKRrkaLTEPEARYYLRQIV 161
Cdd:cd06648  37 VKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTDIvtHTR---MNEEQIATVCRAVL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 162 LGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIM 241
Cdd:cd06648 114 KALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMV 193
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 242 YTLLVGKPPFETSCLKETYLRIKKNEYSIPKH---INPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd06648 194 IEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNlhkVSPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
59-307 1.60e-34

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: 132.46  E-value: 1.60e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKMSMEISIHRSLAHQHVVGF-HGFFEDNDfVFVVLELCRRRS 137
Cdd:cd06643  13 LGDGAFGKVYKAQNKETGILAAAKVIDTK---SEEELEDYMVEIDILASCDHPNIVKLlDAFYYENN-LWILIEFCAGGA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 ----LLELhkrRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd06643  89 vdavMLEL---ERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDSFIG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVL----SK-KGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNE---YSIPKHINPVAASLIQKM 285
Cdd:cd06643 166 TPYWMAPEVVmcetSKdRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPEFKDFLRKC 245
                       250       260
                ....*....|....*....|..
gi 21359873 286 LQTDPTARPTINELLNDEFFTS 307
Cdd:cd06643 246 LEKNVDARWTTSQLLQHPFVSV 267
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
59-301 1.66e-34

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: 131.84  E-value: 1.66e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCF------EISDADTKEVfAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd14076   9 LGEGEFGKVKlgwplpKANHRSGVQV-AIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKV-EYDGERKKTL 211
Cdd:cd14076  88 VSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFdHFNGDLMSTS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPE--VLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-------ETSCLKETYLRIKKNEYSIPKHINPVAASLI 282
Cdd:cd14076 168 CGSPCYAAPElvVSDSMYAGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPLIFPEYVTPKARDLL 247
                       250
                ....*....|....*....
gi 21359873 283 QKMLQTDPTARPTINELLN 301
Cdd:cd14076 248 RRILVPNPRKRIRLSAIMR 266
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
58-306 1.98e-34

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: 133.67  E-value: 1.98e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05593  22 LLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd05593 102 LFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEY 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR---- 293
Cdd:cd05593 182 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPNKRlggg 261
                       250
                ....*....|....
gi 21359873 294 -PTINELLNDEFFT 306
Cdd:cd05593 262 pDDAKEIMRHSFFT 275
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
59-293 3.11e-34

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: 131.66  E-value: 3.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCF---EISDADTKEVFAGKIVPKSLLLkphQREKMSMEISIHRSLAhQHV------VGFHGFFEDNDFVFVV 129
Cdd:cd05613   8 LGTGAYGKVFlvrKVSGHDAGKLYAMKVLKKATIV---QKAKTAEHTRTERQVL-EHIrqspflVTLHYAFQTDTKLHLI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD-GERK 208
Cdd:cd05613  84 LDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDeNERA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTLCGTPNYIAPEVL--SKKGHSFEVDVWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSIPKHINPVAASLI 282
Cdd:cd05613 164 YSFCGTIEYMAPEIVrgGDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKDII 243
                       250
                ....*....|.
gi 21359873 283 QKMLQTDPTAR 293
Cdd:cd05613 244 QRLLMKDPKKR 254
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
59-304 3.19e-34

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: 131.12  E-value: 3.19e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIV------PKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKQVelpsvsAENKDRKKSMLDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD------GE 206
Cdd:cd06628  88 VPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANslstknNG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 RKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY-SIPKHINPVAASLIQKM 285
Cdd:cd06628 168 ARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASpTIPSNISSEARDFLEKT 247
                       250
                ....*....|....*....
gi 21359873 286 LQTDPTARPTINELLNDEF 304
Cdd:cd06628 248 FEIDHNKRPTADELLKHPF 266
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
59-301 3.23e-34

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: 130.92  E-value: 3.23e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKivpKSLLLKPHQREKMSMEISIHRSLA-HQHVVGF--HGFFEDNDF--VFVVLELC 133
Cdd:cd13985   8 LGEGGFSYVYLAHDVNTGRRYALK---RMYFNDEEQLRVAIKEIEIMKRLCgHPNIVQYydSAILSSEGRkeVLLLMEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRrSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRN--RVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKK 209
Cdd:cd13985  85 PG-SLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHSQspPIIHRDIKIENILFSNTGRFKLCDFGSATTEHYPLERAE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TlCG----------TPNYIAPEVL---SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSclkeTYLRIKKNEYSIPKHIN- 275
Cdd:cd13985 164 E-VNiieeeiqkntTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDES----SKLAIVAGKYSIPEQPRy 238
                       250       260
                ....*....|....*....|....*..
gi 21359873 276 -PVAASLIQKMLQTDPTARPTINELLN 301
Cdd:cd13985 239 sPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
59-306 3.27e-34

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: 132.40  E-value: 3.27e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIH-RSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd05603  83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCGTPEY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPT----AR 293
Cdd:cd05603 163 LAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRrrlgAK 242
                       250
                ....*....|...
gi 21359873 294 PTINELLNDEFFT 306
Cdd:cd05603 243 ADFLEIKNHVFFS 255
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
58-304 3.47e-34

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: 130.93  E-value: 3.47e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIV---PKSLLLKpHQREKMSMEISIHRSLAHQHVVGFHGFFED--NDFVFVVLEL 132
Cdd:cd06652   9 LLGQGAFGRVYLCYDADTGRELAVKQVqfdPESPETS-KEVNALECEIQLLKNLLHERIVQYYGCLRDpqERTLSIFMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE---YDGERKK 209
Cdd:cd06652  88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQticLSGTGMK 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETY-LRIKKNEYSIPKHINPVAASLIQKMLq 287
Cdd:cd06652 168 SVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWaEFEAMAAIFkIATQPTNPQLPAHVSDHCRDFLKRIF- 246
                       250
                ....*....|....*..
gi 21359873 288 TDPTARPTINELLNDEF 304
Cdd:cd06652 247 VEAKLRPSADELLRHTF 263
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
59-306 4.04e-34

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: 132.83  E-value: 4.04e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIV-PKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05602  15 IGKGSFGKVLLARHKSDEKFYAVKVLqKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATK-VEYDGErKKTLCGTPN 216
Cdd:cd05602  95 LFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKEnIEPNGT-TSTFCGTPE 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR--- 293
Cdd:cd05602 174 YLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRlga 253
                       250
                ....*....|....
gi 21359873 294 -PTINELLNDEFFT 306
Cdd:cd05602 254 kDDFTEIKNHIFFS 267
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
59-300 8.46e-34

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: 129.63  E-value: 8.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKslllkPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd14114  10 LGTGAFGVVHRCTERATGNNFAAKFIMT-----PHESDKETVrkEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN--EDLEVKIGDFGLATKVEYDgERKKTLCG 213
Cdd:cd14114  85 ELFErIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDPK-ESVKVTTG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTD 289
Cdd:cd14114 164 TAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDdsafSGISEEAKDFIRKLLLAD 243
                       250
                ....*....|.
gi 21359873 290 PTARPTINELL 300
Cdd:cd14114 244 PNKRMTIHQAL 254
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
59-301 8.90e-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: 129.38  E-value: 8.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLL-KPHQREKmsmEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14184   9 IGDGNFAVVKECVERSTGKEFALKIIDKAKCCgKEHLIEN---EVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE----DLEVKIGDFGLATKVE---YdgerkkT 210
Cdd:cd14184  86 LFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLATVVEgplY------T 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFET-SCLKETY---LRIKKNEYSIP--KHINPVAASLIQK 284
Cdd:cd14184 160 VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSeNNLQEDLfdqILLGKLEFPSPywDNITDSAKELISH 239
                       250
                ....*....|....*..
gi 21359873 285 MLQTDPTARPTINELLN 301
Cdd:cd14184 240 MLQVNVEARYTAEQILS 256
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
59-300 1.23e-33

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: 130.13  E-value: 1.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllkphqREKMSMEISIH-RSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14178  11 IGIGSYSVCKRCVHKATSTEYAVKIIDKS-------KRDPSEEIEILlRYGQHPNIITLKDVYDDGKFVYLVMELMRGGE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNED---LEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd14178  84 LLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNiLYMDESgnpESIRICDFGFAKQLRAENGLLMTPCY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFET---SCLKETYLRIKKNEYSIP----KHINPVAASLIQKML 286
Cdd:cd14178 164 TANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpdDTPEEILARIGSGKYALSggnwDSISDAAKDIVSKML 243
                       250
                ....*....|....
gi 21359873 287 QTDPTARPTINELL 300
Cdd:cd14178 244 HVDPHQRLTAPQVL 257
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
59-306 1.70e-33

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: 129.76  E-value: 1.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllkphqREKMSMEISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14175   9 IGVGSYSVCKRCVHKATNMEYAVKVIDKS-------KRDPSEEIEILLRYGqHPNIITLKDVYDDGKHVYLVTELMRGGE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNEDLE---VKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd14175  82 LLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNiLYVDESGNpesLRICDFGFAKQLRAENGLLMTPCY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFE---TSCLKETYLRIKKNEYSIP----KHINPVAASLIQKML 286
Cdd:cd14175 162 TANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSggnwNTVSDAAKDLVSKML 241
                       250       260
                ....*....|....*....|
gi 21359873 287 QTDPTARPTINELLNDEFFT 306
Cdd:cd14175 242 HVDPHQRLTAKQVLQHPWIT 261
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
59-293 1.73e-33

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: 130.81  E-value: 1.73e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIhRSLAHQHVVGFHGF--FEDNDFVFVVLELCRRR 136
Cdd:cd05619  13 LGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRV-LSLAWEHPFLTHLFctFQTKENLFFVMEYLNGG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd05619  92 DLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTSTFCGTPD 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05619 172 YIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLFVREPERR 248
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
58-304 2.09e-33

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: 128.87  E-value: 2.09e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADtKEVFAGKIVPkslLLKPHQREKMSM--EISIHRSLAHQ-HVVGF--HGFFEDNDFVFVVLEl 132
Cdd:cd14131   8 QLGKGGSSKVYKVLNPK-KKIYALKRVD---LEGADEQTLQSYknEIELLKKLKGSdRIIQLydYEVTDEDDYLYMVME- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLE-LHKRRKALTEPEA-RYYLRQIVLGCQYLHRNRVIHRDLKLGNlFLNEDLEVKIGDFGLATKVEYDGER--K 208
Cdd:cd14131  83 CGEIDLATiLKKKRPKPIDPNFiRYYWKQMLEAVHTIHEEGIVHSDLKPAN-FLLVKGRLKLIDFGIAKAIQNDTTSivR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTLCGTPNYIAPEVL---SKKGHSFEV-------DVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKKNEYSI--PKHIN 275
Cdd:cd14131 162 DSQVGTLNYMSPEAIkdtSASGEGKPKskigrpsDVWSLGCILYQMVYGKTPFqHITNPIAKLQAIIDPNHEIefPDIPN 241
                       250       260
                ....*....|....*....|....*....
gi 21359873 276 PVAASLIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd14131 242 PDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
59-307 3.46e-33

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: 128.61  E-value: 3.46e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS- 137
Cdd:cd06644  20 LGDGAFGKVYKAKNKETGALAAAKVIETK---SEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAv 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 ---LLELHKrrkALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd06644  97 daiMLELDR---GLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGT 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEV-----LSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNE---YSIPKHINPVAASLIQKML 286
Cdd:cd06644 174 PYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFLKTAL 253
                       250       260
                ....*....|....*....|.
gi 21359873 287 QTDPTARPTINELLNDEFFTS 307
Cdd:cd06644 254 DKHPETRPSAAQLLEHPFVSS 274
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
59-316 4.01e-33

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: 129.22  E-value: 4.01e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPhQREKMSMEISihrsLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANT-QREVAALRLC----QSHPNIVALHEVLHDQYHTYLVMELLRGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE---VKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd14180  89 LDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQTPCFTL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK-------ETYLRIKKNEYSIP----KHINPVAASLIQK 284
Cdd:cd14180 169 QYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEgeawKGVSEEAKDLVRG 248
                       250       260       270
                ....*....|....*....|....*....|..
gi 21359873 285 MLQTDPTARPTINELLNDEFFTSGYIPARLPI 316
Cdd:cd14180 249 LLTVDPAKRLKLSELRESDWLQGGSALSSTPL 280
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
59-300 4.01e-33

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: 127.54  E-value: 4.01e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKpHQREKMSMEISIHRSLAHQHVVGFH-GFFEDNDFVfVVLELCRRRS 137
Cdd:cd08220   8 VGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTK-EERQAALNEVKVLSMLHHPNIIEYYeSFLEDKALM-IVMEYAPGGT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKA--LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE-VKIGDFGLaTKVEYDGERKKTLCGT 214
Cdd:cd08220  86 LFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGI-SKILSSKSKAYTVVGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd08220 165 PCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHLILSMLHLDPNKR 244

                ....*..
gi 21359873 294 PTINELL 300
Cdd:cd08220 245 PTLSEIM 251
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
59-305 4.83e-33

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: 127.16  E-value: 4.83e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSmEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd08221   8 LGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALN-EIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE--LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd08221  87 HDkiAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESIVGTPY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYsipKHINPVAA----SLIQKMLQTDPTA 292
Cdd:cd08221 167 YMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEY---EDIDEQYSeeiiQLVHDCLHQDPED 243
                       250
                ....*....|...
gi 21359873 293 RPTINELLNDEFF 305
Cdd:cd08221 244 RPTAEELLERPLL 256
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
96-299 5.63e-33

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: 128.16  E-value: 5.63e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  96 EKMSMEISIHRSLAHQHVVGFHGFFED--NDFVFVVLELCRRRSLLELhKRRKALTEPEARYYLRQIVLGCQYLHRNRVI 173
Cdd:cd14199  70 ERVYQEIAILKKLDHPNVVKLVEVLDDpsEDHLYMVFELVKQGPVMEV-PTLKPLSEDQARFYFQDLIKGIEYLHYQKII 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFE---VDVWSIGCIMYTLLVGKPP 250
Cdd:cd14199 149 HRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRKIFSgkaLDVWAMGVTLYCFVFGQCP 228
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21359873 251 FETSCLKETYLRIKKNEYSIPKH--INPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd14199 229 FMDERILSLHSKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRISVPEI 279
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
58-305 5.65e-33

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: 127.43  E-value: 5.65e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEV-FAGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd14202   9 LIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAK--SQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN---------EDLEVKIGDFGLATKVEyDGER 207
Cdd:cd14202  87 DLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFARYLQ-NNMM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 KKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY---SIPKHINPVAASLIQK 284
Cdd:cd14202 166 AATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSlspNIPRETSSHLRQLLLG 245
                       250       260
                ....*....|....*....|.
gi 21359873 285 MLQTDPTARPTINELLNDEFF 305
Cdd:cd14202 246 LLQRNQKDRMDFDEFFHHPFL 266
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
98-305 6.35e-33

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: 127.43  E-value: 6.35e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  98 MSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDL 177
Cdd:cd14201  52 LGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDL 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 178 KLGNLFLN---------EDLEVKIGDFGLATKVEYDgERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGK 248
Cdd:cd14201 132 KPQNILLSyasrkkssvSGIRIKIADFGFARYLQSN-MMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGK 210
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 249 PPFETSCLKETYLRIKKNEY---SIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14201 211 PPFQANSPQDLRMFYEKNKNlqpSIPRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
59-305 9.38e-33

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: 126.57  E-value: 9.38e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADT-KEVFAGKIVPKSLLlkPHQREKMSMEISIHRSLAHQHVVGFHGFFED---NDFVFVVlELCR 134
Cdd:cd13983   9 LGRGSFKTVYRAFDTEEgIEVAWNEIKLRKLP--KAERQRFKQEIEILKSLKHPNIIKFYDSWESkskKEVIFIT-ELMT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHrNR---VIHRDLKLGNLFLNEDL-EVKIGDFGLATKVEYDgeRKKT 210
Cdd:cd13983  86 SGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLH-TRdppIIHRDLKCDNIFINGNTgEVKIGDLGLATLLRQS--FAKS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKK-GHSfeVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKKNEY--SIPKHINPVAASLIQKML 286
Cdd:cd13983 163 VIGTPEFMAPEMYEEHyDEK--VDIYAFGMCLLEMATGEYPYsECTNAAQIYKKVTSGIKpeSLSKVKDPELKDFIEKCL 240
                       250
                ....*....|....*....
gi 21359873 287 QTdPTARPTINELLNDEFF 305
Cdd:cd13983 241 KP-PDERPSARELLEHPFF 258
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
58-304 3.00e-32

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: 125.52  E-value: 3.00e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREK------MSMEISIHRSLAHQHVVGFHGFFEDND----FVF 127
Cdd:cd06653   9 LLGRGAFGEVYLCYDADTGRELAVKQVP----FDPDSQETskevnaLECEIQLLKNLRHDRIVQYYGCLRDPEekklSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 128 VvlELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE---YD 204
Cdd:cd06653  85 V--EYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQticMS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETY-LRIKKNEYSIPKHINPVAASLI 282
Cdd:cd06653 163 GTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWaEYEAMAAIFkIATQPTKPQLPDGVSDACRDFL 242
                       250       260
                ....*....|....*....|..
gi 21359873 283 QKMLqTDPTARPTINELLNDEF 304
Cdd:cd06653 243 RQIF-VEEKRRPTAEFLLRHPF 263
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
99-305 3.14e-32

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: 125.46  E-value: 3.14e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  99 SMEISIHR-SLAHQHVVGFHGFFEDNDFVFVVLELCRRrSLLEL--HKRRKALTE---PEARYYLRQIVLGCQYLHRNRV 172
Cdd:cd13982  42 DREVQLLReSDEHPNVIRYFCTEKDRQFLYIALELCAA-SLQDLveSPRESKLFLrpgLEPVRLLRQIASGLAHLHSLNI 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 173 IHRDLKLGNLFLNED-----LEVKIGDFGLATKVEYDGE---RKKTLCGTPNYIAPEVLS---KKGHSFEVDVWSIGCIM 241
Cdd:cd13982 121 VHRDLKPQNILISTPnahgnVRAMISDFGLCKKLDVGRSsfsRRSGVAGTSGWIAPEMLSgstKRRQTRAVDIFSLGCVF 200
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 242 -YTLLVGKPPFETSCLKETylRIKKNEYSIPK-----HINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd13982 201 yYVLSGGSHPFGDKLEREA--NILKGKYSLDKllslgEHGPEAQDLIERMIDFDPEKRPSAEEVLNHPFF 268
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
59-305 3.28e-32

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: 128.23  E-value: 3.28e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC---RR 135
Cdd:cd05600  19 VGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVpggDF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKrrkALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAT------KVE------- 202
Cdd:cd05600  99 RTLLNNSG---ILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtlspkKIEsmkirle 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 203 ------------------------YDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKE 258
Cdd:cd05600 176 evkntafleltakerrniyramrkEDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGSTPNE 255
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 259 TYL----------RIKKNEYSIPKHINPVAASLIQKMLqTDPTAR-PTINELLNDEFF 305
Cdd:cd05600 256 TWAnlyhwkktlqRPVYTDPDLEFNLSDEAWDLITKLI-TDPQDRlQSPEQIKNHPFF 312
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
60-304 3.34e-32

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: 125.49  E-value: 3.34e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  60 GKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREKMSMEISIHRSLAHQH-VVGFHGFF------EDNDFVFVVLEL 132
Cdd:cd06608  15 GEGTYGKVYKARHKKTGQLAAIKIMD----IIEDEEEEIKLEINILRKFSNHPnIATFYGAFikkdppGGDDQLWLVMEY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLEL----HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERK 208
Cdd:cd06608  91 CGGGSVTDLvkglRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQLDSTLGRR 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTLCGTPNYIAPEVLSKK-----GHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASL-- 281
Cdd:cd06608 171 NTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKSPEKWSKEFnd 250
                       250       260
                ....*....|....*....|....
gi 21359873 282 -IQKMLQTDPTARPTINELLNDEF 304
Cdd:cd06608 251 fISECLIKNYEQRPFTEELLEHPF 274
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
58-303 4.45e-32

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: 125.17  E-value: 4.45e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFA---KCFEISDADTKEVFAGKIVPKSLLLKphqreKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd14046  13 VLGKGAFGqvvKVRNKLDGRYYAIKKIKLRSESKNNS-----RILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTL--- 211
Cdd:cd14046  88 KSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVELATQDink 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 ---------------CGTPNYIAPEVLSKKGHSFE--VDVWSIGCIMYTLLVgkpPFETSCLKE---TYLRIKKNEY--S 269
Cdd:cd14046 168 stsaalgssgdltgnVGTALYVAPEVQSGTKSTYNekVDMYSLGIIFFEMCY---PFSTGMERVqilTALRSVSIEFppD 244
                       250       260       270
                ....*....|....*....|....*....|....
gi 21359873 270 IPKHINPVAASLIQKMLQTDPTARPTINELLNDE 303
Cdd:cd14046 245 FDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKSE 278
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
59-300 4.76e-32

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: 124.42  E-value: 4.76e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLkPHQREKMSMEISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd13997   8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRG-PKERARALREVEAHAALGqHPNIVRYYSSWEEGGHLYIQMELCENGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 L---LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKtlcGT 214
Cdd:cd13997  87 LqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEE---GD 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLS-KKGHSFEVDVWSIGCIMYTLLVGKpPFETSCLKETYLRIKKneysIPKHINPVA----ASLIQKMLQTD 289
Cdd:cd13997 164 SRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGE-PLPRNGQQWQQLRQGK----LPLPPGLVLsqelTRLLKVMLDPD 238
                       250
                ....*....|.
gi 21359873 290 PTARPTINELL 300
Cdd:cd13997 239 PTRRPTADQLL 249
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
59-306 4.93e-32

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: 125.51  E-value: 4.93e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllkphqREKMSMEISI-HRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14177  12 IGVGSYSVCKRCIHRATNMEFAVKIIDKS-------KRDPSEEIEIlMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL----EVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd14177  85 LLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFAKQLRGENGLLLTPCY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFE---TSCLKETYLRIKKNEYSIP----KHINPVAASLIQKML 286
Cdd:cd14177 165 TANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSggnwDTVSDAAKDLLSHML 244
                       250       260
                ....*....|....*....|
gi 21359873 287 QTDPTARPTINELLNDEFFT 306
Cdd:cd14177 245 HVDPHQRYTAEQVLKHSWIA 264
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
59-307 5.09e-32

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: 126.27  E-value: 5.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05601   9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKA-LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE-RKKTLCGTPN 216
Cdd:cd05601  89 LSLLSRYDDiFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTvTSKMPVGTPD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVL------SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIPKH--INPVAASLIQKML 286
Cdd:cd05601 169 YIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNImnFKKFLKFPEDpkVSESAVDLIKGLL 248
                       250       260
                ....*....|....*....|.
gi 21359873 287 qTDPTARPTINELLNDEFFTS 307
Cdd:cd05601 249 -TDAKERLGYEGLCCHPFFSG 268
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
59-293 7.55e-32

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: 124.56  E-value: 7.55e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRI-KKKKGETMALnEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLE--LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd05577  80 LKYhiYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFK-GGKKIKGRVGTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKK-GHSFEVDVWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDP 290
Cdd:cd05577 159 GYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFrqrkEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDP 238

                ...
gi 21359873 291 TAR 293
Cdd:cd05577 239 ERR 241
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
59-336 9.45e-32

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: 125.38  E-value: 9.45e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd05585  82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTPEYL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN- 297
Cdd:cd05585 162 APELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGYNg 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 21359873 298 --ELLNDEFFTSgyIPARLPITCLTIPPRFSIAPSSLDPSN 336
Cdd:cd05585 242 aqEIKNHPFFDQ--IDWKRLLMKKIQPPFKPAVENAIDTSN 280
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
59-300 4.47e-31

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: 123.98  E-value: 4.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllkphqREKMSMEISIH-RSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14176  27 IGVGSYSVCKRCIHKATNMEFAVKIIDKS-------KRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNED---LEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd14176 100 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNiLYVDESgnpESIRICDFGFAKQLRAENGLLMTPCY 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFET---SCLKETYLRIKKNEYSIP----KHINPVAASLIQKML 286
Cdd:cd14176 180 TANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKML 259
                       250
                ....*....|....
gi 21359873 287 QTDPTARPTINELL 300
Cdd:cd14176 260 HVDPHQRLTAALVL 273
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
58-307 4.69e-31

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: 122.68  E-value: 4.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKslllkphQREKMSM---------EISIHRSLAHQHVVGFHGFFEDNDFVFV 128
Cdd:cd07841   7 KLGEGTYAVVYKARDKETGRIVAIKKIKL-------GERKEAKdginftalrEIKLLQELKHPNIIGLLDVFGHKSNINL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 129 VLELCRrrSLLE--LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE 206
Cdd:cd07841  80 VFEFME--TDLEkvIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPNR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 RKKTLCGTPNYIAPEVL--SKKgHSFEVDVWSIGCIMYTLLVGKP--------------------PFET-----SCLKeT 259
Cdd:cd07841 158 KMTHQVVTRWYRAPELLfgARH-YGVGVDMWSVGCIFAELLLRVPflpgdsdidqlgkifealgtPTEEnwpgvTSLP-D 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 21359873 260 YLRIKKNEYSIPKHINPvAAS-----LIQKMLQTDPTARPTINELLNDEFFTS 307
Cdd:cd07841 236 YVEFKPFPPTPLKQIFP-AASddaldLLQRLLTLNPNKRITARQALEHPYFSN 287
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
62-293 4.72e-31

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: 122.51  E-value: 4.72e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  62 GGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLEL 141
Cdd:cd05609  11 GAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDCATL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 142 HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA-------TKVEYDG--ERK---- 208
Cdd:cd05609  91 LKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkiglmslTTNLYEGhiEKDtref 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 --KTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKH---INPVAASLIQ 283
Cdd:cd05609 171 ldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGddaLPDDAQDLIT 250
                       250
                ....*....|
gi 21359873 284 KMLQTDPTAR 293
Cdd:cd05609 251 RLLQQNPLER 260
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-306 7.38e-31

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: 122.24  E-value: 7.38e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLllkphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14085  11 LGRGATSVVYRCRQKGTQKPYAVKKLKKTV-----DKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLF---LNEDLEVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd14085  86 FDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGLSKIVD-QQVTMKTVCGTP 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKKNEYSIPK----HINPVAASLIQKMLQTDP 290
Cdd:cd14085 165 GYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFyDERGDQYMFKRILNCDYDFVSpwwdDVSLNAKDLVKKLIVLDP 244
                       250
                ....*....|....*.
gi 21359873 291 TARPTINELLNDEFFT 306
Cdd:cd14085 245 KKRLTTQQALQHPWVT 260
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
59-304 7.56e-31

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: 122.02  E-value: 7.56e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIV-PKSLLlkphqREKMSMEISIHRSLA-HQHVVGFHGFFEDNDF-----VFVVLE 131
Cdd:cd06639  30 IGKGTYGKVYKVTNKKDGSLAAVKILdPISDV-----DEEIEAEYNILRSLPnHPNVVKFYGMFYKADQyvggqLWLVLE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRRSLLELHK----RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGER 207
Cdd:cd06639 105 LCNGGSVTELVKgllkCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSARLR 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 KKTLCGTPNYIAPEVLS---KKGHSFEV--DVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNeySIPKHINPVA---- 278
Cdd:cd06639 185 RNTSVGTPFWMAPEVIAceqQYDYSYDArcDVWSLGITAIELADGDPPLFDMHPVKALFKIPRN--PPPTLLNPEKwcrg 262
                       250       260
                ....*....|....*....|....*..
gi 21359873 279 -ASLIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd06639 263 fSHFISQCLIKDFEKRPSVTHLLEHPF 289
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
58-301 9.90e-31

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: 121.75  E-value: 9.90e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKMSMEISI-HRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd14090   9 LLGEGAYASVQTCINLYTGKEYAVKIIEKH---PGHSRSRVFREVETlHQCQGHPNILQLIEYFEDDERFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLF---LNEDLEVKIGDFGLATKVEYDGERKK---- 209
Cdd:cd14090  86 PLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGSGIKLSSTSMTpvtt 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 ----TLCGTPNYIAPEVL---SKKGHSFE--VDVWSIGCIMYTLLVGKPPFETSCLKET---------------YLRIKK 265
Cdd:cd14090 166 pellTPVGSAEYMAPEVVdafVGEALSYDkrCDLWSLGVILYIMLCGYPPFYGRCGEDCgwdrgeacqdcqellFHSIQE 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21359873 266 NEYSIP----KHINPVAASLIQKMLQTDPTARPTINELLN 301
Cdd:cd14090 246 GEYEFPekewSHISAEAKDLISHLLVRDASQRYTAEQVLQ 285
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
59-300 1.25e-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: 120.60  E-value: 1.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKsLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRrSL 138
Cdd:cd14082  11 LGSGQFGIVYGGKHRKTGRDVAIKVIDK-LRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHG-DM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE--LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL---EVKIGDFGLATKVeydGER--KKTL 211
Cdd:cd14082  89 LEmiLSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARII---GEKsfRRSV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKEtylRIKKNEYSIP----KHINPVAASLIQKML 286
Cdd:cd14082 166 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIND---QIQNAAFMYPpnpwKEISPDAIDLINNLL 242
                       250
                ....*....|....
gi 21359873 287 QTDPTARPTINELL 300
Cdd:cd14082 243 QVKMRKRYSVDKSL 256
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
59-286 1.29e-30

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: 124.35  E-value: 1.29e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05624  80 IGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDL 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LEL-HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLC-GTPN 216
Cdd:cd05624 160 LTLlSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQSSVAvGTPD 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSF-----EVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNE--YSIPKHINPV---AASLIQKML 286
Cdd:cd05624 240 YISPEILQAMEDGMgkygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEerFQFPSHVTDVseeAKDLIQRLI 319
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
59-305 1.77e-30

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: 120.01  E-value: 1.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREkmsmEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRrSL 138
Cdd:cd14108  10 IGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARR----ELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE-EL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE--VKIGDFGLATKVEyDGERKKTLCGTPN 216
Cdd:cd14108  85 LERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQELT-PNEPQYCKYGTPE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKN----EYSIPKHINPVAASLIQKMLQTDpTA 292
Cdd:cd14108 164 FVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYnvafEESMFKDLCREAKGFIIKVLVSD-RL 242
                       250
                ....*....|...
gi 21359873 293 RPTINELLNDEFF 305
Cdd:cd14108 243 RPDAEETLEHPWF 255
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
59-300 2.16e-30

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: 120.11  E-value: 2.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14191  10 LGSGKFGQVFRLVEKKTKKVWAGKFF-KAYSAK--EKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLF-LNED-LEVKIGDFGLATKVEYDGERKkTLCGTP 215
Cdd:cd14191  87 FErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTKIKLIDFGLARRLENAGSLK-VLFGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTDPT 291
Cdd:cd14191 166 EFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKKDMK 245

                ....*....
gi 21359873 292 ARPTINELL 300
Cdd:cd14191 246 ARLTCTQCL 254
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
58-304 2.57e-30

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: 120.19  E-value: 2.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIV---PKSlllkPHQREKMSM---EISIHRSLAHQHVVGFHGFFEDN--DFVFVV 129
Cdd:cd06651  14 LLGQGAFGRVYLCYDVDTGRELAAKQVqfdPES----PETSKEVSAlecEIQLLKNLQHERIVQYYGCLRDRaeKTLTIF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE---YDGE 206
Cdd:cd06651  90 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticMSGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 RKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIPKHINPVAASLIQK 284
Cdd:cd06651 170 GIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatQPTNPQLPSHISEHARDFLGC 249
                       250       260
                ....*....|....*....|
gi 21359873 285 MLqTDPTARPTINELLNDEF 304
Cdd:cd06651 250 IF-VEARHRPSAEELLRHPF 268
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
59-293 2.71e-30

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: 120.37  E-value: 2.71e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR---- 134
Cdd:cd05608   9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNggdl 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd05608  89 RYHIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTKGYAGT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDP 290
Cdd:cd05608 169 PGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFrargEKVENKELKQRILNDSVTYSEKFSPASKSICEALLAKDP 248

                ...
gi 21359873 291 TAR 293
Cdd:cd05608 249 EKR 251
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
59-301 2.72e-30

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: 119.76  E-value: 2.72e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLL----LKPHQREKMSMEISIHRSL-AHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd13993   8 IGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPnskdGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIYIVLEYC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLEL-HKRRKALTEPE-ARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED-LEVKIGDFGLATKVEYDGERKkt 210
Cdd:cd13993  88 PNGDLFEAiTENRIYVGKTElIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLATTEKISMDFG-- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 lCGTPNYIAPEVLSKKGHSFE------VDVWSIGCIMYTLLVGKPPFETSCLKE-TYLRIKKNEYSIPKHINPVAA---S 280
Cdd:cd13993 166 -VGSEFYMAPECFDEVGRSLKgypcaaGDIWSLGIILLNLTFGRNPWKIASESDpIFYDYYLNSPNLFDVILPMSDdfyN 244
                       250       260
                ....*....|....*....|.
gi 21359873 281 LIQKMLQTDPTARPTINELLN 301
Cdd:cd13993 245 LLRQIFTVNPNNRILLPELQL 265
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
59-305 3.19e-30

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: 119.26  E-value: 3.19e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISD-ADTKEVfAGKIVPKSlllkpHQRE--------KMSMEISIHR---SLAHQHVVGFHGFFEDNDFV 126
Cdd:cd14005   8 LGKGGFGTVYSGVRiRDGLPV-AVKFVPKS-----RVTEwamingpvPVPLEIALLLkasKPGVPGVIRLLDWYERPDGF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 127 FVVLElcrRRS----LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN-EDLEVKIGDFGLATKV 201
Cdd:cd14005  82 LLIME---RPEpcqdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGALL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 202 EydGERKKTLCGTPNYIAPE-VLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSclketyLRIKKNEYSIPKHINPVAAS 280
Cdd:cd14005 159 K--DSVYTDFDGTRVYSPPEwIRHGRYHGRPATVWSLGILLYDMLCGDIPFEND------EQILRGNVLFRPRLSKECCD 230
                       250       260
                ....*....|....*....|....*
gi 21359873 281 LIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14005 231 LISRCLQFDPSKRPSLEQILSHPWF 255
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
59-304 3.50e-30

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: 119.08  E-value: 3.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEIS-DADTKEVfagkIVPKSLLLKPHQREKMS--MEISIHRSLAHQHVVGFHGFFEDND-FVFVVLELCR 134
Cdd:cd08223   8 IGKGSYGEVWLVRhKRDRKQY----VIKKLNLKNASKRERKAaeQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGFCE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARY--YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLC 212
Cdd:cd08223  84 GGDLYTRLKEQKGVLLEERQVveWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMATTLI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 213 GTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY-SIPKHINPVAASLIQKMLQTDPT 291
Cdd:cd08223 164 GTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIKAMLHQDPE 243
                       250
                ....*....|...
gi 21359873 292 ARPTINELLNDEF 304
Cdd:cd08223 244 KRPSVKRILRQPY 256
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
59-306 3.50e-30

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: 119.78  E-value: 3.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06642  12 IGKGSFGEVYKGIDNRTKEVVAIKII--DLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRrKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd06642  90 LDLLKP-GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWM 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd06642 169 APEVIKQSAYDFKADIWSLGITAIELAKGEPPNsDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDPRFRPTAK 248

                ....*....
gi 21359873 298 ELLNDEFFT 306
Cdd:cd06642 249 ELLKHKFIT 257
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
58-304 4.19e-30

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: 120.34  E-value: 4.19e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPH--QREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14094  10 VIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSL-LELHKRRKA---LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKVEYDGERK 208
Cdd:cd14094  90 ADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGLVA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSClKETYLRIKKNEYSI----PKHINPVAASLIQK 284
Cdd:cd14094 170 GGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnprqWSHISESAKDLVRR 248
                       250       260
                ....*....|....*....|
gi 21359873 285 MLQTDPTARPTINELLNDEF 304
Cdd:cd14094 249 MLMLDPAERITVYEALNHPW 268
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
59-293 6.87e-30

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 120.47  E-value: 6.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   59 LGKGGFAKCF--EISDADTKEVfAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:PTZ00426  38 LGTGSFGRVIlaTYKNEDFPPV-AIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydgERKKTLCGTPN 216
Cdd:PTZ00426 117 EFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD---TRTYTLCGTPE 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873  217 YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:PTZ00426 194 YIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLTKR 270
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
58-320 7.71e-30

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 120.25  E-value: 7.71e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLK--PHQREKMSM---------EISIHRSLAHQHVVGFHGFFEDNDFV 126
Cdd:PTZ00024  16 HLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNdvTKDRQLVGMcgihfttlrELKIMNEIKHENIMGLVDVYVEGDFI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  127 FVVLELcRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDG- 205
Cdd:PTZ00024  96 NLVMDI-MASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGYPPy 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  206 ----ERKKTLCGTPN---------YIAPEVL--SKKGHsFEVDVWSIGCIMYTLLVGKPPF------------------- 251
Cdd:PTZ00024 175 sdtlSKDETMQRREEmtskvvtlwYRAPELLmgAEKYH-FAVDMWSVGCIFAELLTGKPLFpgeneidqlgrifellgtp 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  252 ------ETSCLK---ETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYI---PARLPITCL 319
Cdd:PTZ00024 254 nednwpQAKKLPlytEFTPRKPKDLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKSDPLpcdPSQLPFNFL 333

                 .
gi 21359873  320 T 320
Cdd:PTZ00024 334 T 334
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
59-305 8.38e-30

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: 118.79  E-value: 8.38e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLllkPHQREKMSM-EISIHRSL-AHQHVVGFHGFFEDNDFVFVVLELCRRr 136
Cdd:cd07830   7 LGDGTFGSVYLARNKETGELVAIKKMKKKF---YSWEECMNLrEVKSLRKLnEHPNIVKLKEVFRENDELYFVFEYMEG- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydgERK--KTLC 212
Cdd:cd07830  83 NLYQLMKDRkgKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIR---SRPpyTDYV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 213 GTPNYIAPEVLSKKG-HSFEVDVWSIGCIMYTLLVGKPPF----ETSCL---------------KETYLRIKKNEYSIPK 272
Cdd:cd07830 160 STRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFpgssEIDQLykicsvlgtptkqdwPEGYKLASKLGFRFPQ 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21359873 273 -----------HINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07830 240 faptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
59-307 1.30e-29

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: 117.79  E-value: 1.30e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKM-SMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14183  14 IGDGNFAVVKECVERSTGREYALKIINKS---KCRGKEHMiQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE----VKIGDFGLATKVeyDGERKkTLCG 213
Cdd:cd14183  91 LFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDgsksLKLGDFGLATVV--DGPLY-TVCG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYL----RIKKNEYSIP--KHINPVAASLIQKMLQ 287
Cdd:cd14183 168 TPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLfdqiLMGQVDFPSPywDNVSDSAKELITMMLQ 247
                       250       260
                ....*....|....*....|
gi 21359873 288 TDPTARPTINELLNDEFFTS 307
Cdd:cd14183 248 VDVDQRYSALQVLEHPWVND 267
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
59-293 1.39e-29

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: 118.20  E-value: 1.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRI-KKRKGEAMALnEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLE--LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd05630  87 LKFhiYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVP-EGQTIKGRVGTV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK------ETYLRIKKNEYSipKHINPVAASLIQKMLQTD 289
Cdd:cd05630 166 GYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKikreevERLVKEVPEEYS--EKFSPQARSLCSMLLCKD 243

                ....
gi 21359873 290 PTAR 293
Cdd:cd05630 244 PAER 247
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
59-301 2.49e-29

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: 117.01  E-value: 2.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkslllkpHQREKMSMEISIH-RSLAHQHVVGFHGFFED----NDFVFVVLELC 133
Cdd:cd14172  12 LGLGVNGKVLECFHRRTGQKCALKLL--------YDSPKARREVEHHwRASGGPHIVHILDVYENmhhgKRCLLIIMECM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKVEYDGERK 208
Cdd:cd14172  84 EGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTVQNALQ 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 kTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSC-------LKEtylRIKKNEYSIPK----HINPV 277
Cdd:cd14172 164 -TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTgqaispgMKR---RIRMGQYGFPNpewaEVSEE 239
                       250       260
                ....*....|....*....|....
gi 21359873 278 AASLIQKMLQTDPTARPTINELLN 301
Cdd:cd14172 240 AKQLIRHLLKTDPTERMTITQFMN 263
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
59-300 2.56e-29

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: 117.21  E-value: 2.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPkslllkpHQREKMSMEISIHRSLAHQHVVGFHGFFEDND-------------- 124
Cdd:cd14047  14 IGSGGFGQVFKAKHRIDGKTYAIKRVK-------LNNEKAEREVKALAKLDHPNIVRYNGCWDGFDydpetsssnssrsk 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 --FVFVVLELCRRRSLLE-LHKRRKALTEP-EARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATK 200
Cdd:cd14047  87 tkCLFIQMEFCEKGTLESwIEKRNGEKLDKvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLVTS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 201 VEYDGERKKTLcGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPFETsclKETYLRIKKNEysIPKHIN---P 276
Cdd:cd14047 167 LKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLhVCDSAFEK---SKFWTDLRNGI--LPDIFDkryK 240
                       250       260
                ....*....|....*....|....
gi 21359873 277 VAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14047 241 IEKTIIKKMLSKKPEDRPNASEIL 264
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
59-300 3.94e-29

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: 116.57  E-value: 3.94e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFA---KCFEisdADTKEVFAGKivpksLLLKPHQREKMSMEIsIHR------SLAHQHVVGFHGFFEDNDFVFVV 129
Cdd:cd14197  17 LGRGKFAvvrKCVE---KDSGKEFAAK-----FMRKRRKGQDCRMEI-IHEiavlelAQANPWVINLHEVYETASEMILV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSLLE--LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL---EVKIGDFGLaTKVEYD 204
Cdd:cd14197  88 LEYAAGGEIFNqcVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGL-SRILKN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAAS 280
Cdd:cd14197 167 SEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSeeefEHLSESAID 246
                       250       260
                ....*....|....*....|
gi 21359873 281 LIQKMLQTDPTARPTINELL 300
Cdd:cd14197 247 FIKTLLIKKPENRATAEDCL 266
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
59-304 4.08e-29

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: 117.03  E-value: 4.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIvpksllLKP-HQ-REKMSMEISIHRSLA-HQHVVGFHGFF-----EDNDFVFVVL 130
Cdd:cd06638  26 IGKGTYGKVFKVLNKKNGSKAAVKI------LDPiHDiDEEIEAEYNILKALSdHPNVVKFYGMYykkdvKNGDQLWLVL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 131 ELCRRRSLLELHK----RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE 206
Cdd:cd06638 100 ELCNGGSVTDLVKgflkRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRL 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 RKKTLCGTPNYIAPEVLS-----KKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNeySIPKHINPVAAS- 280
Cdd:cd06638 180 RRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRN--PPPTLHQPELWSn 257
                       250       260
                ....*....|....*....|....*...
gi 21359873 281 ----LIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd06638 258 efndFIRKCLTKDYEKRPTVSDLLQHVF 285
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
59-305 4.12e-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. 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: 117.03  E-value: 4.12e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGK---IVPKSlllkPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd07833   9 VGEGAYGVVLKCRNKATGEIVAIKkfkESEDD----EDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKT-LCGT 214
Cdd:cd07833  85 TLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASPLTdYVAT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPPFE-TSCLKETYL--------------RIKKN------------ 266
Cdd:cd07833 165 RWYRAPELLvGDTNYGKPVDVWAIGCIMAELLDGEPLFPgDSDIDQLYLiqkclgplppshqeLFSSNprfagvafpeps 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21359873 267 -----EYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07833 245 qpeslERRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
101-340 5.70e-29

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: 117.86  E-value: 5.70e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGF--------FEDndfVFVVLELCRRrsllELH---KRRKALTEPEARYYLRQIVLGCQYLHR 169
Cdd:cd07858  54 EIKLLRHLDHENVIAIKDImppphreaFND---VYIVYELMDT----DLHqiiRSSQTLSDDHCQYFLYQLLRGLKYIHS 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 170 NRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGK 248
Cdd:cd07858 127 ANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDFMTEYVVTRWYRAPELlLNCSEYTTAIDVWSVGCIFAELLGRK 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 249 PPFE-TSCLKETYLRI-----------------KKNEY--SIPK-----------HINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd07858 207 PLFPgKDYVHQLKLITellgspseedlgfirneKARRYirSLPYtprqsfarlfpHANPLAIDLLEKMLVFDPSKRITVE 286
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21359873 298 ELLNDEFFTSGYIPARLPItCLTiPPRFSIAPSSLDPSNRKPL 340
Cdd:cd07858 287 EALAHPYLASLHDPSDEPV-CQT-PFSFDFEEDALTEEDIKEL 327
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
59-251 6.19e-29

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: 116.66  E-value: 6.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKivpKSLLLKPHQREKMSM--EI-SIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd07832   8 IGEGAHGIVFKAKDRETGETVALK---KVALRKLEGGIPNQAlrEIkALQACQGHPYVVKLRDVFPHGTGFVLVFEYMLS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 rSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKT-LCG 213
Cdd:cd07832  85 -SLSEvLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPRLYShQVA 163
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21359873 214 TPNYIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd07832 164 TRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNGSPLF 202
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
59-293 7.13e-29

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: 116.30  E-value: 7.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQrEKMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05605   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKG-EAMALnEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 L-LELHK-RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd05605  87 LkFHIYNmGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIP-EGETIRGRVGTV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK----ETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPT 291
Cdd:cd05605 166 GYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKvkreEVDRRVKEDQEEYSEKFSEEAKSICSQLLQKDPK 245

                ..
gi 21359873 292 AR 293
Cdd:cd05605 246 TR 247
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
59-305 9.25e-29

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: 115.30  E-value: 9.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKslllkphqREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14109  12 EKRAAQGAPFHVTERSTGRNFLAQLRYG--------DPFLMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 L---ELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDlEVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd14109  84 LvrdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQSRRLL-RGKLTTLIYGSP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY----SIPKHINPVAASLIQKMLQTDPT 291
Cdd:cd14109 162 EFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWsfdsSPLGNISDDARDFIKKLLVYIPE 241
                       250
                ....*....|....
gi 21359873 292 ARPTINELLNDEFF 305
Cdd:cd14109 242 SRLTVDEALNHPWF 255
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
59-304 9.99e-29

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: 115.55  E-value: 9.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06641  12 IGKGSFGEVFKGIDNRTQKVVAIKII--DLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRrKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd06641  90 LDLLEP-GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FVGTPFWM 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd06641 169 APEVIKQSAYDSKADIWSLGITAIELARGEPPHsELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAK 248

                ....*..
gi 21359873 298 ELLNDEF 304
Cdd:cd06641 249 ELLKHKF 255
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
58-305 1.07e-28

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: 117.01  E-value: 1.07e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKivpKslLLKPHQRE----KMSMEISIHRSLAHQHVVG----FHGFFEDNDF--VF 127
Cdd:cd07851  22 PVGSGAYGQVCSAFDTKTGRKVAIK---K--LSRPFQSAihakRTYRELRLLKHMKHENVIGlldvFTPASSLEDFqdVY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 128 VVLELCRRrsllELHK--RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydg 205
Cdd:cd07851  97 LVTHLMGA----DLNNivKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTD--- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 ERKKTLCGTPNYIAPEVLSKKGH-SFEVDVWSIGCIMYTLLVGKPPFE--------------TSCLKETYL-RIKKNE-- 267
Cdd:cd07851 170 DEMTGYVATRWYRAPEIMLNWMHyNQTVDIWSVGCIMAELLTGKTLFPgsdhidqlkrimnlVGTPDEELLkKISSESar 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 21359873 268 -Y--SIPKH-----------INPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07851 250 nYiqSLPQMpkkdfkevfsgANPLAIDLLEKMLVLDPDKRITAAEALAHPYL 301
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
59-305 1.28e-28

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: 117.09  E-value: 1.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKP-------HQREKMSMEISihrslahQHVVGFHGFFEDNDFVFVVLE 131
Cdd:cd05596  34 IGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRsdsaffwEERDIMAHANS-------EWIVQLHYAFQDDKYLYMVMD 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRRSLLELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE-RKKT 210
Cdd:cd05596 107 YMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDGLvRSDT 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKKGH----SFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIPK--HINPVAASLI 282
Cdd:cd05596 186 AVGTPDYISPEVLKSQGGdgvyGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKImnHKNSLQFPDdvEISKDAKSLI 265
                       250       260
                ....*....|....*....|....*
gi 21359873 283 QKML--QTDPTARPTINELLNDEFF 305
Cdd:cd05596 266 CAFLtdREVRLGRNGIEEIKAHPFF 290
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
59-300 2.47e-28

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: 114.74  E-value: 2.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKslllKP-HQREKMSMEIS-IHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd14173  10 LGEGAYARVQTCINLITNKEYAVKIIEK----RPgHSRSRVFREVEmLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKVEYDGERKK---- 209
Cdd:cd14173  86 SILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLGSGIKLNSDCSPistp 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 ---TLCGTPNYIAPEVLSKKGHSFEV-----DVWSIGCIMYTLLVGKPPFE---------------TSCLKETYLRIKKN 266
Cdd:cd14173 166 ellTPCGSAEYMAPEVVEAFNEEASIydkrcDLWSLGVILYIMLSGYPPFVgrcgsdcgwdrgeacPACQNMLFESIQEG 245
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21359873 267 EYSIPK----HINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14173 246 KYEFPEkdwaHISCAAKDLISKLLVRDAKQRLSAAQVL 283
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
59-285 2.66e-28

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: 117.03  E-value: 2.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05626   9 LGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGDM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD-------------- 204
Cdd:cd05626  89 MSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWThnskyyqkgshirq 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 -----------------GERKKTL----------------CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd05626 169 dsmepsdlwddvsncrcGDRLKTLeqratkqhqrclahslVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPF 248
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21359873 252 ETSCLKETYLRIK--KNEYSIPKHI--NPVAASLIQKM 285
Cdd:cd05626 249 LAPTPTETQLKVInwENTLHIPPQVklSPEAVDLITKL 286
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
64-304 3.23e-28

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: 113.97  E-value: 3.23e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  64 FAKCFEISDADTKEVFAGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHK 143
Cdd:cd14088  14 FCEIFRAKDKTTGKLYTCKKFLKRDGRK--VRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWIL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 144 RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE---VKIGDFGLAtKVEyDGERKKTlCGTPNYIAP 220
Cdd:cd14088  92 DQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKnskIVISDFHLA-KLE-NGLIKEP-CGTPEYLAP 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 221 EVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKN----------EYSIP--KHINPVAASLIQKMLQT 288
Cdd:cd14088 169 EVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYENHDKNlfrkilagdyEFDSPywDDISQAAKDLVTRLMEV 248
                       250
                ....*....|....*.
gi 21359873 289 DPTARPTINELLNDEF 304
Cdd:cd14088 249 EQDQRITAEEAISHEW 264
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
60-305 3.27e-28

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: 114.52  E-value: 3.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  60 GKGGFAKCFEISDADTKEVFAGKIVPkslllkPHQREKmSMEISIHRSLAHQHVVGFHGFF------EDNDFVFVVLE-- 131
Cdd:cd14137  13 GSGSFGVVYQAKLLETGEVVAIKKVL------QDKRYK-NRELQIMRRLKHPNIVKLKYFFyssgekKDEVYLNLVMEym 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 ---LCRRrsLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN-EDLEVKIGDFGLAtkveydger 207
Cdd:cd14137  86 petLYRV--IRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFGSA--------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 KKTLCGTPN--YI------APE-VLSKKGHSFEVDVWSIGCIMYTLLVGKPPF--ETS---------------------- 254
Cdd:cd14137 155 KRLVPGEPNvsYIcsryyrAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFpgESSvdqlveiikvlgtptreqikam 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 255 ---CLKETYLRIKKNEYS--IPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14137 235 npnYTEFKFPQIKPHPWEkvFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFF 290
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
89-311 3.38e-28

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: 114.70  E-value: 3.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  89 LLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKaLTEPEARYYLRQIVLGCQYLH 168
Cdd:cd06659  56 LRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDIVSQTR-LNEEQIATVCEAVLQALAYLH 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 169 RNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGK 248
Cdd:cd06659 135 SQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGE 214
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 249 PPFETSCLKETYLRIKKNEYSIPKH---INPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIP 311
Cdd:cd06659 215 PPYFSDSPVQAMKRLRDSPPPKLKNshkASPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLP 280
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
101-305 3.95e-28

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: 114.11  E-value: 3.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR--RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLK 178
Cdd:cd07836  48 EISLMKELKHENIVRLHDVIHTENKLMLVFEYMDKdlKKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 179 LGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK 257
Cdd:cd07836 128 PQNLLINKRGELKLADFGLARAFGIPVNTFSNEVVTLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNE 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 258 ETYLRIKK-----NEYSIPK------------------------HINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07836 208 DQLLKIFRimgtpTESTWPGisqlpeykptfpryppqdlqqlfpHADPLGIDLLHRLLQLNPELRISAHDALQHPWF 284
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
59-300 6.69e-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: 112.80  E-value: 6.69e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLL-LKPHQREkmsMEISIHRSlAHQHVVG-FHGFFEDNDFVFVVLELCRRR 136
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTkLKDFLRE---YNISLELS-VHPHIIKtYDVAFETEDYYVFAQEYAPYG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL--NEDLEVKIGDFGLATKVeydGERKKTLCGT 214
Cdd:cd13987  77 DLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLTRRV---GSTVKRVSGT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVL-SKKGHSFEV----DVWSIGCIMYTLLVGKPPFETSCLK----ETYLRIKKNE-YSIPKHIN---PVAASL 281
Cdd:cd13987 154 IPYTAPEVCeAKKNEGFVVdpsiDVWAFGVLLFCCLTGNFPWEKADSDdqfyEEFVRWQKRKnTAVPSQWRrftPKALRM 233
                       250
                ....*....|....*....
gi 21359873 282 IQKMLQTDPTARPTINELL 300
Cdd:cd13987 234 FKKLLAPEPERRCSIKEVF 252
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
101-326 1.16e-27

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: 114.00  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFF----EDNDF--VFVVLELCRRrsllELHK---RRKALTEPEARYYLRQIVLGCQYLHRNR 171
Cdd:cd07855  54 ELKILRHFKHDNIIAIRDILrpkvPYADFkdVYVVLDLMES----DLHHiihSDQPLTLEHIRYFLYQLLRGLKYIHSAN 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 172 VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTL----CGTPNYIAPEV-LSKKGHSFEVDVWSIGCI------ 240
Cdd:cd07855 130 VIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPEEHKYFmteyVATRWYRAPELmLSLPEYTQAIDMWSVGCIfaemlg 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 241 ---------------MYTLLVGKPPfeTSCLKETYL-RIKKNEYSIPKH-----------INPVAASLIQKMLQTDPTAR 293
Cdd:cd07855 210 rrqlfpgknyvhqlqLILTVLGTPS--QAVINAIGAdRVRRYIQNLPNKqpvpwetlypkADQQALDLLSQMLRFDPSER 287
                       250       260       270
                ....*....|....*....|....*....|...
gi 21359873 294 PTINELLNDEFFTSGYIPARLPiTCltiPPRFS 326
Cdd:cd07855 288 ITVAEALQHPFLAKYHDPDDEP-DC---APPFD 316
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
59-299 1.18e-27

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: 112.60  E-value: 1.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEI-SDADTKEVFAGK-IVPKSLLLKPHQREK------MSMEISIHR-SLAHQHVVGFHGFFEDNDFVFVV 129
Cdd:cd08528   8 LGSGAFGCVYKVrKKSNGQTLLALKeINMTNPAFGRTEQERdksvgdIISEVNIIKeQLRHPNIVRYYKTFLENDRLYIV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSLLELHKRRKALTE--PEARYY--LRQIVLGCQYLHRNR-VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD 204
Cdd:cd08528  88 MELIEGAPLGEHFSSLKEKNEhfTEDRIWniFVQMVLALRYLHKEKqIVHRDLKPNNIMLGEDDKVTITDFGLAKQKGPE 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHI-NPVAASLI 282
Cdd:cd08528 168 SSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEpLPEGMySDDITFVI 247
                       250
                ....*....|....*..
gi 21359873 283 QKMLQTDPTARPTINEL 299
Cdd:cd08528 248 RSCLTPDPEARPDIVEV 264
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
59-295 1.21e-27

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: 112.32  E-value: 1.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFA---KCFEISdadTKEVFAGKIVPKSlllKPHQ--REKMSMEISI-HRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd14198  16 LGRGKFAvvrQCISKS---TGQEYAAKFLKKR---RRGQdcRAEILHEIAVlELAKSNPRVVNLHEVYETTSEIILILEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLEL--HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKVEYDGER 207
Cdd:cd14198  90 AAGGEIFNLcvPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLssiYPLGDIKIVDFGMSRKIGHACEL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 KKTLcGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKK--NEYSIP--KHINPVAASLIQ 283
Cdd:cd14198 170 REIM-GTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQvnVDYSEEtfSSVSQLATDFIQ 248
                       250
                ....*....|..
gi 21359873 284 KMLQTDPTARPT 295
Cdd:cd14198 249 KLLVKNPEKRPT 260
POLO_box cd13112
Polo-box domain (PBD), a C-terminal tandemly repeated region of polo-like kinases; The ...
409-486 1.24e-27

Polo-box domain (PBD), a C-terminal tandemly repeated region of polo-like kinases; The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.


Pssm-ID: 240556  Cd Length: 76  Bit Score: 105.97  E-value: 1.24e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 409 FWVSKWVDYsdKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYM 486
Cdd:cd13112   1 PTLKVWYFT--KYGIGQLLSTGSVEILFNDGTKLILSPDGSSLKYYDPDGQLTRYYLSELPSELRSKLEYLNTFVTHV 76
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
59-296 1.32e-27

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: 112.43  E-value: 1.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGF-HGFFEDNDfVFVVLELCRRRS 137
Cdd:cd08228  10 IGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYlDSFIEDNE-LNIVLELADAGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLEL----HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd08228  89 LSQMikyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYL--RIKKNEY-SIPK-HINPVAASLIQKMLQTD 289
Cdd:cd08228 169 TPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLcqKIEQCDYpPLPTeHYSEKLRELVSMCIYPD 248

                ....*..
gi 21359873 290 PTARPTI 296
Cdd:cd08228 249 PDQRPDI 255
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
59-299 1.35e-27

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: 111.88  E-value: 1.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFE-DNDFVFVVLElCRRRS 137
Cdd:cd14164   8 IGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYIVME-AAATD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE-VKIGDFGLATKVEYDGERKKTLCGTPN 216
Cdd:cd14164  87 LLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRkIKIADFGFARFVEDYPELSTTFCGSRA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGH-SFEVDVWSIGCIMYTLLVGKPPF-ETSClkeTYLRIKKNEYSIPKHI---NPVAAsLIQKMLQTDPT 291
Cdd:cd14164 167 YTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFdETNV---RRLRLQQRGVLYPSGValeEPCRA-LIRTLLQFNPS 242

                ....*...
gi 21359873 292 ARPTINEL 299
Cdd:cd14164 243 TRPSIQQV 250
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
59-305 1.55e-27

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: 112.90  E-value: 1.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPkslLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06655  27 IGQGASGTVFTAIDVATGQEVAIKQIN---LQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGSL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELhKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd06655 104 TDV-VTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWM 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLrIKKN---EYSIPKHINPVAASLIQKMLQTDPTARP 294
Cdd:cd06655 183 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYL-IATNgtpELQNPEKLSPIFRDFLNRCLEMDVEKRG 261
                       250
                ....*....|.
gi 21359873 295 TINELLNDEFF 305
Cdd:cd06655 262 SAKELLQHPFL 272
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
59-304 2.07e-27

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: 112.07  E-value: 2.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06640  12 IGKGSFGEVFKGIDNRTQQVVAIKII--DLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELhKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd06640  90 LDL-LRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWM 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd06640 169 APEVIQQSAYDSKADIWSLGITAIELAKGEPPnSDMHPMRVLFLIPKNNPPTLVGDFSKPFKEFIDACLNKDPSFRPTAK 248

                ....*..
gi 21359873 298 ELLNDEF 304
Cdd:cd06640 249 ELLKHKF 255
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
107-302 2.34e-27

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: 112.11  E-value: 2.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 107 SLAHQH--VVGFHGFFED---------NDFVFV---------VLE-LC------RRRSLLELHK---RRKALTEPEARYY 156
Cdd:cd13974  58 SLLHDQdgVVHHHGLFQDraceikedkSSNVYTgrvrkrlclVLDcLCahdfsdKTADLINLQHyviREKRLSEREALVI 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 157 LRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL-EVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFE-VDV 234
Cdd:cd13974 138 FYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTrKITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYLGKpSDM 217
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 235 WSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK--HINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd13974 218 WALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKRLTASEVLDS 287
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-300 2.77e-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: 2.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  74 DTKEVFAGKIvpksLLLKPhqreKMSMEISIHRSLA-HQHVVGFHGFFEdNDFVF-----------VVLELCRRRSLLEL 141
Cdd:cd14171  29 STGERFALKI----LLDRP----KARTEVRLHMMCSgHPNIVQIYDVYA-NSVQFpgessprarllIVMELMEGGELFDR 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 142 HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLAtKVEyDGERkKTLCGTPNYI 218
Cdd:cd14171 100 ISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGFA-KVD-QGDL-MTPQFTPYYV 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVL-SKKGHSFE----------------VDVWSIGCIMYTLLVGKPPF--ET---SCLKETYLRIKKNEYSIP----K 272
Cdd:cd14171 177 APQVLeAQRRHRKErsgiptsptpytydksCDMWSLGVIIYIMLCGYPPFysEHpsrTITKDMKRKIMTGSYEFPeeewS 256
                       250       260
                ....*....|....*....|....*...
gi 21359873 273 HINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14171 257 QISEMAKDIVRKLLCVDPEERMTIEEVL 284
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
59-305 2.94e-27

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: 111.60  E-value: 2.94e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTkevfaGKIVPKSLLLKPHQREKMSM----EISIHRSL---AHQHVVG----FHGFFEDNDF-V 126
Cdd:cd07838   7 IGEGAYGTVYKARDLQD-----GRFVALKKVRVPLSEEGIPLstirEIALLKQLesfEHPNVVRlldvCHGPRTDRELkL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 127 FVVLELCRR--RSLLELHKRRkALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKveYD 204
Cdd:cd07838  82 TLVFEHVDQdlATYLDKCPKP-GLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARI--YS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLC-GTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTL---------------------LVGKP-----PFETSCLK 257
Cdd:cd07838 159 FEMALTSVvVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELfnrrplfrgsseadqlgkifdVIGLPseeewPRNSALPR 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 21359873 258 ET---YLRIKKNeySIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07838 239 SSfpsYTPRPFK--SFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
60-301 4.32e-27

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: 110.30  E-value: 4.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  60 GKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLL 139
Cdd:cd14111  12 ARGRFGVIRRCRENATGKNFPAKIVP----YQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 140 ELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKT-LCGTPNYI 218
Cdd:cd14111  88 HSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGrRTGTLEYM 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK---HINPVAASLIQKMLQTDPTARPT 295
Cdd:cd14111 168 APEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAFKlypNVSQSASLFLKKVLSSYPWSRPT 247

                ....*.
gi 21359873 296 INELLN 301
Cdd:cd14111 248 TKDCFA 253
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
59-303 4.54e-27

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: 111.12  E-value: 4.54e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGK--IVPKSLLlkphQREKMSMEISIHRSLAHQHVVGF---------HGFFEDND--F 125
Cdd:cd14048  14 LGRGGFGVVFEAKNKVDDCNYAVKriRLPNNEL----AREKVLREVRALAKLDHPGIVRYfnawlerppEGWQEKMDevY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 126 VFVVLELCRRRSLLELHKRRKALTEPEARYYL---RQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE 202
Cdd:cd14048  90 LYIQMQLCRKENLKDWMNRRCTMESRELFVCLnifKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVTAMD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 203 YDGERKKTL------------CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVgkpPFETSCLKETYLRIKKNEYSI 270
Cdd:cd14048 170 QGEPEQTVLtpmpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIY---SFSTQMERIRTLTDVRKLKFP 246
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21359873 271 PKHIN--PVAASLIQKMLQTDPTARPTINELLNDE 303
Cdd:cd14048 247 ALFTNkyPEERDMVQQMLSPSPSERPEAHEVIEHA 281
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
59-305 4.68e-27

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: 112.06  E-value: 4.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05597   9 IGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDYYCGGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LEL-HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE-RKKTLCGTPN 216
Cdd:cd05597  89 LTLlSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDGTvQSSVAVGTPD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVL--SKKGH---SFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIPKHINPVAAS---LIQKML 286
Cdd:cd05597 169 YISPEILqaMEDGKgryGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHKEHFSFPDDEDDVSEEakdLIRRLI 248
                       250       260
                ....*....|....*....|.
gi 21359873 287 QTDPT--ARPTINELLNDEFF 305
Cdd:cd05597 249 CSRERrlGQNGIDDFKKHPFF 269
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
59-306 5.07e-27

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: 110.51  E-value: 5.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06605   9 LGEGNGGVVSKVRHRPSGQIMAVKVI--RLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNR-VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDgeRKKTLCGTPNY 217
Cdd:cd06605  87 DKILKEVGRIPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDS--LAKTFVGTRSY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFEtSCLKETYLRIKK------NEYS--IPKHI-NPVAASLIQKMLQT 288
Cdd:cd06605 165 MAPERISGGKYTVKSDIWSLGLSLVELATGRFPYP-PPNAKPSMMIFEllsyivDEPPplLPSGKfSPDFQDFVSQCLQK 243
                       250
                ....*....|....*...
gi 21359873 289 DPTARPTINELLNDEFFT 306
Cdd:cd06605 244 DPTERPSYKELMEHPFIK 261
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
59-306 5.08e-27

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: 113.02  E-value: 5.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05629   9 IGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIMEFLPGGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAT------------------- 199
Cdd:cd05629  89 MTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkqhdsayyqkllqgks 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 200 -KVEYDGER--------------------KK-------TLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd05629 169 nKNRIDNRNsvavdsinltmsskdqiatwKKnrrlmaySTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIGWPPF 248
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21359873 252 ETSCLKETYLRIKKNEYSI--PK--HINPVAASLIQKMLqTDPT---ARPTINELLNDEFFT 306
Cdd:cd05629 249 CSENSHETYRKIINWRETLyfPDdiHLSVEAEDLIRRLI-TNAEnrlGRGGAHEIKSHPFFR 309
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
59-301 1.03e-26

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: 109.46  E-value: 1.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPH------QREKMSMEIsihrslaHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEErkallkEAEKMERAR-------HSYVLPLLGVCVERRSLGLVMEY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARY-YLRQIVLGCQYLH--RNRVIHRDLKLGNLFLNEDLEVKIGDFGLA-----TKVEYD 204
Cdd:cd13978  74 MENGSLKSLLEREIQDVPWSLRFrIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSklgmkSISANR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLCGTPNYIAPEVLSKKGHSFEV--DVWSIGCIMYTLLVGKPPFE--TSCLKETYLRIKKNEYSI-----PKHIN 275
Cdd:cd13978 154 RRGTENLGGTPIYMAPEAFDDFNKKPTSksDVYSFAIVIWAVLTRKEPFEnaINPLLIMQIVSKGDRPSLddigrLKQIE 233
                       250       260
                ....*....|....*....|....*...
gi 21359873 276 PVA--ASLIQKMLQTDPTARPTINELLN 301
Cdd:cd13978 234 NVQelISLMIRCWDGNPDARPTFLECLD 261
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
89-307 1.11e-26

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: 111.58  E-value: 1.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  89 LLKPHQRE----KMSMEISIHRSLAHQHVVGFHGFFED-------NDFVFVVLELCRRRSLLELHKRrkaLTEPEARYYL 157
Cdd:cd07880  48 LYRPFQSElfakRAYRELRLLKHMKHENVIGLLDVFTPdlsldrfHDFYLVMPFMGTDLGKLMKHEK---LSEDRIQFLV 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 158 RQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeyDGERKKTLCgTPNYIAPEV-LSKKGHSFEVDVWS 236
Cdd:cd07880 125 YQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQT--DSEMTGYVV-TRWYRAPEViLNWMHYTQTVDIWS 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 237 IGCIMYTLLVGKPPFE--------TSCLKET------------------YL----RIKKNEY-SIPKHINPVAASLIQKM 285
Cdd:cd07880 202 VGCIMAEMLTGKPLFKghdhldqlMEIMKVTgtpskefvqklqsedaknYVkklpRFRKKDFrSLLPNANPLAVNVLEKM 281
                       250       260
                ....*....|....*....|..
gi 21359873 286 LQTDPTARPTINELLNDEFFTS 307
Cdd:cd07880 282 LVLDAESRITAAEALAHPYFEE 303
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
101-305 1.12e-26

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: 110.01  E-value: 1.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQH-------VVGfhgffEDNDFVFVVLELCRR--RSLLELHKRRkaLTEPEARYYLRQIVLGCQYLHRNR 171
Cdd:cd07843  54 EINILLKLQHPNivtvkevVVG-----SNLDKIYMVMEYVEHdlKSLMETMKQP--FLQSEVKCLMLQLLSGVAHLHDNW 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 172 VIHRDLKLGNLFLNEDLEVKIGDFGLATKVeydGERKKTLcgTPN-----YIAPEVL-SKKGHSFEVDVWSIGCIMYTLL 245
Cdd:cd07843 127 ILHRDLKTSNLLLNNRGILKICDFGLAREY---GSPLKPY--TQLvvtlwYRAPELLlGAKEYSTAIDMWSVGCIFAELL 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 246 VGKPPF----ETSCLK-----------------ETYLRIKKNEYSIPKH-----------INPVAASLIQKMLQTDPTAR 293
Cdd:cd07843 202 TKKPLFpgksEIDQLNkifkllgtptekiwpgfSELPGAKKKTFTKYPYnqlrkkfpalsLSDNGFDLLNRLLTYDPAKR 281
                       250
                ....*....|..
gi 21359873 294 PTINELLNDEFF 305
Cdd:cd07843 282 ISAEDALKHPYF 293
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
59-299 1.19e-26

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: 109.31  E-value: 1.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDND-FVFVVLELCRRRS 137
Cdd:cd14163   8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLVMELAEDGD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLnEDLEVKIGDFGLATKVEYDG-ERKKTLCGTPN 216
Cdd:cd14163  88 VFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPKGGrELSQTFCGSTA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLSKKGH-SFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNeYSIPKH--INPVAASLIQKMLQTDPTAR 293
Cdd:cd14163 167 YAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKG-VSLPGHlgVSRTCQDLLKRLLEPDMVLR 245

                ....*.
gi 21359873 294 PTINEL 299
Cdd:cd14163 246 PSIEEV 251
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
80-312 2.70e-26

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: 108.96  E-value: 2.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  80 AGKIVP--KSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLEL--HKRrkaLTEPEARY 155
Cdd:cd06657  44 SGKLVAvkKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIvtHTR---MNEEQIAA 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 156 YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVW 235
Cdd:cd06657 121 VCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIW 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 236 SIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASL---IQKMLQTDPTARPTINELLNDEFFTSGYIPA 312
Cdd:cd06657 201 SLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPSLkgfLDRLLVRDPAQRATAAELLKHPFLAKAGPPS 280
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
59-286 2.71e-26

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: 111.65  E-value: 2.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05623  80 IGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDL 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LEL-HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLC-GTPN 216
Cdd:cd05623 160 LTLlSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAvGTPD 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLS-----KKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIPKHINPV---AASLIQKML 286
Cdd:cd05623 240 YISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHKERFQFPTQVTDVsenAKDLIRRLI 319
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
84-312 2.97e-26

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: 108.97  E-value: 2.97e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  84 VPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLEL--HKRrkaLTEPEARYYLRQIV 161
Cdd:cd06658  52 VKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDIvtHTR---MNEEQIATVCLSVL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 162 LGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIM 241
Cdd:cd06658 129 RALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMV 208
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21359873 242 YTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASL---IQKMLQTDPTARPTINELLNDEFFTSGYIPA 312
Cdd:cd06658 209 IEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHKVSSVLrgfLDLMLVREPSQRATAQELLQHPFLKLAGPPS 282
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
59-263 3.23e-26

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: 110.53  E-value: 3.23e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05627  10 IGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAT------KVEY--------- 203
Cdd:cd05627  90 MTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTglkkahRTEFyrnlthnpp 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 204 --------DGERKK------------TLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI 263
Cdd:cd05627 170 sdfsfqnmNSKRKAetwkknrrqlaySTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKV 249
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
58-300 3.28e-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: 3.28e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKMSMEI-SIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd14174   9 LLGEGAYAKVQGCVSLQNGKEYAVKIIEKN---AGHSRSRVFREVeTLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLfLNEDLE----VKIGDFGLATKVEYDGE------ 206
Cdd:cd14174  86 SILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENI-LCESPDkvspVKICDFDLGSGVKLNSActpitt 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 -RKKTLCGTPNYIAPEVLS--KKGHSF---EVDVWSIGCIMYTLLVGKPPF-------------ET--SCLKETYLRIKK 265
Cdd:cd14174 165 pELTTPCGSAEYMAPEVVEvfTDEATFydkRCDLWSLGVILYIMLSGYPPFvghcgtdcgwdrgEVcrVCQNKLFESIQE 244
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 21359873 266 NEYSIPK----HINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14174 245 GKYEFPDkdwsHISSEAKDLISKLLVRDAKERLSAAQVL 283
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
101-325 3.77e-26

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: 109.70  E-value: 3.77e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFH-----GFFEDNDFVFVVLELCRRrsllELHK--RRKALTEPEARYYLRQIVLGCQYLHRNRVI 173
Cdd:cd07849  53 EIKILLRFKHENIIGILdiqrpPTFESFKDVYIVQELMET----DLYKliKTQHLSNDHIQYFLYQILRGLKYIHSANVL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTL---CGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKP 249
Cdd:cd07849 129 HRDLKPSNLLLNTNCDLKICDFGLARIADPEHDHTGFLteyVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRP 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 250 PFE---------------TSCLKETYLRI---KKNEY--SIP-----------KHINPVAASLIQKMLQTDPTARPTINE 298
Cdd:cd07849 209 LFPgkdylhqlnlilgilGTPSQEDLNCIislKARNYikSLPfkpkvpwnklfPNADPKALDLLDKMLTFNPHKRITVEE 288
                       250       260
                ....*....|....*....|....*..
gi 21359873 299 LLNDEFFTSGYIPARLPITCLTIPPRF 325
Cdd:cd07849 289 ALAHPYLEQYHDPSDEPVAEEPFPFDM 315
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
59-306 5.78e-26

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: 108.58  E-value: 5.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkslllkpHQREKMSMEISIH-RSLAHQHVVG----FHGFFEDNDFVFVVLELC 133
Cdd:cd14170  10 LGLGINGKVLQIFNKRTQEKFALKML--------QDCPKARREVELHwRASQCPHIVRivdvYENLYAGRKCLLIVMECL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE---DLEVKIGDFGLATKVEYDGERK 208
Cdd:cd14170  82 DGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 kTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETS-------CLKEtylRIKKNEYSIPK----HINPV 277
Cdd:cd14170 162 -TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhglaispGMKT---RIRMGQYEFPNpewsEVSEE 237
                       250       260
                ....*....|....*....|....*....
gi 21359873 278 AASLIQKMLQTDPTARPTINELLNDEFFT 306
Cdd:cd14170 238 VKMLIRNLLKTEPTQRMTITEFMNHPWIM 266
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
59-293 6.02e-26

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: 107.77  E-value: 6.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRI-KKRKGEAMALnEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LlELH---KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGT 214
Cdd:cd05631  87 L-KFHiynMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIP-EGETVRGRVGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDP 290
Cdd:cd05631 165 VGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFrkrkERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNP 244

                ...
gi 21359873 291 TAR 293
Cdd:cd05631 245 KER 247
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
94-305 6.85e-26

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: 106.94  E-value: 6.85e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  94 QREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELhKRRKALTEPEARYYLRQIVLGCQYLHRNRVI 173
Cdd:cd06647  47 KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV-VTETCMDEGQIAAVCRECLQALEFLHSNQVI 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-E 252
Cdd:cd06647 126 HRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlN 205
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 253 TSCLKETYLrIKKN---EYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd06647 206 ENPLRALYL-IATNgtpELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
59-295 7.05e-26

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: 106.58  E-value: 7.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFA---KCfeISDADTKEVfAGKIVPKslllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14115   1 IGRGRFSivkKC--LHKATRKDV-AVKFVSK----KMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL---EVKIGDFGLAtkVEYDGERK-KTL 211
Cdd:cd14115  74 GRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDA--VQISGHRHvHHL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKH----INPVAASLIQKMLQ 287
Cdd:cd14115 152 LGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEyfgdVSQAARDFINVILQ 231

                ....*...
gi 21359873 288 TDPTARPT 295
Cdd:cd14115 232 EDPRRRPT 239
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
59-263 8.62e-26

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: 109.36  E-value: 8.62e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05628   9 IGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGDM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAT------KVEY--------- 203
Cdd:cd05628  89 MTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTglkkahRTEFyrnlnhslp 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 204 --------DGERKK------------TLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI 263
Cdd:cd05628 169 sdftfqnmNSKRKAetwkrnrrqlafSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKV 248
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
59-299 8.75e-26

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: 106.83  E-value: 8.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREkmsmEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKVR----LEVFRAE----ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED-LEVKIGDFGLATKVEYDGERKKTLC----- 212
Cdd:cd13991  86 GQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHAECLDPDGLGKSLFTgdyip 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 213 GTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNE---YSIPKHINPVAASLIQKMLQTD 289
Cdd:cd13991 166 GTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPpplREIPPSCAPLTAQAIQAGLRKE 245
                       250
                ....*....|
gi 21359873 290 PTARPTINEL 299
Cdd:cd13991 246 PVHRASAAEL 255
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
59-306 9.95e-26

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: 107.05  E-value: 9.95e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQR-EKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd06645  19 IGSGTYGDVYKARNVNTGELAAIKVIK----LEPGEDfAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGS 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd06645  95 LQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYW 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLS---KKGHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYLRIKKNeYSIPKHINPVAAS-----LIQKMLQT 288
Cdd:cd06645 175 MAPEVAAverKGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFLMTKSN-FQPPKLKDKMKWSnsfhhFVKMALTK 253
                       250
                ....*....|....*...
gi 21359873 289 DPTARPTINELLNDEFFT 306
Cdd:cd06645 254 NPKKRPTAEKLLQHPFVT 271
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
82-305 1.21e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 110.49  E-value: 1.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   82 KIVPKSLLLKpHQREKMSMEISIHRSLAHQH--VVGFHGFFEDNDFVFVVLELCR----RRSLLELHKRRKALTEPEARY 155
Cdd:PTZ00267  95 KVVAKFVMLN-DERQAAYARSELHCLAACDHfgIVKHFDDFKSDDKLLLIMEYGSggdlNKQIKQRLKEHLPFQEYEVGL 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  156 YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATK----VEYDgeRKKTLCGTPNYIAPEVLSKKGHSFE 231
Cdd:PTZ00267 174 LFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQysdsVSLD--VASSFCGTPYYLAPELWERKRYSKK 251
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873  232 VDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:PTZ00267 252 ADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFL 326
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
59-301 1.32e-25

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: 106.61  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKivpKSLLLKPHQREKMSMEISIHRSLAHQHVVGF--HGFFEDND---FVFVVLELC 133
Cdd:cd13986   8 LGEGGFSFVYLVEDLSTGRLYALK---KILCHSKEDVKEAMREIENYRLFNHPNILRLldSQIVKEAGgkkEVYLLLPYY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKA----LTEPEARYYLRQIVLGCQYLHRNR---VIHRDLKLGNLFLNEDLEVKIGDFGLATKV----- 201
Cdd:cd13986  85 KRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLSEDDEPILMDLGSMNPArieie 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 202 ---------EYDGERkktlcGTPNYIAPEVLSKKGHSF---EVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI------ 263
Cdd:cd13986 165 grrealalqDWAAEH-----CTMPYRAPELFDVKSHCTideKTDIWSLGCTLYALMYGESPFERIFQKGDSLALavlsgn 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21359873 264 ----KKNEYSIPKHinpvaaSLIQKMLQTDPTARPTINELLN 301
Cdd:cd13986 240 ysfpDNSRYSEELH------QLVKSMLVVNPAERPSIDDLLS 275
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
59-293 1.45e-25

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: 109.32  E-value: 1.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05622  81 IGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDL 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE-RKKTLCGTPNY 217
Cdd:cd05622 161 VNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMvRCDTAVGTPDY 239
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKG----HSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIPK--HINPVAASLIQKMLqTD 289
Cdd:cd05622 240 ISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDdnDISKEAKNLICAFL-TD 318

                ....
gi 21359873 290 PTAR 293
Cdd:cd05622 319 REVR 322
POLO_box cd13112
Polo-box domain (PBD), a C-terminal tandemly repeated region of polo-like kinases; The ...
509-590 2.11e-25

Polo-box domain (PBD), a C-terminal tandemly repeated region of polo-like kinases; The polo-like Ser/Thr kinases (Plk1, Plk2/Snk, Plk3/Prk/Fnk, Plk4/Sak, and the inactive kinase Plk5) play various roles in cytokinesis and mitosis. At their C-terminus, they contain a tandemly repeated polo-box domain (in the case of Plk4, a tandem repeat of cryptic PBDs is found in the middle of the protein followed by a C-terminal single repeat), which appears to be involved in autoinhibition and in mediating the subcellular localization. The latter may be controlled via interactions between the polo-box domain and phospho-peptide motifs. The phosphopeptide binding site is formed at the interface between the two tandemly repeated PBDs. The PBDs of Plk4/Sak appear unique in participating in homodimer interactions, though it is not clear whether and how they interact with phosphopeptides.


Pssm-ID: 240556  Cd Length: 76  Bit Score: 99.81  E-value: 2.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 509 PYLRTWFRTRSAIILHLSNGSVQINFFqDHTKLILCPLMAAVTYIDEKRDFRTYRLSLleeygCCKELASRLRYARTMVD 588
Cdd:cd13112   1 PTLKVWYFTKYGIGQLLSTGSVEILFN-DGTKLILSPDGSSLKYYDPDGQLTRYYLSE-----LPSELRSKLEYLNTFVT 74

                ..
gi 21359873 589 KL 590
Cdd:cd13112  75 HV 76
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
59-304 2.18e-25

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: 107.05  E-value: 2.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC--RRR 136
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYClgSAS 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKrrKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeydgERKKTLCGTPN 216
Cdd:cd06633 109 DLLEVHK--KPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIA----SPANSFVGTPY 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEV---LSKKGHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYL-------RIKKNEYSIPkhinpvAASLIQKM 285
Cdd:cd06633 183 WMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPlFNMNAMSALYHiaqndspTLQSNEWTDS------FRGFVDYC 256
                       250
                ....*....|....*....
gi 21359873 286 LQTDPTARPTINELLNDEF 304
Cdd:cd06633 257 LQKIPQERPSSAELLRHDF 275
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
59-305 2.25e-25

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: 106.35  E-value: 2.25e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAgkIVPKSLLLKPhQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06654  28 IGQGASGTVYTAMDVATGQEVA--IRQMNLQQQP-KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELhKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd06654 105 TDV-VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWM 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLrIKKN---EYSIPKHINPVAASLIQKMLQTDPTARP 294
Cdd:cd06654 184 APEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYlNENPLRALYL-IATNgtpELQNPEKLSAIFRDFLNRCLEMDVEKRG 262
                       250
                ....*....|.
gi 21359873 295 TINELLNDEFF 305
Cdd:cd06654 263 SAKELLQHQFL 273
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
59-293 2.61e-25

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: 107.27  E-value: 2.61e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQH---VVGFHGFFE-DNDFVFVVLELCR 134
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTALDEspfIVGLKFSFQtPTDLYLVTDYMSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd05586  81 GELFWHLQKEGR-FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKH-INPVAASLIQKMLQTDPTA 292
Cdd:cd05586 160 TEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDvLSDEGRSFVKGLLNRNPKH 239

                .
gi 21359873 293 R 293
Cdd:cd05586 240 R 240
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
143-301 4.65e-25

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 108.80  E-value: 4.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  143 KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAT--KVEYDGERKKTLCGTPNYIAP 220
Cdd:PTZ00283 135 KTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKmyAATVSDDVGRTFCGTPYYVAP 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  221 EVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYS-IPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:PTZ00283 215 EIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDpLPPSISPEMQEIVTALLSSDPKRRPSSSKL 294

                 ..
gi 21359873  300 LN 301
Cdd:PTZ00283 295 LN 296
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
59-307 4.82e-25

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: 107.44  E-value: 4.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05625   9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD-------------- 204
Cdd:cd05625  89 MSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWThdskyyqsgdhlrq 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 -----------------GERKK----------------TLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd05625 169 dsmdfsnewgdpencrcGDRLKplerraarqhqrclahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPF 248
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21359873 252 ETSCLKETYLRIKKNEYS--IPKH--INPVAASLIQKMLQ--TDPTARPTINELLNDEFFTS 307
Cdd:cd05625 249 LAQTPLETQMKVINWQTSlhIPPQakLSPEASDLIIKLCRgpEDRLGKNGADEIKAHPFFKT 310
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
59-307 5.55e-25

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: 104.45  E-value: 5.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKivpKSLLLKPHQREK---MSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC-- 133
Cdd:cd06607   9 IGHGSFGAVYYARNKRTSEVVAIK---KMSYSGKQSTEKwqdIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYClg 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKrrKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeydgERKKTLCG 213
Cdd:cd06607  86 SASDIVEVHK--KPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLV----CPANSFVG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVL--SKKGH-SFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYlRIKKNEYSI--PKHINPVAASLIQKMLQ 287
Cdd:cd06607 160 TPYWMAPEVIlaMDEGQyDGKVDVWSLGITCIELAERKPPlFNMNAMSALY-HIAQNDSPTlsSGEWSDDFRNFVDSCLQ 238
                       250       260
                ....*....|....*....|
gi 21359873 288 TDPTARPTINELLNDEFFTS 307
Cdd:cd06607 239 KIPQDRPSAEDLLKHPFVTR 258
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
61-300 5.83e-25

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: 104.23  E-value: 5.83e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  61 KGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLE 140
Cdd:cd14110  13 RGRFSVVRQCEEKRSGQMLAAKIIP----YKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 141 LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGtpNYI-- 218
Cdd:cd14110  89 NLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKG--DYVet 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 -APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPK---HINPVAASLIQKMLQTDPTARP 294
Cdd:cd14110 167 mAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRcyaGLSGGAVNFLKSTLCAKPWGRP 246

                ....*.
gi 21359873 295 TINELL 300
Cdd:cd14110 247 TASECL 252
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
59-304 7.49e-25

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: 104.34  E-value: 7.49e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkslllKPHQREKMSM---EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd06646  17 VGSGTYGDVYKARNLHTGELAAVKII------KLEPGDDFSLiqqEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd06646  91 GSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRKSFIGTP 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKK---GHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYLrIKKNEYSIPK-----HINPVAASLIQKML 286
Cdd:cd06646 171 YWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALFL-MSKSNFQPPKlkdktKWSSTFHNFVKISL 249
                       250
                ....*....|....*...
gi 21359873 287 QTDPTARPTINELLNDEF 304
Cdd:cd06646 250 TKNPKKRPTAERLLTHLF 267
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
59-251 8.22e-25

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: 103.85  E-value: 8.22e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14190  12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQ---NSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL--NEDLEVKIGDFGLATKveYDGERK-KTLCGT 214
Cdd:cd14190  89 FErIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARR--YNPREKlKVNFGT 166
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd14190 167 PEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPF 203
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
59-304 8.89e-25

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: 104.29  E-value: 8.89e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGK--IVPKSlllkpHQREKMSMEISIHRSLA-HQHVVGF---------HGFFEdndfV 126
Cdd:cd14037  11 LAEGGFAHVYLVKTSNGGNRAALKrvYVNDE-----HDLNVCKREIEIMKRLSgHKNIVGYidssanrsgNGVYE----V 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 127 FVVLELCRRRSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRNR--VIHRDLKLGNLFLNEDLEVKIGDFGLATK-- 200
Cdd:cd14037  82 LLLMEYCKGGGVIDLMNQRlqTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSATTki 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 201 -----------VEYDGERKKTLCgtpnYIAPEVL---SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSclkeTYLRIKKN 266
Cdd:cd14037 162 lppqtkqgvtyVEEDIKKYTTLQ----YRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPFEES----GQLAILNG 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 21359873 267 EYSIP---KHINPVaASLIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd14037 234 NFTFPdnsRYSKRL-HKLIRYMLEEDPEKRPNIYQVSYEAF 273
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
59-304 8.99e-25

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: 104.09  E-value: 8.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAH---QHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd06917   9 VGRGSYGAVYRGYHVKTGRVVALKVL--NLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCEG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELhKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd06917  87 GSIRTL-MRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRSTFVGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSK-KGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKKNEYSIP-KHINPVAASLIQKMLQTDPTA 292
Cdd:cd06917 166 YWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYsDVDALRAVMLIPKSKPPRLEgNGYSPLLKEFVAACLDEEPKD 245
                       250
                ....*....|..
gi 21359873 293 RPTINELLNDEF 304
Cdd:cd06917 246 RLSADELLKSKW 257
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
72-300 1.03e-24

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: 103.28  E-value: 1.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  72 DADTKEVFAGKIVPKSL---LLKPHQREKmsmeisihrslAHQHVVGFHGFFEDNDFVFVVLElcrrRSLLELH---KRR 145
Cdd:cd13976  14 DIHTGEELVCKVVPVPEchaVLRAYFRLP-----------SHPNISGVHEVIAGETKAYVFFE----RDHGDLHsyvRSR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 146 KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGErKKTLC---GTPNYIAPEV 222
Cdd:cd13976  79 KRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEGE-DDSLSdkhGCPAYVSPEI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 223 LSKKGH--SFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd13976 158 LNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDIL 237
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
59-301 1.20e-24

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: 103.16  E-value: 1.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpKSLLLKPHQREKMSMEISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELCRRrS 137
Cdd:cd14050   9 LGEGSFGEVFKVRSREDGKLYAVKRS-RSRFRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEEKGILYIQTELCDT-S 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtkVEYDGERKKTLC-GTPN 216
Cdd:cd14050  87 LQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLV--VELDKEDIHDAQeGDPR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEVLskKGH-SFEVDVWSIGCimyTLLvgkppfETSCLKE------TYLRIKKNEysIPKHI-NPVA---ASLIQKM 285
Cdd:cd14050 165 YMAPELL--QGSfTKAADIFSLGI---TIL------ELACNLElpsggdGWHQLRQGY--LPEEFtAGLSpelRSIIKLM 231
                       250
                ....*....|....*.
gi 21359873 286 LQTDPTARPTINELLN 301
Cdd:cd14050 232 MDPDPERRPTAEDLLA 247
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
59-300 1.39e-24

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: 103.66  E-value: 1.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKE-VFAGKIVpKSLLLKPHQREKMSMEISIHRSL---AHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd14052   8 IGSGEFSQVYKVSERVPTGkVYAVKKL-KPNYAGAKDRLRRLEEVSILRELtldGHDNIVQLIDSWEYHGHLYIQTELCE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSL---LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATK------VEYDG 205
Cdd:cd14052  87 NGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVwplirgIEREG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 ERKktlcgtpnYIAPEVLSKKGHSFEVDVWSIGCIMYTL--------------------LVGKPPFETSCLKETYLRIKK 265
Cdd:cd14052 167 DRE--------YIAPEILSEHMYDKPADIFSLGLILLEAaanvvlpdngdawqklrsgdLSDAPRLSSTDLHSASSPSSN 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 21359873 266 NEYSIPKHINPVAA--SLIQKMLQTDPTARPTINELL 300
Cdd:cd14052 239 PPPDPPNMPILSGSldRVVRWMLSPEPDRRPTADDVL 275
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
59-337 1.53e-24

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: 104.03  E-value: 1.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAgkIVPKSLLLKPhQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06656  27 IGQGASGTVYTAIDIATGQEVA--IKQMNLQQQP-KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELhKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYI 218
Cdd:cd06656 104 TDV-VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWM 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLrIKKN---EYSIPKHINPVAASLIQKMLQTDPTARP 294
Cdd:cd06656 183 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYL-IATNgtpELQNPERLSAVFRDFLNRCLEMDVDRRG 261
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21359873 295 TINELLNDEFFTSGYiparlPITCLTipPRFSIAPSSLDPSNR 337
Cdd:cd06656 262 SAKELLQHPFLKLAK-----PLSSLT--PLIIAAKEAIKNSSR 297
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
59-304 1.60e-24

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: 103.55  E-value: 1.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREKMSMEISIHRSLAH-QHVVGFHGFF------EDNDFVFVVLE 131
Cdd:cd06636  24 VGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKLEINMLKKYSHhRNIATYYGAFikksppGHDDQLWLVME 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRRSLLELHKRRK--ALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKK 209
Cdd:cd06636 100 FCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TLCGTPNYIAPEVLS-----KKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYL-------RIKKNEYSiPKHINP 276
Cdd:cd06636 180 TFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLcDMHPMRALFLiprnpppKLKSKKWS-KKFIDF 258
                       250       260
                ....*....|....*....|....*...
gi 21359873 277 VAASLIQKMLQtdptaRPTINELLNDEF 304
Cdd:cd06636 259 IEGCLVKNYLS-----RPSTEQLLKHPF 281
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
92-302 1.88e-24

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: 102.86  E-value: 1.88e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  92 PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVfVVLELCRRRSL------LELHKRRKALTEpearyYLRQIVLGCQ 165
Cdd:cd14062  30 PSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLA-IVTQWCEGSSLykhlhvLETKFEMLQLID-----IARQTAQGMD 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 166 YLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAT-KVEYDGERK-KTLCGTPNYIAPEVLSKKG---HSFEVDVWSIGCI 240
Cdd:cd14062 104 YLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATvKTRWSGSQQfEQPTGSILWMAPEVIRMQDenpYSFQSDVYAFGIV 183
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21359873 241 MYTLLVGKPPFETSCLKET--------YLR--IKKNEYSIPKHINPVAASLIQKmlqtDPTARPTINELLND 302
Cdd:cd14062 184 LYELLTGQLPYSHINNRDQilfmvgrgYLRpdLSKVRSDTPKALRRLMEDCIKF----QRDERPLFPQILAS 251
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
59-308 2.30e-24

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: 103.02  E-value: 2.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14104   8 LGRGQFGIVHRCVETSSKKTYMAKFVK----VKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVDI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNL--FLNEDLEVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd14104  84 FErITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIiyCTRRGSYIKIIEFGQSRQLK-PGDKFRLQYTSA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTDPT 291
Cdd:cd14104 163 EFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDdeafKNISIEALDFVDRLLVKERK 242
                       250
                ....*....|....*..
gi 21359873 292 ARPTINELLNDEFFTSG 308
Cdd:cd14104 243 SRMTAQEALNHPWLKQG 259
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
59-293 2.40e-24

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: 103.90  E-value: 2.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05632  10 LGKGGFGEVCACQVRATGKMYACKRLEKKRI-KKRKGESMALnEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LlELH---KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGT 214
Cdd:cd05632  89 L-KFHiynMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIP-EGESIRGRVGT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDP 290
Cdd:cd05632 167 VGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFrgrkEKVKREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKDP 246

                ...
gi 21359873 291 TAR 293
Cdd:cd05632 247 KQR 249
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
59-251 2.97e-24

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: 103.60  E-value: 2.97e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKslllkphQREKMSM------EISIHRSLAHQHVVGFHGFFEDN--DFVFVVL 130
Cdd:cd07845  15 IGEGTYGIVYRARDTTSGEIVALKKVRM-------DNERDGIpisslrEITLLLNLRHPNIVELKEVVVGKhlDSIFLVM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 131 ELCRR--RSLLELHKRrkALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEY-DGER 207
Cdd:cd07845  88 EYCEQdlASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLpAKPM 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 kktlcgTPN-----YIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd07845 166 ------TPKvvtlwYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLL 209
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
101-300 3.15e-24

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: 102.74  E-value: 3.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKRR--KALTEPEaRYYL-RQIVLGCQYLH---RNRVI 173
Cdd:cd14066  40 ELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDrLHCHKgsPPLPWPQ-RLKIaKGIARGLEYLHeecPPPII 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKT--LCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd14066 119 HGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAV 198
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 252 ETSCLKETYLRIK---KNEYS------IPKHI---NPVAASLIQKMLQ-------TDPTARPTINELL 300
Cdd:cd14066 199 DENRENASRKDLVewvESKGKeelediLDKRLvddDGVEEEEVEALLRlallctrSDPSLRPSMKEVV 266
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
59-251 3.36e-24

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: 102.35  E-value: 3.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPkslLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIK---VKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL--EVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd14192  89 FDrITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTgnQIKIIDFGLARRYK-PREKLKVNFGTP 167
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd14192 168 EFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPF 203
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
58-303 3.75e-24

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: 102.01  E-value: 3.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHqrekmsmEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd13995  11 FIPRGAFGKVYLAQDTKTKKRMACKLIPVEQF-KPS-------DVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIgDFGLATKVEYDGERKKTLCGTPNY 217
Cdd:cd13995  83 VLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSVQMTEDVYVPKDLRGTEIY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKE---TYLRIKKNEY----SIPKHINPVAASLIQKMLQTDP 290
Cdd:cd13995 162 MSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSaypSYLYIIHKQAppleDIAQDCSPAMRELLEAALERNP 241
                       250
                ....*....|...
gi 21359873 291 TARPTINELLNDE 303
Cdd:cd13995 242 NHRSSAAELLKHE 254
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
135-315 4.68e-24

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: 103.41  E-value: 4.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLE-LHKRrkaltepearYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG 213
Cdd:cd07852 100 RANILEdIHKQ----------YIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDENPVL 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TpNYIA------PEVL--SKKgHSFEVDVWSIGCIMYTLLVGKP-------------------------------PFETS 254
Cdd:cd07852 170 T-DYVAtrwyraPEILlgSTR-YTKGVDMWSVGCILGEMLLGKPlfpgtstlnqlekiievigrpsaediesiqsPFAAT 247
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21359873 255 CLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLP 315
Cdd:cd07852 248 MLESLPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFHNPADEP 308
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
148-300 4.93e-24

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: 103.25  E-value: 4.93e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 148 LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA-----TKVEYDGERKKTLcGTPNYIAPEV 222
Cdd:cd07857 102 LTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLArgfseNPGENAGFMTEYV-ATRWYRAPEI 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 223 -LSKKGHSFEVDVWSIGCIMYTLLVGKPPFETS----------CL-----KETYLRIK--------KNEYSIPK------ 272
Cdd:cd07857 181 mLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKdyvdqlnqilQVlgtpdEETLSRIGspkaqnyiRSLPNIPKkpfesi 260
                       170       180       190
                ....*....|....*....|....*....|
gi 21359873 273 --HINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd07857 261 fpNANPLALDLLEKLLAFDPTKRISVEEAL 290
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
59-305 5.01e-24

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: 102.45  E-value: 5.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKS---LLLKphqreKMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd07847   9 IGEGSYGVVFKCRNRETGQIVAIKKFVESeddPVIK-----KIALrEIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd07847  84 HTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDYVAT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVL---SKKGHSfeVDVWSIGCIMYTLLVGKPPFE-TSCLKETYLRIK--------------KNEY----SIPK 272
Cdd:cd07847 164 RWYRAPELLvgdTQYGPP--VDVWAIGCVFAELLTGQPLWPgKSDVDQLYLIRKtlgdliprhqqifsTNQFfkglSIPE 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 21359873 273 ------------HINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07847 242 petrepleskfpNISSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
81-305 5.58e-24

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: 102.12  E-value: 5.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  81 GKIVP-KSLLLKPHQRE--KMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYY 156
Cdd:cd07846  26 GQIVAiKKFLESEDDKMvkKIAMrEIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTVLDDLEKYPNGLDESRVRKY 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 157 LRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVL---SKKGHSfeVD 233
Cdd:cd07846 106 LFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLvgdTKYGKA--VD 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 234 VWSIGCIMYTLLVGKPPFE-TSCLKETYLRIKKNEYSIPKH------------------------------INPVAASLI 282
Cdd:cd07846 184 VWAVGCLVTEMLTGEPLFPgDSDIDQLYHIIKCLGNLIPRHqelfqknplfagvrlpevkeveplerrypkLSGVVIDLA 263
                       250       260
                ....*....|....*....|...
gi 21359873 283 QKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07846 264 KKCLHIDPDKRPSCSELLHHEFF 286
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
58-303 5.84e-24

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI 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: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 102.20  E-value: 5.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAgkiVPKSLLLKPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDN--DFVFVVLELC 133
Cdd:cd14049  13 RLGKGGYGKVYKVRNKLDGQYYA---IKKILIKKVTKRDCMKVlrEVKVLAGLQHPNIVGYHTAWMEHvqLMLYIQMQLC 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 R---RRSLLELHKRRKALTEPEARYY----------LRQIVLGCQYLHRNRVIHRDLKLGNLFLN-EDLEVKIGDFGLAT 199
Cdd:cd14049  90 ElslWDWIVERNKRPCEEEFKSAPYTpvdvdvttkiLQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLAC 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 200 KVEYDGERKKTLC------------GTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVgkpPFETSCLKETYLRIKKNE 267
Cdd:cd14049 170 PDILQDGNDSTTMsrlnglthtsgvGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---PFGTEMERAEVLTQLRNG 246
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 21359873 268 ySIPKHIN---PVAASLIQKMLQTDPTARPTINELLNDE 303
Cdd:cd14049 247 -QIPKSLCkrwPVQAKYIKLLTSTEPSERPSASQLLESE 284
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
90-305 1.14e-23

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: 100.12  E-value: 1.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  90 LKPHQREKMSMEISIHRSlAHQHVVGFHGFFEDNDFVFVVLElcrrRSLLELH---KRRKALTEPEARYYLRQIVLGCQY 166
Cdd:cd14023  25 VFPLKHYQDKIRPYIQLP-SHRNITGIVEVILGDTKAYVFFE----KDFGDMHsyvRSCKRLREEEAARLFKQIVSAVAH 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 167 LHRNRVIHRDLKLGN-LFLNED---LEVKIGDFGLATKVEYDGERKKTLCgtPNYIAPEVLSKKG--HSFEVDVWSIGCI 240
Cdd:cd14023 100 CHQSAIVLGDLKLRKfVFSDEErtqLRLESLEDTHIMKGEDDALSDKHGC--PAYVSPEILNTTGtySGKSADVWSLGVM 177
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 241 MYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14023 178 LYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERLTAPEILLHPWF 242
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
59-315 1.16e-23

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: 102.43  E-value: 1.16e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQReKMSMEISIHRSLAHQHVVGFHGFF------EDNDFVFVVLEL 132
Cdd:cd07878  23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHAR-RTYRELRLLKHMKHENVIGLLDVFtpatsiENFNEVYLVTNL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 crRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydgERKKTLC 212
Cdd:cd07878 102 --MGADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQAD---DEMTGYV 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 213 GTPNYIAPEVLSKKGHSFE-VDVWSIGCIMYTLLVGKPPFETSCLKETYLRI--------------------KKNEYSIP 271
Cdd:cd07878 177 ATRWYRAPEIMLNWMHYNQtVDIWSVGCIMAELLKGKALFPGNDYIDQLKRImevvgtpspevlkkissehaRKYIQSLP 256
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 272 -----------KHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLP 315
Cdd:cd07878 257 hmpqqdlkkifRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFSQYHDPEDEP 311
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
118-308 1.22e-23

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: 102.90  E-value: 1.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 118 GFFEDndfVFVVLELCRRrsllELHK---RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGD 194
Cdd:cd07853  74 DPFEE---IYVVTELMQS----DLHKiivSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICD 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 195 FGLATKVEYDGERKKTL-CGTPNYIAPEVLSKKGH-SFEVDVWSIGCIMYTLLVGKPPFE----------------TSCL 256
Cdd:cd07853 147 FGLARVEEPDESKHMTQeVVTQYYRAPEILMGSRHyTSAVDIWSVGCIFAELLGRRILFQaqspiqqldlitdllgTPSL 226
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 257 KETY----------LRIKKNE------YSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSG 308
Cdd:cd07853 227 EAMRsacegarahiLRGPHKPpslpvlYTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEG 294
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
59-305 1.44e-23

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: 102.26  E-value: 1.44e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSME---ISIHRSlahQHVVGFHGFFEDNDFVFVVLELC-- 133
Cdd:cd05610  12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAErdaLALSKS---PFIVHLYYSLQSANNVYLVMEYLig 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 -RRRSLLELHKRrkaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA-------------- 198
Cdd:cd05610  89 gDVKSLLHIYGY---FDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnrelnmmdil 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 199 -----------------------------TKVEY-------------DGERkktLCGTPNYIAPEVLSKKGHSFEVDVWS 236
Cdd:cd05610 166 ttpsmakpkndysrtpgqvlslisslgfnTPTPYrtpksvrrgaarvEGER---ILGTPDYLAPELLLGKPHGPAVDWWA 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21359873 237 IGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP---KHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd05610 243 LGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAGLKELKQHPLF 314
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
59-300 1.52e-23

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: 100.37  E-value: 1.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14193  12 LGGGRFGQVHKCEEKSSGLKLAAKIIKAR---SQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL--NEDLEVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd14193  89 FDrIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARRYK-PREKLRVNFGTP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTDPT 291
Cdd:cd14193 168 EFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEdeefADISEEAKDFISKLLIKEKS 247

                ....*....
gi 21359873 292 ARPTINELL 300
Cdd:cd14193 248 WRMSASEAL 256
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-293 1.53e-23

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: 100.99  E-value: 1.53e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFED------NDFVFVVLEL 132
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPEleklspNDLPLLAMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRR---RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKVEyDGE 206
Cdd:cd13989  81 CSGgdlRKVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqqgGGRVIYKLIDLGYAKELD-QGS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 RKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF----------------ETSCLKETYLRIKKNEYS- 269
Cdd:cd13989 160 LCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFlpnwqpvqwhgkvkqkKPEHICAYEDLTGEVKFSs 239
                       250       260       270
                ....*....|....*....|....*....|.
gi 21359873 270 ---IPKHINPVAA----SLIQKMLQTDPTAR 293
Cdd:cd13989 240 elpSPNHLSSILKeyleSWLQLMLRWDPRQR 270
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
59-304 1.55e-23

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: 101.25  E-value: 1.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC--RRR 136
Cdd:cd06634  23 IGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYClgSAS 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKrrKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeydgERKKTLCGTPN 216
Cdd:cd06634 103 DLLEVHK--KPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIM----APANSFVGTPY 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEV---LSKKGHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYlRIKKNEYSI--PKHINPVAASLIQKMLQTDP 290
Cdd:cd06634 177 WMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSALY-HIAQNESPAlqSGHWSEYFRNFVDSCLQKIP 255
                       250
                ....*....|....
gi 21359873 291 TARPTINELLNDEF 304
Cdd:cd06634 256 QDRPTSDVLLKHRF 269
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
58-304 1.56e-23

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: 101.33  E-value: 1.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPksllLKPHQREKMSMEISIHRSLAH-QHVVGFHG-FFEDN-----DFVFVVL 130
Cdd:cd06637  13 LVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKKYSHhRNIATYYGaFIKKNppgmdDQLWLVM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 131 ELCRRRSLLELHKRRKA--LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERK 208
Cdd:cd06637  89 EFCGAGSVTDLIKNTKGntLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTLCGTPNYIAPEVLS-----KKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYL-------RIKKNEYSipkhin 275
Cdd:cd06637 169 NTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLcDMHPMRALFLiprnpapRLKSKKWS------ 242
                       250       260
                ....*....|....*....|....*....
gi 21359873 276 PVAASLIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd06637 243 KKFQSFIESCLVKNHSQRPSTEQLMKHPF 271
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
77-307 1.67e-23

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: 101.90  E-value: 1.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  77 EVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHvvGFHGFFEDNDFVFVvlelcrrrsllELHK-RRKALTEPEARY 155
Cdd:cd07879  55 EIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGD--EFQDFYLVMPYMQT-----------DLQKiMGHPLSEDKVQY 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 156 YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeyDGERKKTLCgTPNYIAPEV-LSKKGHSFEVDV 234
Cdd:cd07879 122 LVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHA--DAEMTGYVV-TRWYRAPEViLNWMHYNQTVDI 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 235 WSIGCIMYTLLVGKPPFE--------TSCLKET------------------YL----RIKKNEYSI--PKhINPVAASLI 282
Cdd:cd07879 199 WSVGCIMAEMLTGKTLFKgkdyldqlTQILKVTgvpgpefvqkledkaaksYIkslpKYPRKDFSTlfPK-ASPQAVDLL 277
                       250       260
                ....*....|....*....|....*
gi 21359873 283 QKMLQTDPTARPTINELLNDEFFTS 307
Cdd:cd07879 278 EKMLELDVDKRLTATEALEHPYFDS 302
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
59-296 1.73e-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: 100.88  E-value: 1.73e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCR---- 134
Cdd:cd08229  32 IGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADagdl 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGT 214
Cdd:cd08229 112 SRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGT 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYL--RIKKNEY-SIPK-HINPVAASLIQKMLQTDP 290
Cdd:cd08229 192 PYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLckKIEQCDYpPLPSdHYSEELRQLVNMCINPDP 271

                ....*.
gi 21359873 291 TARPTI 296
Cdd:cd08229 272 EKRPDI 277
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
76-316 1.99e-23

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: 101.49  E-value: 1.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  76 KEVFAGKIVPKSLLLKPHQR----EKMSMEISIHRSLAHQHVVGFHGFF----EDndfVFVVLELCRRrsllELHK--RR 145
Cdd:cd07856  30 RDQLTGQNVAVKKIMKPFSTpvlaKRTYRELKLLKHLRHENIISLSDIFisplED---IYFVTELLGT----DLHRllTS 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 146 KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydgERKKTLCGTPNYIAPEV-LS 224
Cdd:cd07856 103 RPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQD---PQMTGYVSTRYYRAPEImLT 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 225 KKGHSFEVDVWSIGCIMYTLLVGKPPF------------------------ETSCLKETyLRI-----KKNEYSIP---K 272
Cdd:cd07856 180 WQKYDVEVDIWSAGCIFAEMLEGKPLFpgkdhvnqfsiitellgtppddviNTICSENT-LRFvqslpKRERVPFSekfK 258
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21359873 273 HINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPI 316
Cdd:cd07856 259 NADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHDPTDEPV 302
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
59-316 2.17e-23

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: 101.65  E-value: 2.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCfeISDADTKEVFagKIVPKSLLlKPHQR----EKMSMEISIHRSLAHQHVVGFHGFF-------EDNDfVF 127
Cdd:cd07877  25 VGSGAYGSV--CAAFDTKTGL--RVAVKKLS-RPFQSiihaKRTYRELRLLKHMKHENVIGLLDVFtparsleEFND-VY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 128 VVLELcRRRSLLELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtkvEYDGER 207
Cdd:cd07877  99 LVTHL-MGADLNNIVKCQK-LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLA---RHTDDE 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 KKTLCGTPNYIAPEVLSKKGH-SFEVDVWSIGCIMYTLLVGKPPF-------------------ETSCLKETYLRIKKNE 267
Cdd:cd07877 174 MTGYVATRWYRAPEIMLNWMHyNQTVDIWSVGCIMAELLTGRTLFpgtdhidqlklilrlvgtpGAELLKKISSESARNY 253
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21359873 268 YS----IPKH--------INPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPI 316
Cdd:cd07877 254 IQsltqMPKMnfanvfigANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPV 314
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
78-252 2.18e-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: 99.11  E-value: 2.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  78 VFAGKIVPKSLLLKPHQREKmSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYL 157
Cdd:cd14059   9 VFLGKFRGEEVAVKKVRDEK-ETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPSLLVDWS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 158 RQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGlATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSI 237
Cdd:cd14059  88 KQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFG-TSKELSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSF 166
                       170
                ....*....|....*
gi 21359873 238 GCIMYTLLVGKPPFE 252
Cdd:cd14059 167 GVVLWELLTGEIPYK 181
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-294 2.46e-23

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: 100.42  E-value: 2.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLllKPHQREKMSMEISIHRSLAHQHVVGFHGFFED------NDFVFVVLEL 132
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQEL--SPKNRERWCLEIQIMKRLNHPNVVAARDVPEGlqklapNDLPLLAMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CR---RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED---LEVKIGDFGLATKVEyDGE 206
Cdd:cd14038  80 CQggdLRKYLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGeqrLIHKIIDLGYAKELD-QGS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 RKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK---ETYLRIKKNEYSI------------- 270
Cdd:cd14038 159 LCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPvqwHGKVRQKSNEDIVvyedltgavkfss 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 21359873 271 ----PKHINPVAASLIQKMLQ-----------TDPTARP 294
Cdd:cd14038 239 vlptPNNLNGILAGKLERWLQcmlmwhprqrgTDPPQNP 277
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
59-293 3.66e-23

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: 101.29  E-value: 3.66e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQ----HVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd05633  13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNERIMLSLVSTgdcpFIVCMTYAFHTPDKLCFILDLMN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtkVEYDGERKKTLCGT 214
Cdd:cd05633  92 GGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA--CDFSKKKPHASVGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLsKKGHSFE--VDVWSIGCIMYTLLVGKPPFETSCLKETY----LRIKKNeYSIPKHINPVAASLIQKMLQT 288
Cdd:cd05633 170 HGYMAPEVL-QKGTAYDssADWFSLGCMLFKLLRGHSPFRQHKTKDKHeidrMTLTVN-VELPDSFSPELKSLLEGLLQR 247

                ....*
gi 21359873 289 DPTAR 293
Cdd:cd05633 248 DVSKR 252
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
59-305 6.52e-23

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: 100.84  E-value: 6.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05621  60 IGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDL 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE-RKKTLCGTPNY 217
Cdd:cd05621 140 VNLMSNYD-VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMvHCDTAVGTPDY 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKG----HSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI--KKNEYSIPK--HINPVAASLIQKMLqTD 289
Cdd:cd05621 219 ISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKImdHKNSLNFPDdvEISKHAKNLICAFL-TD 297
                       250
                ....*....|....*....
gi 21359873 290 PT---ARPTINELLNDEFF 305
Cdd:cd05621 298 REvrlGRNGVEEIKQHPFF 316
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
59-299 7.79e-23

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general 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). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk 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: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 98.28  E-value: 7.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVfAGKIVPKSLLLkpHQREkMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd05148  14 LGSGYFGEVWEGLWKNRVRV-AIKILKSDDLL--KQQD-FQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LEL--HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE---YDGERKKtlcg 213
Cdd:cd05148  90 LAFlrSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKedvYLSSDKK---- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKNeYSIPKhinPVA--ASLIQKMLQ-- 287
Cdd:cd05148 166 IPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAG-YRMPC---PAKcpQEIYKIMLEcw 241
                       250
                ....*....|...
gi 21359873 288 -TDPTARPTINEL 299
Cdd:cd05148 242 aAEPEDRPSFKAL 254
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
59-305 1.15e-22

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: 98.93  E-value: 1.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKivpksLLLKPHQREKMSM----EISIHRSLAHQHVV---------GFHGFFEDNDF 125
Cdd:cd07866  16 LGEGTFGEVYKARQIKTGRVVALK-----KILMHNEKDGFPItalrEIKILKKLKHPNVVplidmaverPDKSKRKRGSV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 126 VFVVLELCRRRSLLeLHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtKVEYD- 204
Cdd:cd07866  91 YMVTPYMDHDLSGL-LENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLA-RPYDGp 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 ----------GERKKTLC-GTPNYIAPE-VLSKKGHSFEVDVWSIGCI---MYT---LLVGK--------------PPFE 252
Cdd:cd07866 169 ppnpkgggggGTRKYTNLvVTRWYRPPElLLGERRYTTAVDIWGIGCVfaeMFTrrpILQGKsdidqlhlifklcgTPTE 248
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21359873 253 TSCLKETYLRIKKNEYSIPKHIN----------PVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07866 249 ETWPGWRSLPGCEGVHSFTNYPRtleerfgklgPEGLDLLSKLLSLDPYKRLTASDALEHPYF 311
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
59-293 1.20e-22

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: 98.97  E-value: 1.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQ----HVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd14223   8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNERIMLSLVSTgdcpFIVCMSYAFHTPDKLSFILDLMN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtkVEYDGERKKTLCGT 214
Cdd:cd14223  87 GGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA--CDFSKKKPHASVGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKK-GHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYlRIKKNEYS----IPKHINPVAASLIQKMLQTD 289
Cdd:cd14223 165 HGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKH-EIDRMTLTmaveLPDSFSPELRSLLEGLLQRD 243

                ....
gi 21359873 290 PTAR 293
Cdd:cd14223 244 VNRR 247
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
58-305 1.45e-22

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: 99.18  E-value: 1.45e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKI---VPKslllkphQREKMSMEISIHRSLAHQ------HVVGFHGFFEDNDFVFV 128
Cdd:cd14134  19 LLGEGTFGKVLECWDRKRKRYVAVKIirnVEK-------YREAAKIEIDVLETLAEKdpngksHCVQLRDWFDYRGHMCI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 129 VLELCRRrSLLELHK--RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNEDL----------------- 188
Cdd:cd14134  92 VFELLGP-SLYDFLKknNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENiLLVDSDYvkvynpkkkrqirvpks 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 189 -EVKIGDFGLATkveYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFET-------------- 253
Cdd:cd14134 171 tDIKLIDFGSAT---FDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQThdnlehlammeril 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 254 ------------------------------SCLKETYLRIKKNEYSIPKHINPVAAS---LIQKMLQTDPTARPTINELL 300
Cdd:cd14134 248 gplpkrmirrakkgakyfyfyhgrldwpegSSSGRSIKRVCKPLKRLMLLVDPEHRLlfdLIRKMLEYDPSKRITAKEAL 327

                ....*
gi 21359873 301 NDEFF 305
Cdd:cd14134 328 KHPFF 332
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
59-305 2.04e-22

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 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: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 98.70  E-value: 2.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAgkiVPKSLLLKPHQREKMSMEISIHRSLAHQHVVG-FHGFFEDN-------------D 124
Cdd:cd07854  13 LGCGSNGLVFSAVDSDCDKRVA---VKKIVLTDPQSVKHALREIKIIRRLDHDNIVKvYEVLGPSGsdltedvgsltelN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 FVFVVLELCRR--RSLLElhkrRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN-EDLEVKIGDFGLATKV 201
Cdd:cd07854  90 SVYIVQEYMETdlANVLE----QGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLARIV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 202 EYDGERKKTLC---GTPNYIAPE-VLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-----------------------ETS 254
Cdd:cd07854 166 DPHYSHKGYLSeglVTKWYRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFagaheleqmqlilesvpvvreedRNE 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 255 CLKETYLRIKKNEySIPKH--------INPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07854 246 LLNVIPSFVRNDG-GEPRRplrdllpgVNPEALDFLEQILTFNPMDRLTAEEALMHPYM 303
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
59-304 3.27e-22

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: 97.81  E-value: 3.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC--RRR 136
Cdd:cd06635  33 IGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYClgSAS 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKrrKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeydgERKKTLCGTPN 216
Cdd:cd06635 113 DLLEVHK--KPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIA----SPANSFVGTPY 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 217 YIAPEV---LSKKGHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYlRIKKNEYSI--PKHINPVAASLIQKMLQTDP 290
Cdd:cd06635 187 WMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSALY-HIAQNESPTlqSNEWSDYFRNFVDSCLQKIP 265
                       250
                ....*....|....
gi 21359873 291 TARPTINELLNDEF 304
Cdd:cd06635 266 QDRPTSEELLKHMF 279
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
59-301 3.34e-22

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: 96.81  E-value: 3.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAgkivPKSLLLKPHQREK-MSMEISIHRSLA-HQHVVGFHGFF----EDNDFV---FVV 129
Cdd:cd14036   8 IAEGGFAFVYEAQDVGTGKEYA----LKRLLSNEEEKNKaIIQEINFMKKLSgHPNIVQFCSAAsigkEESDQGqaeYLL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 L-ELCRRrSLLELHKRRKALTEPEARYYLR---QIVLGCQYLHRNR--VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEY 203
Cdd:cd14036  84 LtELCKG-QLVDFVKKVEAPGPFSPDTVLKifyQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAH 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 204 DG------------ERKKTLCGTPNYIAPEVL---SKKGHSFEVDVWSIGCIMYTLLVGKPPFETSclkeTYLRIKKNEY 268
Cdd:cd14036 163 YPdyswsaqkrslvEDEITRNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFEDG----AKLRIINAKY 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 21359873 269 SIPKHIN--PVAASLIQKMLQTDPTARPTINELLN 301
Cdd:cd14036 239 TIPPNDTqyTVFHDLIRSTLKVNPEERLSITEIVE 273
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
58-305 5.10e-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: 95.80  E-value: 5.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKMSmEISIHRSLA------HQHVVGFHGFFEDNDFVFVVLE 131
Cdd:cd14133   6 VLGKGTFGQVVKCYDLLTGEEVALKIIKNN---KDYLDQSLD-EIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCIVFE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRrSLLELHK--RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL--NEDLEVKIGDFGLATkveYDGER 207
Cdd:cd14133  82 LLSQ-NLYEFLKqnKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGSSC---FLTQR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 208 KKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHI-------NPVAAS 280
Cdd:cd14133 158 LYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMldqgkadDELFVD 237
                       250       260
                ....*....|....*....|....*
gi 21359873 281 LIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14133 238 FLKKLLEIDPKERPTASQALSHPWL 262
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
59-274 8.15e-22

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: 96.14  E-value: 8.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFED-----NDFVFVVLELC 133
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSC--RLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEmnflvNDVPLLAMEYC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RR---RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE---DLEVKIGDFGLATKVEyDGER 207
Cdd:cd14039  79 SGgdlRKLLNKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEingKIVHKIIDLGYAKDLD-QGSL 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 208 KKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYL-RIKKNEysiPKHI 274
Cdd:cd14039 158 CTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNLQPFTWHeKIKKKD---PKHI 222
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
58-305 8.59e-22

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: 96.28  E-value: 8.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREK----MSMEISIHRSLAHQHVVGFHGFFE-DNDFVFVVLEL 132
Cdd:cd14041  13 LLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENyhkhACREYRIHKELDHPRIVKLYDYFSlDTDSFCTVLEY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR--VIHRDLKLGNLFLNEDL---EVKIGDFGLATKVEYDG-- 205
Cdd:cd14041  93 CEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTacgEIKITDFGLSKIMDDDSyn 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 -----ERKKTLCGTPNYIAPE--VLSKKGH--SFEVDVWSIGCIMYTLLVGKPPF-----ETSCLKETYLrIKKNEYSIP 271
Cdd:cd14041 173 svdgmELTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFYQCLYGRKPFghnqsQQDILQENTI-LKATEVQFP 251
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21359873 272 KH--INPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14041 252 PKpvVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
59-293 1.22e-21

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: 95.20  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQH-----VVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05606   2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRI-KMKQGETLALNERIMLSLVSTGgdcpfIVCMTYAFQTPDKLCFILDLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtkVEYDGERKKTLCG 213
Cdd:cd05606  81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA--CDFSKKKPHASVG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSK-KGHSFEVDVWSIGCIMYTLLVGKPPFETSCLK---ETYLRIKKNEYSIPKHINPVAASLIQKMLQTD 289
Cdd:cd05606 159 THGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKdkhEIDRMTLTMNVELPDSFSPELKSLLEGLLQRD 238

                ....
gi 21359873 290 PTAR 293
Cdd:cd05606 239 VSKR 242
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
58-300 1.24e-21

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: 94.76  E-value: 1.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEisdADTK-EVFAGKIVPKslllkphQREKMSMEISIHR-----SLAHQHVV---GFHGFFEDNDFVFV 128
Cdd:cd13979  10 PLGSGGFGSVYK---ATYKgETVAVKIVRR-------RRKNRASRQSFWAelnaaRLRHENIVrvlAAETGTDFASLGLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 129 VLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD--- 204
Cdd:cd13979  80 IMEYCGNGTLQQlIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGnev 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETscLKET--YLRIKKNEYSIPKHI-----NPV 277
Cdd:cd13979 160 GTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAG--LRQHvlYAVVAKDLRPDLSGLedsefGQR 237
                       250       260
                ....*....|....*....|...
gi 21359873 278 AASLIQKMLQTDPTARPTINELL 300
Cdd:cd13979 238 LRSLISRCWSAQPAERPNADESL 260
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
101-305 2.39e-21

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: 94.26  E-value: 2.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLA-HQHVVGFHGFFEDND-----FVFVVLELcrrrSLLELHK-RRKALTEPEARYYLRQIVLGCQYLHRNRVI 173
Cdd:cd07831  47 EIQALRRLSpHPNILRLIEVLFDRKtgrlaLVFELMDM----NLYELIKgRKRPLPEKRVKNYMYQLLKSLDHMHRNGIF 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLeVKIGDFGLAtkveydgerkKTLCGTP---NYI------APEVLSKKG-HSFEVDVWSIGCIMYT 243
Cdd:cd07831 123 HRDIKPENILIKDDI-LKLADFGSC----------RGIYSKPpytEYIstrwyrAPECLLTDGyYGPKMDIWAVGCVFFE 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 244 LLVGKPPFE------------------TSCLKETYLRIKKNEYSIPK-----------HINPVAASLIQKMLQTDPTARP 294
Cdd:cd07831 192 ILSLFPLFPgtneldqiakihdvlgtpDAEVLKKFRKSRHMNYNFPSkkgtglrkllpNASAEGLDLLKKLLAYDPDERI 271
                       250
                ....*....|.
gi 21359873 295 TINELLNDEFF 305
Cdd:cd07831 272 TAKQALRHPYF 282
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
92-251 2.66e-21

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: 93.97  E-value: 2.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  92 PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVfVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRN 170
Cdd:cd14151  45 PQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLA-IVTQWCEGSSLYHhLHIIETKFEMIKLIDIARQTAQGMDYLHAK 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 171 RVIHRDLKLGNLFLNEDLEVKIGDFGLAT-KVEYDGERK-KTLCGTPNYIAPEVL---SKKGHSFEVDVWSIGCIMYTLL 245
Cdd:cd14151 124 SIIHRDLKSNNIFLHEDLTVKIGDFGLATvKSRWSGSHQfEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELM 203

                ....*.
gi 21359873 246 VGKPPF 251
Cdd:cd14151 204 TGQLPY 209
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
59-305 3.82e-21

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: 93.06  E-value: 3.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGF-------AKCFEISDADTKEVFAGK-IVPKSLllkPHqreKMSMEISI-HRSLAHQHVVGFHGFFEDNDFVFVV 129
Cdd:cd14019   9 IGEGTFssvykaeDKLHDLYDRNKGRLVALKhIYPTSS---PS---RILNELEClERLGGSNNVSGLITAFRNEDQVVAV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSLLELHKRrkaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEV-KIGDFGLATKVEYDGERK 208
Cdd:cd14019  83 LPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKgVLVDFGLAQREEDRPEQR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KTLCGTPNYIAPEVLSKKGH-SFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLrikKNEYSIPKHinPVAASLIQKMLQ 287
Cdd:cd14019 160 APRAGTRGFRAPEVLFKCPHqTTAIDIWSAGVILLSILSGRFPFFFSSDDIDAL---AEIATIFGS--DEAYDLLDKLLE 234
                       250
                ....*....|....*...
gi 21359873 288 TDPTARPTINELLNDEFF 305
Cdd:cd14019 235 LDPSKRITAEEALKHPFF 252
POLO_box pfam00659
POLO box duplicated region;
517-580 4.71e-21

POLO box duplicated region;


Pssm-ID: 459894  Cd Length: 61  Bit Score: 86.79  E-value: 4.71e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21359873   517 TRSAIILHLSNGSVQINFfQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLeeYGCCKELASRL 580
Cdd:pfam00659   1 TKYGIGYQLSNGTVQVNF-NDHTKIILSPDGKAVTYIDKEGERRTYTLSTL--SGCPEDLKKKL 61
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
58-305 5.08e-21

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: 93.97  E-value: 5.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREK----MSMEISIHRSLAHQHVVGFHGFFE-DNDFVFVVLEL 132
Cdd:cd14040  13 LLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR--VIHRDLKLGNLFLNEDL---EVKIGDFGLATKVEYDG-- 205
Cdd:cd14040  93 CEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDDDSyg 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 ----ERKKTLCGTPNYIAPE--VLSKKGH--SFEVDVWSIGCIMYTLLVGKPPF-----ETSCLKE-TYLRIKKNEYSIP 271
Cdd:cd14040 173 vdgmDLTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPFghnqsQQDILQEnTILKATEVQFPVK 252
                       250       260       270
                ....*....|....*....|....*....|....
gi 21359873 272 KHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14040 253 PVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
136-305 5.98e-21

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: 92.41  E-value: 5.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELH---KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN--EDLEVKIGDFGLATKVEYDGERKKT 210
Cdd:cd14022  66 RSYGDMHsfvRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKdeERTRVKLESLEDAYILRGHDDSLSD 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKKGhSFE---VDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQ 287
Cdd:cd14022 146 KHGCPAYVSPEILNTSG-SYSgkaADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILR 224
                       170
                ....*....|....*...
gi 21359873 288 TDPTARPTINELLNDEFF 305
Cdd:cd14022 225 REPSERLTSQEILDHPWF 242
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
92-251 7.95e-21

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: 92.39  E-value: 7.95e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  92 PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVfVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRN 170
Cdd:cd14150  37 PEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFA-IITQWCEGSSLYRhLHVTETRFDTMQLIDVARQTAQGMDYLHAK 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 171 RVIHRDLKLGNLFLNEDLEVKIGDFGLAT-KVEYDGERK-KTLCGTPNYIAPEVLSKKG---HSFEVDVWSIGCIMYTLL 245
Cdd:cd14150 116 NIIHRDLKSNNIFLHEGLTVKIGDFGLATvKTRWSGSQQvEQPSGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELM 195

                ....*.
gi 21359873 246 VGKPPF 251
Cdd:cd14150 196 SGTLPY 201
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
101-254 8.91e-21

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: 92.41  E-value: 8.91e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLEL-HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKL 179
Cdd:cd14063  46 EVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCKGRTLYSLiHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKS 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 180 GNLFLnEDLEVKIGDFGL--ATKVEYDGERKKTLcGTPN----YIAPEVL----------SKKGHSFEVDVWSIGCIMYT 243
Cdd:cd14063 126 KNIFL-ENGRVVITDFGLfsLSGLLQPGRREDTL-VIPNgwlcYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYE 203
                       170
                ....*....|.
gi 21359873 244 LLVGKPPFETS 254
Cdd:cd14063 204 LLAGRWPFKEQ 214
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
60-315 9.78e-21

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 94.68  E-value: 9.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   60 GKGGFAkcFEISDADTKEvfagkivpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLElcRRRSLL 139
Cdd:PHA03212 103 GAEGFA--FACIDNKTCE---------HVVIKAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILP--RYKTDL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  140 ELH---KRRKALTEPEA--RYYLRQIvlgcQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAT-KVEYDGERKKTLCG 213
Cdd:PHA03212 170 YCYlaaKRNIAICDILAieRSVLRAI----QYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACfPVDINANKYYGWAG 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGK---------------------------------PPFETSCLKETY 260
Cdd:PHA03212 246 TIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHdslfekdgldgdcdsdrqikliirrsgthpnefPIDAQANLDEIY 325
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873  261 LRIKK-------------NEYSIPKHINpvaaSLIQKMLQTDPTARPTINELLNDEFFTSgyIPARLP 315
Cdd:PHA03212 326 IGLAKkssrkpgsrplwtNLYELPIDLE----YLICKMLAFDAHHRPSAEALLDFAAFQD--IPDPYP 387
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
106-300 1.16e-20

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: 91.48  E-value: 1.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 106 RSLAHQHVVGFHGFFEDNDFVFVVLElcrrRSLLELH---KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNL 182
Cdd:cd14024  40 RLGPHEGVCSVLEVVIGQDRAYAFFS----RHYGDMHshvRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRF 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 183 FLNEDLEVKIGDFGLATKVEYDGERKKTL--CGTPNYIAPEVLSKkGHSFE---VDVWSIGCIMYTLLVGKPPFETSCLK 257
Cdd:cd14024 116 VFTDELRTKLVLVNLEDSCPLNGDDDSLTdkHGCPAYVGPEILSS-RRSYSgkaADVWSLGVCLYTMLLGRYPFQDTEPA 194
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21359873 258 ETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14024 195 ALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPAERLKASEIL 237
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
59-295 1.17e-20

Catalytic domain 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. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. 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. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-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: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 91.58  E-value: 1.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAkcfeisdadtkEVFAGK------IVPKSLllKPHQrekMSM-----EISIHRSLAHQHVVGFHGFFEDNDFVF 127
Cdd:cd05034   3 LGAGQFG-----------EVWMGVwngttkVAVKTL--KPGT---MSPeaflqEAQIMKKLRHDKLVQLYAVCSDEEPIY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 128 VVLELCRRRSLLELHK--RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDG 205
Cdd:cd05034  67 IVTELMSKGSLLDYLRtgEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDE 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 ERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKNeYSIPKHIN-PvaASLI 282
Cdd:cd05034 147 YTAREGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVLEQVERG-YRMPKPPGcP--DELY 223
                       250
                ....*....|....*.
gi 21359873 283 QKMLQT---DPTARPT 295
Cdd:cd05034 224 DIMLQCwkkEPEERPT 239
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
59-245 1.32e-20

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: 92.44  E-value: 1.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAK----CFEISDADTKEVFAGKIVPKSLllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDF--VFVVLEL 132
Cdd:cd05038  12 LGEGHFGSvelcRYDPLGDNTGEQVAVKSLQPSG--EEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRrsLRLIMEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE--RKK 209
Cdd:cd05038  90 LPSGSLRDyLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEyyYVK 169
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21359873 210 TLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL 245
Cdd:cd05038 170 EPGESPiFWYAPECLRESRFSSASDVWSFGVTLYELF 206
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
92-251 1.61e-20

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: 92.02  E-value: 1.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  92 PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVfVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRN 170
Cdd:cd14149  49 PEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLA-IVTQWCEGSSLYKhLHVQETKFQMFQLIDIARQTAQGMDYLHAK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 171 RVIHRDLKLGNLFLNEDLEVKIGDFGLAT-KVEYDGERK-KTLCGTPNYIAPEVLSKKGH---SFEVDVWSIGCIMYTLL 245
Cdd:cd14149 128 NIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRWSGSQQvEQPTGSILWMAPEVIRMQDNnpfSFQSDVYSYGIVLYELM 207

                ....*.
gi 21359873 246 VGKPPF 251
Cdd:cd14149 208 TGELPY 213
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
58-305 1.64e-20

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: 92.73  E-value: 1.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEisdADTKEVFAGKIVP-KSLLLKPHQREKMSM----EISIHRSLAHQHVVGFHG-FFEDNDF-VFVVL 130
Cdd:cd07842   7 CIGRGTYGRVYK---AKRKNGKDGKEYAiKKFKGDKEQYTGISQsacrEIALLRELKHENVVSLVEvFLEHADKsVYLLF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 131 ELCRRrSLLEL-----HKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL----NEDLEVKIGDFGLATKV 201
Cdd:cd07842  84 DYAEH-DLWQIikfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGLARLF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 202 E------YDGERkktLCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKPPF--ETSCLKET------------- 259
Cdd:cd07842 163 NaplkplADLDP---VVVTIWYRAPELlLGARHYTKAIDIWAIGCIFAELLTLEPIFkgREAKIKKSnpfqrdqlerife 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 260 ------------------YLRIKKNE-------------YSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07842 240 vlgtptekdwpdikkmpeYDTLKSDTkastypnsllakwMHKHKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPYF 316
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
59-305 1.68e-20

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: 91.71  E-value: 1.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADT-KEVFAGKIVPKSLLLKPHQREKMSMEISihRSLAHQHVVGFHGFFED----NDFVFVVLELC 133
Cdd:cd14031  18 LGRGAFKTVYKGLDTETwVEVAWCELQDRKLTKAEQQRFKEEAEML--KGLQHPNIVRFYDSWESvlkgKKCIVLVTELM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR--VIHRDLKLGNLFLNEDL-EVKIGDFGLATKVEydGERKKT 210
Cdd:cd14031  96 TSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLMR--TSFAKS 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEvLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKK--NEYSIPKHINPVAASLIQKMLQ 287
Cdd:cd14031 174 VIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRKVTSgiKPASFNKVTDPEVKEIIEGCIR 252
                       250
                ....*....|....*...
gi 21359873 288 TDPTARPTINELLNDEFF 305
Cdd:cd14031 253 QNKSERLSIKDLLNHAFF 270
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
101-307 1.85e-20

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: 91.99  E-value: 1.85e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLG 180
Cdd:cd07873  50 EVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQ 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 181 NLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCL--- 256
Cdd:cd07873 130 NLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVeeq 209
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 257 ------------KETYLRIKKNE----YSIPKH-----------INPVAASLIQKMLQTDPTARPTINELLNDEFFTS 307
Cdd:cd07873 210 lhfifrilgtptEETWPGILSNEefksYNYPKYradalhnhaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHS 287
POLO_box pfam00659
POLO box duplicated region;
419-476 2.31e-20

POLO box duplicated region;


Pssm-ID: 459894  Cd Length: 61  Bit Score: 84.86  E-value: 2.31e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21359873   419 DKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVS---SHPNSLMKKI 476
Cdd:pfam00659   1 TKYGIGYQLSNGTVQVNFNDHTKIILSPDGKAVTYIDKEGERRTYTLStlsGCPEDLKKKL 61
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
92-299 2.77e-20

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: 90.94  E-value: 2.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  92 PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDfVFVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRN 170
Cdd:cd05056  48 PSVREKFLQEAYIMRQFDHPHIVKLIGVITENP-VWIVMELAPLGELRSyLQVNKYSLDLASLILYAYQLSTALAYLESK 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 171 RVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIG-CIMYTLLVGK 248
Cdd:cd05056 127 RFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGvCMWEILMLGV 206
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21359873 249 PPFETSCLKETYLRIKKNE-YSIPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05056 207 KPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTEL 258
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
59-300 3.01e-20

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: 91.11  E-value: 3.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAK----CFEISDADTKEVFAGKIVPKSLllKPHQREKMSMEISIHRSLAHQHVVGFHGFFED--NDFVFVVLEL 132
Cdd:cd05080  12 LGEGHFGKvslyCYDPTNDGTGEMVAVKALKADC--GPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqgGKSLQLIMEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKV----EY----- 203
Cdd:cd05080  90 VPLGSLRDYLPKHS-IGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVpeghEYyrvre 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 204 DGErkktlcgTPNY-IAPEVLSKKGHSFEVDVWSIGCIMYTLL----------------VGKPPFETSCLKETYLRIKKN 266
Cdd:cd05080 169 DGD-------SPVFwYAPECLKEYKFYYASDVWSFGVTLYELLthcdssqspptkflemIGIAQGQMTVVRLIELLERGE 241
                       250       260       270
                ....*....|....*....|....*....|....
gi 21359873 267 EYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd05080 242 RLPCPDKCPQEVYHLMKNCWETEASFRPTFENLI 275
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
62-254 3.56e-20

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: 90.94  E-value: 3.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  62 GGFAKCFeisDADTKEVFAGKIVPKSLllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDN--DFVFVVLELCRRRSLL 139
Cdd:cd06621  15 GSVTKCR---LRNTKTIFALKTITTDP--NPDVQKQILRELEINKSCASPYIVKYYGAFLDEqdSSIGIAMEYCEGGSLD 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 140 ELHKRRKALTEPEARYYLRQI---VL-GCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATkvEYDGERKKTLCGTP 215
Cdd:cd06621  90 SIYKKVKKKGGRIGEKVLGKIaesVLkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSG--ELVNSLAGTFTGTS 167
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETS 254
Cdd:cd06621 168 YYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPE 206
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
58-302 3.78e-20

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: 90.29  E-value: 3.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCF---EISDadtKEVFAGKIVPKSLLLkphQREKMS------MEISIHRSL----AHQHVVGFHGFFEDND 124
Cdd:cd14101   7 LLGKGGFGTVYaghRISD---GLQVAIKQISRNRVQ---QWSKLPgvnpvpNEVALLQSVgggpGHRGVIRLLDWFEIPE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 FVFVVLELCRR-RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLneDL---EVKIGDFG---- 196
Cdd:cd14101  81 GFLLVLERPQHcQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV--DLrtgDIKLIDFGsgat 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 197 LATKVEYDGErkktlcGTPNYIAPE-VLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSclketyLRIKKNEYSIPKHIN 275
Cdd:cd14101 159 LKDSMYTDFD------GTRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPFERD------TDILKAKPSFNKRVS 226
                       250       260
                ....*....|....*....|....*..
gi 21359873 276 PVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd14101 227 NDCRSLIRSCLAYNPSDRPSLEQILLH 253
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
59-300 4.07e-20

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: 90.63  E-value: 4.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQrekMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14664   1 IGRGGAGTVYKGVMPNGTLVAVKRLKGEGTQGGDHG---FQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEP---EARYYLR-QIVLGCQYLHRN---RVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDG-ERKKT 210
Cdd:cd14664  78 GELLHSRPESQPPldwETRQRIAlGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDsHVMSS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKE-----TYLRiKKNEYSIPKHI-------NPVA 278
Cdd:cd14664 158 VAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDgvdivDWVR-GLLEEKKVEALvdpdlqgVYKL 236
                       250       260
                ....*....|....*....|....*...
gi 21359873 279 ASLIQKM------LQTDPTARPTINELL 300
Cdd:cd14664 237 EEVEQVFqvallcTQSSPMERPTMREVV 264
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
59-306 4.24e-20

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: 90.95  E-value: 4.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIhRSLAHQHVVGFHG-FFEDNDfVFVVLELcRRRS 137
Cdd:cd06617   9 LGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQKRLLMDLDISM-RSVDCPYTVTFYGaLFREGD-VWICMEV-MDTS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKR--RKALTEPE---ARYYLrQIVLGCQYLHRN-RVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeYDGERKKTL 211
Cdd:cd06617  86 LDKFYKKvyDKGLTIPEdilGKIAV-SIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYL-VDSVAKTID 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPE----VLSKKGHSFEVDVWSIGCIMYTLLVGKPPFET---------SCLKETYLRIKKNEYSipkhinPVA 278
Cdd:cd06617 164 AGCKPYMAPErinpELNQKGYDVKSDVWSLGITMIELATGRFPYDSwktpfqqlkQVVEEPSPQLPAEKFS------PEF 237
                       250       260
                ....*....|....*....|....*...
gi 21359873 279 ASLIQKMLQTDPTARPTINELLNDEFFT 306
Cdd:cd06617 238 QDFVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
59-252 4.83e-20

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: 90.73  E-value: 4.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd05607  10 LGKGGFGEVCAVQVKNTGQMYACKKLDKKRL-KKKSGEKMALlEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLE--LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGTP 215
Cdd:cd05607  89 LKYhiYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVK-EGKPITQRAGTN 167
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFE 252
Cdd:cd05607 168 GYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFR 204
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
59-300 5.00e-20

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: 90.64  E-value: 5.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCF--EISDadtKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd14158  23 LGEGGFGVVFkgYIND---KNVAVKKLAAMVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLElhkRRKALTE-PEARYYLR-QIVLGC----QYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKT 210
Cdd:cd14158 100 SLLD---RLACLNDtPPLSWHMRcKIAQGTangiNYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTIMT 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 --LCGTPNYIAPEVLskKGH-SFEVDVWSIGCIMYTLLVGKPPF----ETSCLKETYLRIKKNEYSI-----------PK 272
Cdd:cd14158 177 erIVGTTAYMAPEAL--RGEiTPKSDIFSFGVVLLEIITGLPPVdenrDPQLLLDIKEEIEDEEKTIedyvdkkmgdwDS 254
                       250       260
                ....*....|....*....|....*...
gi 21359873 273 HINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14158 255 TSIEAMYSVASQCLNDKKNRRPDIAKVQ 282
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
101-305 8.67e-20

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: 91.00  E-value: 8.67e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFF---EDNDF--VFVVLELCRRrsllELHKRRKA---LTEPEARYYLRQIVLGCQYLHRNRV 172
Cdd:cd07859  49 EIKLLRLLRHPDIVEIKHIMlppSRREFkdIYVVFELMES----DLHQVIKAnddLTPEHHQFFLYQLLRALKYIHTANV 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 173 IHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERK---KTLCGTPNYIAPEV----LSKkgHSFEVDVWSIGCIMYTLL 245
Cdd:cd07859 125 FHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAifwTDYVATRWYRAPELcgsfFSK--YTPAIDIWSIGCIFAEVL 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 246 VGKPPFE-----------TSCL---------------KETYLRIKKNEYSIP-----KHINPVAASLIQKMLQTDPTARP 294
Cdd:cd07859 203 TGKPLFPgknvvhqldliTDLLgtpspetisrvrnekARRYLSSMRKKQPVPfsqkfPNADPLALRLLERLLAFDPKDRP 282
                       250
                ....*....|.
gi 21359873 295 TINELLNDEFF 305
Cdd:cd07859 283 TAEEALADPYF 293
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
59-254 1.17e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 93.65  E-value: 1.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873    59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFF--EDNDFVFVVLELCR-- 134
Cdd:PTZ00266   21 IGNGRFGEVFLVKHKRTQEFFCWKAISYRGL-KEREKSQLVIEVNVMRELKHKNIVRYIDRFlnKANQKLYILMEFCDag 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   135 --RRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHR-------NRVIHRDLKLGNLFLNEDLE---------------- 189
Cdd:PTZ00266  100 dlSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGIRhigkitaqannlngrp 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873   190 -VKIGDFGLATKVEYDgERKKTLCGTPNYIAPEVLSKKGHSFE--VDVWSIGCIMYTLLVGKPPFETS 254
Cdd:PTZ00266  180 iAKIGDFGLSKNIGIE-SMAHSCVGTPYYWSPELLLHETKSYDdkSDMWALGCIIYELCSGKTPFHKA 246
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
59-305 1.20e-19

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: 90.12  E-value: 1.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpksllLKPHQREKMSM----EISIHRSLAHQHVV--------------GFHGFF 120
Cdd:cd07865  20 IGQGTFGEVFKARHRKTGQIVALKKV-----LMENEKEGFPItalrEIKILQLLKHENVVnlieicrtkatpynRYKGSI 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 121 edndfvFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA-- 198
Cdd:cd07865  95 ------YLVFEFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLAra 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 199 --TKVEYDGERKKTLCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIM---------------------YTLLVGK------ 248
Cdd:cd07865 169 fsLAKNSQPNRYTNRVVTLWYRPPELlLGERDYGPPIDMWGAGCIMaemwtrspimqgnteqhqltlISQLCGSitpevw 248
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21359873 249 ------PPFETSCLKETYLRIKKNEYSiPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07865 249 pgvdklELFKKMELPQGQKRKVKERLK-PYVKDPYALDLIDKLLVLDPAKRIDADTALNHDFF 310
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
59-309 1.78e-19

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: 88.71  E-value: 1.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAK---CFEisdadtkeVFAGKIVPKSLLLKPHQ---REKMSMEISIHRSLAHQHVVGFHG-FFEDNDFVfVVLE 131
Cdd:cd14027   1 LDSGGFGKvslCFH--------RTQGLVVLKTVYTGPNCiehNEALLEEGKMMNRLRHSRVVKLLGvILEEGKYS-LVME 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRRSLLELHKRRKALTEPEARYYLrQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA--------TKVEY 203
Cdd:cd14027  72 YMEKGNLMHVLKKVSVPLSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklTKEEH 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 204 DGERK-----KTLCGTPNYIAPEVL-SKKGHSFE-VDVWSIGCIMYTLLVGKPPFEtSCLKE---TYLRIKKN---EYSI 270
Cdd:cd14027 151 NEQREvdgtaKKNAGTLYYMAPEHLnDVNAKPTEkSDVYSFAIVLWAIFANKEPYE-NAINEdqiIMCIKSGNrpdVDDI 229
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 21359873 271 PKHINPVAASLIQKMLQTDPTARPTINELlnDEFFTSGY 309
Cdd:cd14027 230 TEYCPREIIDLMKLCWEANPEARPTFPGI--EEKFRPFY 266
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
59-304 1.96e-19

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: 89.09  E-value: 1.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllkpHQREKMSM----EISIHRSLAHQHVVGFH----------GFFEDND 124
Cdd:cd07864  15 IGEGTYGQVYKAKDKDTGELVALKKVRLD-----NEKEGFPItairEIKILRQLNHRSVVNLKeivtdkqdalDFKKDKG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 FVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD 204
Cdd:cd07864  90 AFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLYNSE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKT-LCGTPNYIAPE-VLSKKGHSFEVDVWSIGCIMYTLLVGKPPFE------------------------------ 252
Cdd:cd07864 170 ESRPYTnKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQanqelaqlelisrlcgspcpavwpdviklp 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 253 ---TSCLKETYLRIKKNEYSipkHINPVAASLIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd07864 250 yfnTMKPKKQYRRRLREEFS---FIPTPALDLLDHMLTLDPSKRCTAEQALNSPW 301
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
59-300 2.42e-19

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: 87.93  E-value: 2.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIvpkslLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKE-----LKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKR-RKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL---NEDLEVKIGDFGLATKV----EYDGERKK- 209
Cdd:cd14065  76 EELLKSmDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMpdekTKKPDRKKr 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 -TLCGTPNYIAPEVLSKKGHSFEVDVWSIGcIMYTLLVGKPPFETSCLKETY---LRIKKNEYSIPKHINPVAASLIQKM 285
Cdd:cd14065 156 lTVVGSPYWMAPEMLRGESYDEKVDVFSFG-IVLCEIIGRVPADPDYLPRTMdfgLDVRAFRTLYVPDCPPSFLPLAIRC 234
                       250
                ....*....|....*
gi 21359873 286 LQTDPTARPTINELL 300
Cdd:cd14065 235 CQLDPEKRPSFVELE 249
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
95-304 3.71e-19

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 89.11  E-value: 3.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   95 REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLlelhKRRKALTEPEARYYLRQIVLGCQYLHRNRVIH 174
Cdd:PLN00034 116 RRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSL----EGTHIADEQFLADVARQILSGIAYLHRRHIVH 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  175 RDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSK-----KGHSFEVDVWSIGCIMYTLLVGKP 249
Cdd:PLN00034 192 RDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTdlnhgAYDGYAGDIWSLGVSILEFYLGRF 271
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  250 PFETSCLKETYLRIKKNEYSIPKHInPVAAS-----LIQKMLQTDPTARPTINELLNDEF 304
Cdd:PLN00034 272 PFGVGRQGDWASLMCAICMSQPPEA-PATASrefrhFISCCLQREPAKRWSAMQLLQHPF 330
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
101-305 4.55e-19

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: 87.73  E-value: 4.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELcrrrslLEL-------HKRRKALTEPEARYYLRQIVLGCQYLHRNRVI 173
Cdd:cd07835  48 EISLLKELNHPNIVRLLDVVHSENKLYLVFEF------LDLdlkkymdSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVL 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKV-----EYDGErKKTLCgtpnYIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVG 247
Cdd:cd07835 122 HRDLKPQNLLIDTEGALKLADFGLARAFgvpvrTYTHE-VVTLW----YRAPEILlGSKHYSTPVDIWSVGCIFAEMVTR 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 248 KPPF-------------------------ETSCL---KETYLRIKKNEYS--IPKHiNPVAASLIQKMLQTDPTARPTIN 297
Cdd:cd07835 197 RPLFpgdseidqlfrifrtlgtpdedvwpGVTSLpdyKPTFPKWARQDLSkvVPSL-DEDGLDLLSQMLVYDPAKRISAK 275

                ....*...
gi 21359873 298 ELLNDEFF 305
Cdd:cd07835 276 AALQHPYF 283
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
90-301 7.77e-19

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: 86.64  E-value: 7.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  90 LKPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKR-RKALTEPEARYYLRQIVLGCQ 165
Cdd:cd05039  37 LKDDSTAAQAFlaEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSLVDyLRSRgRAVITRKDQLGFALDVCEGME 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 166 YLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKtlcgTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTL 244
Cdd:cd05039 117 YLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSNQDGGK----LPiKWTAPEALREKKFSTKSDVWSFGILLWEI 192
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 245 L-VGKPPFETSCLKETYLRIKKNeYSI------PKHInpvaaslIQKMLQT---DPTARPTINELLN 301
Cdd:cd05039 193 YsFGRVPYPRIPLKDVVPHVEKG-YRMeapegcPPEV-------YKVMKNCwelDPAKRPTFKQLRE 251
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
159-300 9.28e-19

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: 86.29  E-value: 9.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNR---VIHRDLKLGNLFL-----NEDLE---VKIGDFGLATkvEYDGERKKTLCGTPNYIAPEVLSKKG 227
Cdd:cd14061 100 QIARGMNYLHNEApvpIIHRDLKSSNILIleaieNEDLEnktLKITDFGLAR--EWHKTTRMSAAGTYAWMAPEVIKSST 177
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 228 HSFEVDVWSIGCIMYTLLVGKPPFE-TSCLKETY-LRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14061 178 FSKASDVWSYGVLLWELLTGEVPYKgIDGLAVAYgVAVNKLTLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADIL 252
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
59-305 1.02e-18

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: 86.21  E-value: 1.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTK-EVFAGKIVPKSLllKPHQREKMSMEISIHRSLAHQHVVGFHGFFED----NDFVFVVLELC 133
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTvEVAWCELQTRKL--SKGERQRFSEEVEMLKGLQHPNIVRFYDSWKStvrgHKCIILVTELM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR--VIHRDLKLGNLFLN-EDLEVKIGDFGLATKVEydGERKKT 210
Cdd:cd14033  87 TSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATLKR--ASFAKS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKKgHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKK--NEYSIPKHINPVAASLIQKMLQ 287
Cdd:cd14033 165 VIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYsECQNAAQIYRKVTSgiKPDSFYKVKVPELKEIIEGCIR 243
                       250
                ....*....|....*...
gi 21359873 288 TDPTARPTINELLNDEFF 305
Cdd:cd14033 244 TDKDERFTIQDLLEHRFF 261
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
138-305 1.05e-18

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 86.45  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE-VKIGDFGLA----TKVEYDgerkktlc 212
Cdd:PHA03390  96 LFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDrIYLCDYGLCkiigTPSCYD-------- 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  213 GTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETS---CLK-ETYLRIKKNEYSIPKHINPVAASLIQKMLQT 288
Cdd:PHA03390 168 GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDedeELDlESLLKRQQKKLPFIKNVSKNANDFVQSMLKY 247
                        170
                 ....*....|....*...
gi 21359873  289 DPTAR-PTINELLNDEFF 305
Cdd:PHA03390 248 NINYRlTNYNEIIKHPFL 265
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
101-307 1.28e-18

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: 86.25  E-value: 1.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKA--LTEPEARYYLRQIVLGCQYLHRNRVIHRDLK 178
Cdd:cd05072  52 EANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLLDFLKSDEGgkVLLPKLIDFSAQIAEGMAYIERKNYIHRDLR 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 179 LGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCL 256
Cdd:cd05072 132 AANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSN 211
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 257 KETYLRIKKNeYSIPKHIN-PVAASLIQKMLQTD-PTARPTINELLN--DEFFTS 307
Cdd:cd05072 212 SDVMSALQRG-YRMPRMENcPDELYDIMKTCWKEkAEERPTFDYLQSvlDDFYTA 265
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
107-302 1.56e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 89.08  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  107 SLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNE 186
Cdd:NF033483  63 SLSHPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITK 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  187 DLEVKIGDFGLA-----TKVEYDGerkkTLCGTPNYIAPE-----VLSKKghsfeVDVWSIGCIMYTLLVGKPPF--ETS 254
Cdd:NF033483 143 DGRVKVTDFGIAralssTTMTQTN----SVLGTVHYLSPEqarggTVDAR-----SDIYSLGIVLYEMLTGRPPFdgDSP 213
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21359873  255 clketylrikkneYSI-----------PKHINP-VAASL---IQKMLQTDPTARP-TINELLND 302
Cdd:NF033483 214 -------------VSVaykhvqedpppPSELNPgIPQSLdavVLKATAKDPDDRYqSAAEMRAD 264
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
101-258 1.68e-18

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: 86.22  E-value: 1.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLG 180
Cdd:cd07871  53 EVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQ 132
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 181 NLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKE 258
Cdd:cd07871 133 NLLINEKGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKE 211
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
59-300 1.95e-18

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: 85.47  E-value: 1.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFeisdadtKEVFAGKIVP-KSLLLKPHQ-----REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd14146   2 IGVGGFGKVY-------RATWKGQEVAvKAARQDPDEdikatAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLlelhkrRKALT----EPEARYYLR-----------QIVLGCQYLHRNRV---IHRDLKLGNLFLNEDLE----- 189
Cdd:cd14146  75 ARGGTL------NRALAaanaAPGPRRARRipphilvnwavQIARGMLYLHEEAVvpiLHRDLKSSNILLLEKIEhddic 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 190 ---VKIGDFGLATkvEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFE-TSCLKETY-LRIK 264
Cdd:cd14146 149 nktLKITDFGLAR--EWHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRgIDGLAVAYgVAVN 226
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21359873 265 KNEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14146 227 KLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALIL 262
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
101-305 4.72e-18

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: 84.86  E-value: 4.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRrsllELHK-----RRKALTEPEARYYLRQIVLGCQYLHRNRVIHR 175
Cdd:cd07860  49 EISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQ----DLKKfmdasALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 176 DLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKPPFETS 254
Cdd:cd07860 125 DLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGD 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 255 CLKETYLRIKKN----------------EY--SIPK-----------HINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07860 205 SEIDQLFRIFRTlgtpdevvwpgvtsmpDYkpSFPKwarqdfskvvpPLDEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
78-300 5.61e-18

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: 83.47  E-value: 5.61e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  78 VFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLEL--HKRRKALTEPEARY 155
Cdd:cd14060   9 VYRAIWVSQDKEVAVKKLLKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYlnSNESEEMDMDQIMT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 156 YLRQIVLGCQYLHRN---RVIHRDLKLGNLFLNEDLEVKIGDFGlATKVeYDGERKKTLCGTPNYIAPEVLSKKGHSFEV 232
Cdd:cd14060  89 WATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFG-ASRF-HSHTTHMSLVGTFPWMAPEVIQSLPVSETC 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 233 DVWSIGCIMYTLLVGKPPFE-TSCLKETYLRIKKNEY-SIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14060 167 DTYSYGVVLWEMLTREVPFKgLEGLQVAWLVVEKNERpTIPSSCPRSFAELMRRCWEADVKERPSFKQII 236
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
148-307 9.30e-18

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: 83.91  E-value: 9.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 148 LTEPEARYYLRQIVLGCQYLHRN-RVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE----------YDGERKKTLCG-TP 215
Cdd:cd14011 111 LYDVEIKYGLLQISEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFCISSEqatdqfpyfrEYDPNLPPLAQpNL 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFEtscLKETYLRIKKNEYSIPKHINPVAA-------SLIQKMLQ 287
Cdd:cd14011 191 NYLAPEYILSKTCDPASDMFSLGVLIYAIYNkGKPLFD---CVNNLLSYKKNSNQLRQLSLSLLEkvpeelrDHVKTLLN 267
                       170       180
                ....*....|....*....|
gi 21359873 288 TDPTARPTINELLNDEFFTS 307
Cdd:cd14011 268 VTPEVRPDAEQLSKIPFFDD 287
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
101-307 9.96e-18

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: 84.27  E-value: 9.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLG 180
Cdd:cd07872  54 EVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQ 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 181 NLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCL--- 256
Cdd:cd07872 134 NLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVede 213
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 257 ------------KETYLRIKKNE----YSIPKH-----------INPVAASLIQKMLQTDPTARPTINELLNDEFFTS 307
Cdd:cd07872 214 lhlifrllgtptEETWPGISSNDefknYNFPKYkpqplinhaprLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRS 291
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
59-245 1.05e-17

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: 83.91  E-value: 1.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFA---KC-FEISDADTKEVFAGKIVPKSLllKPHQREkMSMEISIHRSLAHQHVVGFHG--FFEDNDFVFVVLEL 132
Cdd:cd14205  12 LGKGNFGsveMCrYDPLQDNTGEVVAVKKLQHST--EEHLRD-FEREIEILKSLQHDNIVKYKGvcYSAGRRNLRLIMEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTl 211
Cdd:cd14205  89 LPYGSLRDyLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKV- 167
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21359873 212 cGTPN-----YIAPEVLSKKGHSFEVDVWSIGCIMYTLL 245
Cdd:cd14205 168 -KEPGespifWYAPESLTESKFSVASDVWSFGVVLYELF 205
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
101-299 1.22e-17

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: 83.11  E-value: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFF-EDNDFVFVVLELCRRRSLLE-LHKRRKALTEPEAR-YYLRQIVLGCQYLHRNRVIHRDL 177
Cdd:cd05082  49 EASVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYMAKGSLVDyLRSRGRSVLGGDCLlKFSLDVCEAMEYLEGNNFVHRDL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 178 KLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTlcgTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPFETSCL 256
Cdd:cd05082 129 AARNVLVSEDNVAKVSDFGLTKEASSTQDTGKL---PVKWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYPRIPL 205
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21359873 257 KETYLRIKKN-EYSIPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05082 206 KDVVPRVEKGyKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQL 249
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
101-306 1.25e-17

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: 83.22  E-value: 1.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKL 179
Cdd:cd05068  53 EAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEyLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAA 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 180 GNLFLNEDLEVKIGDFGLA--TKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCL 256
Cdd:cd05068 133 RNVLVGENNICKVADFGLArvIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTN 212
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 257 KETYLRIKKNeYSIPKHINpVAASLIQKMLQT---DPTARPTINEL---LNDEFFT 306
Cdd:cd05068 213 AEVLQQVERG-YRMPCPPN-CPPQLYDIMLECwkaDPMERPTFETLqwkLEDFFVN 266
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
59-300 2.06e-17

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: 82.34  E-value: 2.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFeisdadtKEVFAGKIVP-KSLLLKPHQ-----REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd14148   2 IGVGGFGKVY-------KGLWRGEEVAvKAARQDPDEdiavtAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHKRRKALTEPEARYYLrQIVLGCQYLHRNR---VIHRDLKLGNLFL-----NEDLE---VKIGDFGLATkv 201
Cdd:cd14148  75 ARGGALNRALAGKKVPPHVLVNWAV-QIARGMNYLHNEAivpIIHRDLKSSNILIlepieNDDLSgktLKITDFGLAR-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 202 EYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETY-LRIKKNEYSIPKHINPVAA 279
Cdd:cd14148 152 EWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYrEIDALAVAYgVAMNKLTLPIPSTCPEPFA 231
                       250       260
                ....*....|....*....|.
gi 21359873 280 SLIQKMLQTDPTARPTINELL 300
Cdd:cd14148 232 RLLEECWDPDPHGRPDFGSIL 252
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
59-315 2.09e-17

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: 83.57  E-value: 2.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06650  13 LGAGNGGVVFKVSHKPSGLVMARKLI--HLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYL-HRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeyDGERKKTLCGTPNY 217
Cdd:cd06650  91 DQVLKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQL--IDSMANSFVGTRSY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARP--T 295
Cdd:cd06650 169 MSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPpmA 248
                       250       260
                ....*....|....*....|
gi 21359873 296 INELLNdefFTSGYIPARLP 315
Cdd:cd06650 249 IFELLD---YIVNEPPPKLP 265
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
59-305 2.70e-17

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: 82.79  E-value: 2.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTK-EVFAGKIVPKSLllKPHQREKMSMEISIHRSLAHQHVVGFHGFFED----NDFVFVVLELC 133
Cdd:cd14030  33 IGRGSFKTVYKGLDTETTvEVAWCELQDRKL--SKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCIVLVTELM 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR--VIHRDLKLGNLFLNEDL-EVKIGDFGLATKVEydGERKKT 210
Cdd:cd14030 111 TSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLKR--ASFAKS 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKKgHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKK--NEYSIPKHINPVAASLIQKMLQ 287
Cdd:cd14030 189 VIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRRVTSgvKPASFDKVAIPEVKEIIEGCIR 267
                       250
                ....*....|....*...
gi 21359873 288 TDPTARPTINELLNDEFF 305
Cdd:cd14030 268 QNKDERYAIKDLLNHAFF 285
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
75-305 4.03e-17

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: 82.10  E-value: 4.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  75 TKEVFAGKIVPksLLLKPHQREKMSMEISIHRSLAHQHVVGFHG-FFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEA 153
Cdd:cd06620  29 TGTIMAKKVIH--IDAKSSVRKQILRELQILHECHSPYIVSFYGaFLNENNNIIICMEYMDCGSLDKILKKKGPFPEEVL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 154 RYYLRQIVLGCQYLHR-NRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydGERKKTLCGTPNYIAPEVLSKKGHSFEV 232
Cdd:cd06620 107 GKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELI--NSIADTFVGTSTYMSPERIQGGKYSVKS 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 233 DVWSIGCIMYTLLVGKPPF-ETSCLKETYL----------RIkKNEYS--IPKHIN--PVAASLIQKMLQTDPTARPTIN 297
Cdd:cd06620 185 DVWSLGLSIIELALGEFPFaGSNDDDDGYNgpmgildllqRI-VNEPPprLPKDRIfpKDLRDFVDRCLLKDPRERPSPQ 263

                ....*...
gi 21359873 298 ELLNDEFF 305
Cdd:cd06620 264 LLLDHDPF 271
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
59-251 4.90e-17

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: 82.15  E-value: 4.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISihRSLAHQHVVGFHGFFEDND--FVFVVLELCRRR 136
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQMREFEVL--KKLNHKNIVKLFAIEEELTtrHKVLVMELCPCG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SL---LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNL--FLNEDLEV--KIGDFGLATKVEyDGERKK 209
Cdd:cd13988  79 SLytvLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNImrVIGEDGQSvyKLTDFGAARELE-DDEQFV 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TLCGTPNYIAPE-----VLSK---KGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd13988 158 SLYGTEEYLHPDmyeraVLRKdhqKKYGATVDLWSIGVTFYHAATGSLPF 207
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
59-307 6.77e-17

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: 81.43  E-value: 6.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06622   9 LGKGNYGSVYKVLHRPTGVTMAMKEI--RLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALT---EPEARYYLRQIVLGCQYL-HRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydGERKKTLCGT 214
Cdd:cd06622  87 DKLYAGGVATEgipEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV--ASLAKTNIGC 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 PNYIAPEVLSKKG------HSFEVDVWSIGCIMYTLLVGKPPFEtsclKETYLRIKKNEYSI--------PKHINPVAAS 280
Cdd:cd06622 165 QSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPYP----PETYANIFAQLSAIvdgdpptlPSGYSDDAQD 240
                       250       260
                ....*....|....*....|....*..
gi 21359873 281 LIQKMLQTDPTARPTINELLNDEFFTS 307
Cdd:cd06622 241 FVAKCLNKIPNRRPTYAQLLEHPWLVK 267
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
59-299 7.73e-17

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: 81.14  E-value: 7.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVfagkIVPKSLLLKPHQREKMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKV----MVMKELIRCDEETQKTFLtEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYD------------- 204
Cdd:cd14222  77 LKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEkkkpppdkpttkk 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 -----GERKK--TLCGTPNYIAPEVLSKKGHSFEVDVWSIGcIMYTLLVGKPPFETSCLKETY---LRIKKN-EYSIPKH 273
Cdd:cd14222 157 rtlrkNDRKKryTVVGNPYWMAPEMLNGKSYDEKVDIFSFG-IVLCEIIGQVYADPDCLPRTLdfgLNVRLFwEKFVPKD 235
                       250       260
                ....*....|....*....|....*.
gi 21359873 274 INPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd14222 236 CPPAFFPLAAICCRLEPDSRPAFSKL 261
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
59-259 8.37e-17

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: 81.01  E-value: 8.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVfagkIVPKSLLLKPHQREKMSM-EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEV----MVMKELIRFDEEAQRNFLkEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE---------- 206
Cdd:cd14154  77 LKDvLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEERLpsgnmspset 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21359873 207 --------RKK--TLCGTPNYIAPEVLSKKGHSFEVDVWSIGcIMYTLLVGKPPFETSCLKET 259
Cdd:cd14154 157 lrhlkspdRKKryTVVGNPYWMAPEMLNGRSYDEKVDIFSFG-IVLCEIIGRVEADPDYLPRT 218
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
59-305 1.09e-16

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: 80.51  E-value: 1.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADT-KEVFAGKIVPKSLllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDN----DFVFVVLELC 133
Cdd:cd14032   9 LGRGSFKTVYKGLDTETwVEVAWCELQDRKL--TKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCakgkRCIVLVTELM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR--VIHRDLKLGNLFLNEDL-EVKIGDFGLATKVEydGERKKT 210
Cdd:cd14032  87 TSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLKR--ASFAKS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEvLSKKGHSFEVDVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIK--KNEYSIPKHINPVAASLIQKMLQ 287
Cdd:cd14032 165 VIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRKVTcgIKPASFEKVTDPEIKEIIGECIC 243
                       250
                ....*....|....*...
gi 21359873 288 TDPTARPTINELLNDEFF 305
Cdd:cd14032 244 KNKEERYEIKDLLSHAFF 261
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
59-304 1.89e-16

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: 79.49  E-value: 1.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLllkphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV-----DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRK-ALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED---LEVKIGDFGLATKV----EYDGERKKT 210
Cdd:cd14156  76 EELLAREElPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTprgREAVVTDFGLAREVgempANDPERKLS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTPNYIAPEVLSKKGHSFEVDVWSIGcIMYTLLVGKPPFETSCLKET------YLRIKKNEYSIPKHINPVAASLIqk 284
Cdd:cd14156 156 LVGSAFWMAPEMLRGEPYDRKVDVFSFG-IVLCEILARIPADPEVLPRTgdfgldVQAFKEMVPGCPEPFLDLAASCC-- 232
                       250       260
                ....*....|....*....|
gi 21359873 285 mlQTDPTARPTINELLnDEF 304
Cdd:cd14156 233 --RMDAFKRPSFAELL-DEL 249
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
58-305 2.60e-16

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: 79.90  E-value: 2.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGF---AKCFeisDADTKEVFAGKIVPKSLllKPHQreKMSMEISIHRSLAH------QHVVGFHGFFEDNDFVFV 128
Cdd:cd14210  20 VLGKGSFgqvVKCL---DHKTGQLVAIKIIRNKK--RFHQ--QALVEVKILKHLNDndpddkHNIVRYKDSFIFRGHLCI 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 129 VLELCRRrSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL--NEDLEVKIGDFGLATkveYD 204
Cdd:cd14210  93 VFELLSI-NLYELLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLkqPSKSSIKVIDFGSSC---FE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTlcgtpnYI------APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF--------------------------- 251
Cdd:cd14210 169 GEKVYT------YIqsrfyrAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFpgeneeeqlacimevlgvppkslidka 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 252 --------------ETSCLKETYLRIK-KNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14210 243 srrkkffdsngkprPTTNSKGKKRRPGsKSLAQVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
101-305 2.92e-16

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: 79.39  E-value: 2.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL--CRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLK 178
Cdd:cd07861  49 EISLLKELQHPNIVCLEDVLMQENRLYLVFEFlsMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLK 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 179 LGNLFLNEDLEVKIGDFGLA----TKVEYDGERKKTLCgtpnYIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPPFE- 252
Cdd:cd07861 129 PQNLLIDNKGVIKLADFGLArafgIPVRVYTHEVVTLW----YRAPEVLlGSPRYSTPVDIWSIGTIFAEMATKKPLFHg 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 253 -------------------------TSC--LKETYLRIKKNEY-SIPKHINPVAASLIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd07861 205 dseidqlfrifrilgtptediwpgvTSLpdYKNTFPKWKKGSLrTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284

                .
gi 21359873 305 F 305
Cdd:cd07861 285 F 285
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
59-304 3.10e-16

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: 79.15  E-value: 3.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPhQREKMSmEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06619   9 LGHGNGGTVYKAYHLLTRRILAVKVIPLDITVEL-QKQIMS-ELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 lELHKRrkaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydGERKKTLCGTPNYI 218
Cdd:cd06619  87 -DVYRK---IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV--NSIAKTYVGTNAYM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 219 APEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPfetsclketYLRIKKNEYS-----------------IPKH-INPVAAS 280
Cdd:cd06619 161 APERISGEQYGIHSDVWSLGISFMELALGRFP---------YPQIQKNQGSlmplqllqcivdedppvLPVGqFSEKFVH 231
                       250       260
                ....*....|....*....|....
gi 21359873 281 LIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd06619 232 FITQCMRKQPKERPAPENLMDHPF 255
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
59-305 3.46e-16

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. 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 serine/threonine residues. The CLK3 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: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 80.05  E-value: 3.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISD-ADTKEVFAGKIVPKSlllkPHQREKMSMEISIHRSLAHQH------VVGFHGFFEDNDFVFVVLE 131
Cdd:cd14214  21 LGEGTFGKVVECLDhARGKSQVALKIIRNV----GKYREAARLEINVLKKIKEKDkenkflCVLMSDWFNFHGHMCIAFE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRrSLLELHKRRKALTEP--EARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNEDLE------------------V 190
Cdd:cd14214  97 LLGK-NTFEFLKENNFQPYPlpHIRHMAYQLCHALKFLHENQLTHTDLKPENiLFVNSEFDtlynesksceeksvkntsI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 191 KIGDFGLATkveYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSI 270
Cdd:cd14214 176 RVADFGSAT---FDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHLVMMEKILGPI 252
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 271 PKHI-------------------------------NPVAA-------------SLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14214 253 PSHMihrtrkqkyfykgslvwdenssdgryvsencKPLMSymlgdslehtqlfDLLRRMLEFDPALRITLKEALLHPFF 331
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
101-299 4.49e-16

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: 78.38  E-value: 4.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDfVFVVLELCRRRSLLE-LHKR-RKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLK 178
Cdd:cd05083  49 ETAVMTKLQHKNLVRLLGVILHNG-LYIVMELMSKGNLVNfLRSRgRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLA 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 179 LGNLFLNEDLEVKIGDFGLAtKVEYDGERKKTLcgTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPFETSCLK 257
Cdd:cd05083 128 ARNILVSEDGVAKISDFGLA-KVGSMGVDNSRL--PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFsYGRAPYPKMSVK 204
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21359873 258 ETYLRIKKN-EYSIPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05083 205 EVKEAVEKGyRMEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKL 247
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
59-301 4.61e-16

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: 78.55  E-value: 4.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFE-ISDADTKEVFAGKIVPKSLLlkPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14145  14 IGIGGFGKVYRaIWIGDEVAVKAARHDPDEDI--SQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALTEPEARYYLrQIVLGCQYLHRNR---VIHRDLKLGNLFL-----NEDLE---VKIGDFGLATkvEYDGE 206
Cdd:cd14145  92 LNRVLSGKRIPPDILVNWAV-QIARGMNYLHCEAivpVIHRDLKSSNILIlekveNGDLSnkiLKITDFGLAR--EWHRT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 207 RKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFE-TSCLKETY-LRIKKNEYSIPKHINPVAASLIQK 284
Cdd:cd14145 169 TKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRgIDGLAVAYgVAMNKLSLPIPSTCPEPFARLMED 248
                       250
                ....*....|....*..
gi 21359873 285 MLQTDPTARPTINELLN 301
Cdd:cd14145 249 CWNPDPHSRPPFTNILD 265
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
59-305 5.09e-16

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: 78.63  E-value: 5.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIV---------PKSLLlkphqrekmsMEISIHRSLAHQHVVGFHGFFEDNDFVFVV 129
Cdd:cd07839   8 IGEGTYGTVFKAKNRETHEIVALKRVrlddddegvPSSAL----------REICLLKELKHKNIVRLYDVLHSDKKLTLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKV-----EYD 204
Cdd:cd07839  78 FEYCDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFgipvrCYS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GErkktlCGTPNYIAPEVL-SKKGHSFEVDVWSIGCIMYTLL-VGKPPFETSCLKETYLRIKK-----NEYSIP------ 271
Cdd:cd07839 158 AE-----VVTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRllgtpTEESWPgvsklp 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 21359873 272 ------------------KHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07839 233 dykpypmypattslvnvvPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPYF 284
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
59-245 5.14e-16

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: 78.82  E-value: 5.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCfEISDADTKEVFAGKIVP-KSLllKPHQREK----MSMEISIHRSLAHQHVVGFHGFFEDN--DFVFVVLE 131
Cdd:cd05079  12 LGEGHFGKV-ELCRYDPEGDNTGEQVAvKSL--KPESGGNhiadLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRRSLLELHKRRKA-LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGER--- 207
Cdd:cd05079  89 FLPSGSLKEYLPRNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYytv 168
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21359873 208 KKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLL 245
Cdd:cd05079 169 KDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELL 206
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
71-238 5.65e-16

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-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: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 78.15  E-value: 5.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  71 SDADTKEVfAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVlELCRRRSLLE-LHKRRKALT 149
Cdd:cd05040  19 PSGKVIQV-AVKCLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLMMVT-ELAPLGSLLDrLRKDQGHFL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 150 EPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGL--ATKVEYD----GERKK---TLCgtpnyiAP 220
Cdd:cd05040  97 ISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLmrALPQNEDhyvmQEHRKvpfAWC------AP 170
                       170
                ....*....|....*...
gi 21359873 221 EVLSKKGHSFEVDVWSIG 238
Cdd:cd05040 171 ESLKTRKFSHASDVWMFG 188
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
159-300 6.65e-16

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: 78.15  E-value: 6.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNR---VIHRDLKLGNLFL-----NEDLE---VKIGDFGLATkvEYDGERKKTLCGTPNYIAPEVLSKKG 227
Cdd:cd14147 109 QIARGMHYLHCEAlvpVIHRDLKSNNILLlqpieNDDMEhktLKITDFGLAR--EWHKTTQMSAAGTYAWMAPEVIKAST 186
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 228 HSFEVDVWSIGCIMYTLLVGKPPFE-TSCLKETY-LRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14147 187 FSKGSDVWSFGVLLWELLTGEVPYRgIDCLAVAYgVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASIL 261
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
101-302 7.37e-16

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: 77.57  E-value: 7.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVF-VVLELCRRRSLLELHKRRKALTEPEARYYLR-QIVLGCQYLHR--NRVIHRD 176
Cdd:cd14064  41 EVSILCRLNHPCVIQFVGACLDDPSQFaIVTQYVSGGSLFSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHNltQPIIHRD 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 177 LKLGNLFLNEDLEVKIGDFG---LATKVEYDGERKKTlcGTPNYIAPEVLSKKG-HSFEVDVWSIGCIMYTLLVGKPPFe 252
Cdd:cd14064 121 LNSHNILLYEDGHAVVADFGesrFLQSLDEDNMTKQP--GNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF- 197
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 253 tSCLKE-------TYLRIKKN-EYSIPKHInpvaASLIQKMLQTDPTARPTINELLND 302
Cdd:cd14064 198 -AHLKPaaaaadmAYHHIRPPiGYSIPKPI----SSLLMRGWNAEPESRPSFVEIVAL 250
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
101-305 9.15e-16

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: 78.19  E-value: 9.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR--RSLLELHKRrkALTEPEARYYLRQIVLGCQYLHRNRVIHRDLK 178
Cdd:cd07844  48 EASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLDTdlKQYMDDCGG--GLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLK 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 179 LGNLFLNEDLEVKIGDFGLA------TKVeYDGErkktlCGTPNYIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd07844 126 PQNLLISERGELKLADFGLAraksvpSKT-YSNE-----VVTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLF 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 252 ETSCL----------------KETYLRIKKNE----YSIPKHIN-------------PVAASLIQKMLQTDPTARPTINE 298
Cdd:cd07844 200 PGSTDvedqlhkifrvlgtptEETWPGVSSNPefkpYSFPFYPPrplinhaprldriPHGEELALKFLQYEPKKRISAAE 279

                ....*..
gi 21359873 299 LLNDEFF 305
Cdd:cd07844 280 AMKHPYF 286
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
157-305 1.37e-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: 1.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 157 LRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCgTPNYIAPEVLSKKGHSFEVDVWS 236
Cdd:cd07863 114 MRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSCQMALTPVVV-TLWYRAPEVLLQSTYATPVDMWS 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 237 IGCIMYTLLVGKPPF----ETSCLKETYLRI---KKNEY----SIPKH----------------INPVAASLIQKMLQTD 289
Cdd:cd07863 193 VGCIFAEMFRRKPLFcgnsEADQLGKIFDLIglpPEDDWprdvTLPRGafsprgprpvqsvvpeIEESGAQLLLEMLTFN 272
                       170
                ....*....|....*.
gi 21359873 290 PTARPTINELLNDEFF 305
Cdd:cd07863 273 PHKRISAFRALQHPFF 288
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
120-312 1.54e-15

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: 78.22  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 120 FEDNDFVFVVLE-----LCRRRSLLELHKRrkaltepeARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGD 194
Cdd:cd07850  74 LEEFQDVYLVMElmdanLCQVIQMDLDHER--------MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILD 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 195 FGLATKVEyDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTL---------------------LVGKPPFE- 252
Cdd:cd07850 146 FGLARTAG-TSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMirgtvlfpgtdhidqwnkiieQLGTPSDEf 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 253 TSCLKET---YL--RIKKNEYSIPK---------------HINP-VAASLIQKMLQTDPTARPTINELLNDEFFTSGYIP 311
Cdd:cd07850 225 MSRLQPTvrnYVenRPKYAGYSFEElfpdvlfppdseehnKLKAsQARDLLSKMLVIDPEKRISVDDALQHPYINVWYDP 304

                .
gi 21359873 312 A 312
Cdd:cd07850 305 S 305
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
59-251 1.67e-15

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: 77.34  E-value: 1.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd07848   9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEE-NEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNML 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKT-LCGTPNY 217
Cdd:cd07848  88 ELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTeYVATRWY 167
                       170       180       190
                ....*....|....*....|....*....|....
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd07848 168 RSPELLLGAPYGKAVDMWSVGCILGELSDGQPLF 201
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
85-306 1.76e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 78.38  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   85 PKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGC 164
Cdd:PHA03209  91 PDPVVLKIGQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  165 QYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGlATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTL 244
Cdd:PHA03209 171 RYLHAQRIIHRDVKTENIFINDVDQVCIGDLG-AAQFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEM 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  245 L-------------------------------VGKPPFETSCLKETYLRIKKNEYS---------------IPKHINpvA 278
Cdd:PHA03209 250 LaypstifedppstpeeyvkschshllkiistLKVHPEEFPRDPGSRLVRGFIEYAslerqpytrypcfqrVNLPID--G 327
                        250       260
                 ....*....|....*....|....*...
gi 21359873  279 ASLIQKMLQTDPTARPTINELLNDEFFT 306
Cdd:PHA03209 328 EFLVHKMLTFDAAMRPSAEEILNYPMFA 355
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
59-326 1.79e-15

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 78.92  E-value: 1.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   59 LGKGGFAKCFEISDADTKEvfagKIVPKSLLLKPHQREKmsmEISIHRSLAHQHVVGFHGFF--------EDNDFVFVVL 130
Cdd:PTZ00036  74 IGNGSFGVVYEAICIDTSE----KVAIKKVLQDPQYKNR---ELLIMKNLNHINIIFLKDYYytecfkknEKNIFLNVVM 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  131 ELCRRrsllELHKRRK-------ALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE-VKIGDFGLATKVe 202
Cdd:PTZ00036 147 EFIPQ----TVHKYMKhyarnnhALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNL- 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  203 YDGERKKTLCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRI------------------ 263
Cdd:PTZ00036 222 LAGQRSVSYICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIiqvlgtptedqlkemnpn 301
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873  264 -----------KKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPA-RLPITCLTIPPRFS 326
Cdd:PTZ00036 302 yadikfpdvkpKDLKKVFPKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRDPCiKLPKYIDKLPDLFN 376
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
59-301 1.84e-15

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: 77.00  E-value: 1.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFE-----ISDADTKEVFAGKIVPKSLLLkpHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05032  14 LGQGSFGMVYEglakgVVKGEPETRVAIKTVNENASM--RERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMELM 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLE-LHKRRkaltePEARY--------------YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA 198
Cdd:cd05032  92 AKGDLKSyLRSRR-----PEAENnpglgpptlqkfiqMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 199 TKV-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPFETSCLKETYLRIKKNEYsIPKHIN 275
Cdd:cd05032 167 RDIyETDYYRKGGKGLLPvRWMAPESLKDGVFTTKSDVWSFGVVLWEMAtLAEQPYQGLSNEEVLKFVIDGGH-LDLPEN 245
                       250       260
                ....*....|....*....|....*...
gi 21359873 276 P--VAASLIQKMLQTDPTARPTINELLN 301
Cdd:cd05032 246 CpdKLLELMRMCWQYNPKMRPTFLEIVS 273
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
101-263 2.47e-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: 76.92  E-value: 2.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLG 180
Cdd:cd07870  48 EASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQ 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 181 NLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPPFE-TSCLKE 258
Cdd:cd07870 128 NLLISYLGELKLADFGLARAKSIPSQTYSSEVVTLWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAFPgVSDVFE 207

                ....*
gi 21359873 259 TYLRI 263
Cdd:cd07870 208 QLEKI 212
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
71-304 2.87e-15

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: 76.03  E-value: 2.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  71 SDADTKEVFAGKIVPKSlllkpHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRrSLLELHKRRKALTE 150
Cdd:cd14112  25 STTETDAHCAVKIFEVS-----DEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQE-DVFTRFSSNDYYSE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 151 PEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN--EDLEVKIGDFGLATKVeyDGERKKTLCGTPNYIAPEVLSKKGH 228
Cdd:cd14112  99 EQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQKV--SKLGKVPVDGDTDWASPEFHNPETP 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 229 SF-EVDVWSIGCIMYTLLVGKPPFETSC-----LKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd14112 177 ITvQSDIWGLGVLTFCLLSGFHPFTSEYddeeeTKENVIFVKCRPNLIFVEATQEALRFATWALKKSPTRRMRTDEALEH 256

                ..
gi 21359873 303 EF 304
Cdd:cd14112 257 RW 258
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
59-302 3.01e-15

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: 76.69  E-value: 3.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREK--------MSMEISIHRslaHQHVVGFHGFFEDNDFVFVVL 130
Cdd:cd05053  20 LGEGAFGQVVKAEAVGLDNKPNEVVTVAVKMLKDDATEKdlsdlvseMEMMKMIGK---HKNIINLLGACTQDGPLYVVV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 131 ELCRRRSLLE-LHKRR---------------KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGD 194
Cdd:cd05053  97 EYASKGNLREfLRARRppgeeaspddprvpeEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIAD 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 195 FGLATKVEY-DGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPFETSCLKETYLRIKKNeYSIP 271
Cdd:cd05053 177 FGLARDIHHiDYYRKTTNGRLPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELFKLLKEG-HRME 255
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21359873 272 KhinPVAASLIQKML-----QTDPTARPTINELLND 302
Cdd:cd05053 256 K---PQNCTQELYMLmrdcwHEVPSQRPTFKQLVED 288
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
101-300 3.04e-15

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: 75.95  E-value: 3.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYL-RQIVLGCQYLHRNRVIHRDLKL 179
Cdd:cd05059  49 EAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLLNYLRERRGKFQTEQLLEMcKDVCEAMEYLESNGFIHRDLAA 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 180 GNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLK 257
Cdd:cd05059 129 RNCLVGEQNVVKVSDFGLARYVLDDEYTSSVGTKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNS 208
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21359873 258 ETYLRIKKNeYSIPKhinPVAAS-----LIQKMLQTDPTARPTINELL 300
Cdd:cd05059 209 EVVEHISQG-YRLYR---PHLAPtevytIMYSCWHEKPEERPTFKILL 252
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
145-300 3.27e-15

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: 77.33  E-value: 3.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 145 RKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE--RKKTLCGTPNYIAPEV 222
Cdd:cd05103 173 KDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDyvRKGDARLPLKWMAPET 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 223 LSKKGHSFEVDVWSIGCIMYTLL-VGKPPF------ETSC--LKETyLRIKKNEYSIPKhinpvaasLIQKML---QTDP 290
Cdd:cd05103 253 IFDRVYTIQSDVWSFGVLLWEIFsLGASPYpgvkidEEFCrrLKEG-TRMRAPDYTTPE--------MYQTMLdcwHGEP 323
                       170
                ....*....|
gi 21359873 291 TARPTINELL 300
Cdd:cd05103 324 SQRPTFSELV 333
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
59-299 3.39e-15

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: 76.76  E-value: 3.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDAD-TKEVFAGKIVPKSLLLKPHQREK---MSmEISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05055  43 LGAGAFGKVVEATAYGlSKSDAVMKVAVKMLKPTAHSSERealMS-ELKIMSHLGnHENIVNLLGACTIGGPILVITEYC 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLE-LH-KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGerkktl 211
Cdd:cd05055 122 CYGDLLNfLRrKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDS------ 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 cgtpNYI------------APEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPFETSCLKETYLRIKKNEYSI--PKHINP 276
Cdd:cd05055 196 ----NYVvkgnarlpvkwmAPESIFNCVYTFESDVWSYGILLWEIFsLGSNPYPGMPVDSKFYKLIKEGYRMaqPEHAPA 271
                       250       260
                ....*....|....*....|...
gi 21359873 277 VAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05055 272 EIYDIMKTCWDADPLKRPTFKQI 294
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
58-302 5.09e-15

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: 75.04  E-value: 5.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVfAGKIVPKSLllkPHQ-REKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRR 136
Cdd:cd05085   3 LLGKGNFGEVYKGTLKDKTPV-AVKTCKEDL---PQElKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLaTKVEYDGERKKT-LCGT 214
Cdd:cd05085  79 DFLSfLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGM-SRQEDDGVYSSSgLKQI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 215 P-NYIAPEVLSKKGHSFEVDVWSIGCIMY-TLLVGKPPFETSCLKETYLRIKKN-EYSIPKHINPVAASLIQKMLQTDPT 291
Cdd:cd05085 158 PiKWTAPEALNYGRYSSESDVWSFGILLWeTFSLGVCPYPGMTNQQAREQVEKGyRMSAPQRCPEDIYKIMQRCWDYNPE 237
                       250
                ....*....|.
gi 21359873 292 ARPTINELLND 302
Cdd:cd05085 238 NRPKFSELQKE 248
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
110-299 5.51e-15

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 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 FGFR4 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: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 76.16  E-value: 5.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 110 HQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTE---------PEARYYLR-------QIVLGCQYLHRNRVI 173
Cdd:cd05099  77 HKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPdytfditkvPEEQLSFKdlvscayQVARGMEYLESRRCI 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG-TP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTL--LVGKP 249
Cdd:cd05099 157 HRDLAARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGrLPvKWMAPEALFDRVYTHQSDVWSFGILMWEIftLGGSP 236
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 250 ----PFET--SCLKETYlRIKKneysiPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05099 237 ypgiPVEElfKLLREGH-RMDK-----PSNCTHELYMLMRECWHAVPTQRPTFKQL 286
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
58-295 7.30e-15

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: 75.34  E-value: 7.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRS 137
Cdd:cd14026   4 YLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKALtePEARYYLR-----QIVLGCQYLHRNR--VIHRDLKLGNLFLNEDLEVKIGDFGLA-----TKVEYDG 205
Cdd:cd14026  84 LNELLHEKDIY--PDVAWPLRlrilyEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSkwrqlSISQSRS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 ERKKTLCGTPNYIAPEVLS---KKGHSFEVDVWSIGCIMYTLLVGKPPFE--TSCLKETY-----LRIKKNEYSIPKHIn 275
Cdd:cd14026 162 SKSAPEGGTIIYMPPEEYEpsqKRRASVKHDIYSYAIIMWEVLSRKIPFEevTNPLQIMYsvsqgHRPDTGEDSLPVDI- 240
                       250       260
                ....*....|....*....|...
gi 21359873 276 PVAASLIQKMLQ---TDPTARPT 295
Cdd:cd14026 241 PHRATLINLIESgwaQNPDERPS 263
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
59-301 7.71e-15

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: 74.61  E-value: 7.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLK--PHQREKMSMEISIHRSL--AHQHVVGFHGFFEDNDFVFVVLELCR 134
Cdd:cd14102   8 LGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEwgTLNGVMVPLEIVLLKKVgsGFRGVIKLLDWYERPDGFLIVMERPE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 135 R-RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN-EDLEVKIGDFG----LATKVEYDGErk 208
Cdd:cd14102  88 PvKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGsgalLKDTVYTDFD-- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 ktlcGTPNYIAPE-VLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSclkETYLRIKkneYSIPKHINPVAASLIQKMLQ 287
Cdd:cd14102 166 ----GTRVYSPPEwIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQD---EEILRGR---LYFRRRVSPECQQLIKWCLS 235
                       250
                ....*....|....
gi 21359873 288 TDPTARPTINELLN 301
Cdd:cd14102 236 LRPSDRPTLEQIFD 249
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
110-302 7.99e-15

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: 75.43  E-value: 7.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 110 HQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKRRKALTE--------PEARYYLR-------QIVLGCQYLHRNRVI 173
Cdd:cd05098  78 HKNIINLLGACTQDGPLYVIVEYASKGNLREyLQARRPPGMEycynpshnPEEQLSSKdlvscayQVARGMEYLASKKCI 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG--TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPP 250
Cdd:cd05098 158 HRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGrlPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFtLGGSP 237
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 21359873 251 FETSCLKETYLRIKK-NEYSIPKHINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd05098 238 YPGVPVEELFKLLKEgHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVED 290
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
89-312 9.24e-15

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: 76.22  E-value: 9.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  89 LLKPHQRE----KMSMEISIHRSLAHQHVVGFHGFF------EDNDFVFVVLELCRRRSLLELHKRrkaLTEPEARYYLR 158
Cdd:cd07876  54 LSRPFQNQthakRAYRELVLLKCVNHKNIISLLNVFtpqkslEEFQDVYLVMELMDANLCQVIHME---LDHERMSYLLY 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCgTPNYIAPEVLSKKGHSFEVDVWSIG 238
Cdd:cd07876 131 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVV-TRYYRAPEVILGMGYKENVDIWSVG 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 239 CIMYTLL---------------------VGKPPFE-TSCLKETYLRIKKN---------EYSIPKHINPV---------- 277
Cdd:cd07876 210 CIMGELVkgsvifqgtdhidqwnkvieqLGTPSAEfMNRLQPTVRNYVENrpqypgisfEELFPDWIFPSeserdklkts 289
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21359873 278 -AASLIQKMLQTDPTARPTINELLNDEFFTSGYIPA 312
Cdd:cd07876 290 qARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPA 325
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
58-251 1.08e-14

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: 74.38  E-value: 1.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAG--KIVPKSLLLKPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05044   2 FLGSGAFGEVFEGTAKDILGDGSGetKVAVKTLRKGATDQEKAEFlkEAHLMSNFKHPNILKLLGVCLDNDPQYIILELM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLE-LHKRRKALTEPEARYYLRQIVL------GCQYLHRNRVIHRDLKLGNLFLNE----DLEVKIGDFGLAT--- 199
Cdd:cd05044  82 EGGDLLSyLRAARPTAFTPPLLTLKDLLSIcvdvakGCVYLEDMHFVHRDLAARNCLVSSkdyrERVVKIGDFGLARdiy 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 200 KVEY---DGERKKTLcgtpNYIAPEVLSKKGHSFEVDVWSIGCIMY-TLLVGKPPF 251
Cdd:cd05044 162 KNDYyrkEGEGLLPV----RWMAPESLVDGVFTTQSDVWAFGVLMWeILTLGQQPY 213
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
59-301 1.10e-14

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: 74.02  E-value: 1.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAkcfeisdadtkEVFAGKIVPKSLL---------LKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVV 129
Cdd:cd05041   3 IGRGNFG-----------DVYRGVLKPDNTEvavktcretLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLaTKVEYDGERK 208
Cdd:cd05041  72 MELVPGGSLLTfLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGM-SREEEDGEYT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KT--LCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMY-TLLVGKPPFETSCLKETYLRIKKNeYSIPK-HINPVAAS-LI 282
Cdd:cd05041 151 VSdgLKQIPiKWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYPGMSNQQTREQIESG-YRMPApELCPEAVYrLM 229
                       250
                ....*....|....*....
gi 21359873 283 QKMLQTDPTARPTINELLN 301
Cdd:cd05041 230 LQCWAYDPENRPSFSEIYN 248
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
91-300 1.16e-14

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: 75.42  E-value: 1.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  91 KPHQREKMSME-ISIHRSLAHQhvvgfhGFFEDNDFVFVVLElcrRRSLLELHKRrkALTEPEARYYLRQIVLGCQYLHR 169
Cdd:cd14207 130 EPTGGKKKRLEsVTSSESFASS------GFQEDKSLSDVEEE---EEDSGDFYKR--PLTMEDLISYSFQVARGMEFLSS 198
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 170 NRVIHRDLKLGNLFLNEDLEVKIGDFGLATKV--EYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-V 246
Cdd:cd14207 199 RKCIHRDLAARNILLSENNVVKICDFGLARDIykNPDYVRKGDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFsL 278
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 247 GKPPF------ETSC--LKETyLRIKKNEYSIPKhinpvaasLIQKML---QTDPTARPTINELL 300
Cdd:cd14207 279 GASPYpgvqidEDFCskLKEG-IRMRAPEFATSE--------IYQIMLdcwQGDPNERPRFSELV 334
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
59-299 1.33e-14

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: 74.22  E-value: 1.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVfagkIVPKSLLLKPHQREKMSM-EISIHRSLAHQHVVGFHG-FFEDNDFVFVVlELCRRR 136
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEV----MVMKELIRFDEETQRTFLkEVKVMRCLEHPNVLKFIGvLYKDKRLNFIT-EYIKGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 137 SLLELHKRRKALTEPEARY-YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA-------TKVEYDGERK 208
Cdd:cd14221  76 TLRGIIKSMDSHYPWSQRVsFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdekTQPEGLRSLK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 K-------TLCGTPNYIAPEVLSKKGHSFEVDVWSIGcIMYTLLVGKPPFETSCLKETY-----LRIKKNEY---SIPKH 273
Cdd:cd14221 156 KpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFG-IVLCEIIGRVNADPDYLPRTMdfglnVRGFLDRYcppNCPPS 234
                       250       260
                ....*....|....*....|....*.
gi 21359873 274 INPVAAsliqKMLQTDPTARPTINEL 299
Cdd:cd14221 235 FFPIAV----LCCDLDPEKRPSFSKL 256
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
59-301 1.62e-14

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) 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 of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 74.31  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAK-----CFEISDADTKEVFAGKIVPKSlllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05093  13 LGEGAFGKvflaeCYNLCPEQDKILVAVKTLKDA---SDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSL---LELH----------KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATK 200
Cdd:cd05093  90 KHGDLnkfLRAHgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 201 V-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLKE-----TYLRIKKNEYSIPK 272
Cdd:cd05093 170 VySTDYYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEvieciTQGRVLQRPRTCPK 249
                       250       260
                ....*....|....*....|....*....
gi 21359873 273 HInpvaASLIQKMLQTDPTARPTINELLN 301
Cdd:cd05093 250 EV----YDLMLGCWQREPHMRLNIKEIHS 274
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
101-299 1.65e-14

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: 74.19  E-value: 1.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQ-HVVGFHGFFEDNDFVFVVLELCRRRSL----LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHR 175
Cdd:cd14139  49 EVYAHAVLGHHpHVVRYYSAWAEDDHMIIQNEYCNGGSLqdaiSENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 176 DLKLGNLFLNEDLEV----------------------KIGDFGLATKVeydgERKKTLCGTPNYIAPEVLSKK-GHSFEV 232
Cdd:cd14139 129 DIKPSNIFICHKMQSssgvgeevsneedeflsanvvyKIGDLGHVTSI----NKPQVEEGDSRFLANEILQEDyRHLPKA 204
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 233 DVWSIGcIMYTLLVGKPPFETSclKETYLRIKKNEY-SIPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd14139 205 DIFALG-LTVALAAGAEPLPTN--GAAWHHIRKGNFpDVPQELPESFSSLLKNMIQPDPEQRPSATAL 269
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
101-300 1.67e-14

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: 73.74  E-value: 1.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVL-GCQYLHRNRVIHRDLKL 179
Cdd:cd05114  49 EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNYLRQRRGKLSRDMLLSMCQDVCeGMEYLERNNFIHRDLAA 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 180 GNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLK 257
Cdd:cd05114 129 RNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGAKFPvKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNY 208
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21359873 258 ETYLRIKK-NEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd05114 209 EVVEMVSRgHRLYRPKLASKSVYEVMYSCWHEKPEGRPTFADLL 252
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
96-302 1.96e-14

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: 73.98  E-value: 1.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  96 EKMSM-EISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELCRRRSLLEL----HKRRKALTEPEARYYLRQIVLGCQYLHR 169
Cdd:cd14051  43 EQNALnEVYAHAVLGkHPHVVRYYSAWAEDDHMIIQNEYCNGGSLADAisenEKAGERFSEAELKDLLLQVAQGLKYIHS 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 170 NRVIHRDLKLGNLF------------------------LNEDLEVKIGDFGLATKVeydgERKKTLCGTPNYIAPEVLSK 225
Cdd:cd14051 123 QNLVHMDIKPGNIFisrtpnpvsseeeeedfegeednpESNEVTYKIGDLGHVTSI----SNPQVEEGDCRFLANEILQE 198
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 226 K-GHSFEVDVWSIGCIMYtLLVGKPPFETSclKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd14051 199 NySHLPKADIFALALTVY-EAAGGGPLPKN--GDEWHEIRQGNLPPLPQCSPEFNELLRSMIHPDPEKRPSAAALLQH 273
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
59-304 2.02e-14

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: 73.95  E-value: 2.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLlkphqREKMSMEISIHRSLAHQHVVGFHGFFEDNDfVFVVLELCRRRSL 138
Cdd:cd05069  20 LGQGCFGEVWMGTWNGTTKVAIKTLKPGTMM-----PEAFLQEAQIMKKLRHDKLVPLYAVVSEEP-IYIVTEFMGKGSL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP- 215
Cdd:cd05069  94 LDFLKEGdgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPi 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKN-EYSIPKHINPVAASLIQKMLQTDPTAR 293
Cdd:cd05069 174 KWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGyRMPCPQGCPESLHELMKLCWKKDPDER 253
                       250
                ....*....|....
gi 21359873 294 PT---INELLNDEF 304
Cdd:cd05069 254 PTfeyIQSFLEDYF 267
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
59-301 2.63e-14

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand 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 signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR 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: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 73.85  E-value: 2.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFE-----ISDADTKEVFAGKIVPKSLLLKphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05061  14 LGQGSFGMVYEgnardIIKGEAETRVAVKTVNESASLR--ERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELM 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RR-------RSL---LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKV-E 202
Cdd:cd05061  92 AHgdlksylRSLrpeAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIyE 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 203 YDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYtllvgkppfETSCLKETYLRIKKNEYSI----------- 270
Cdd:cd05061 172 TDYYRKGGKGLLPvRWMAPESLKDGVFTTSSDMWSFGVVLW---------EITSLAEQPYQGLSNEQVLkfvmdggyldq 242
                       250       260       270
                ....*....|....*....|....*....|.
gi 21359873 271 PKHINPVAASLIQKMLQTDPTARPTINELLN 301
Cdd:cd05061 243 PDNCPERVTDLMRMCWQFNPKMRPTFLEIVN 273
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
129-302 2.86e-14

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: 73.42  E-value: 2.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 129 VLELCRRRSLLELHKRRKALTEPEARYYLRQIVL----GCQYLHRNRVIHRDLKLGN-----LFLNEDLEVKIGDFGLAT 199
Cdd:cd14000  86 VLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALqvadGLRYLHSAMIIYRDLKSHNvlvwtLYPNSAIIIKIADYGISR 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 200 KVEYDGerKKTLCGTPNYIAPEVLSKK-GHSFEVDVWSIGCIMYTLLVGKPPFetsclkETYLRIkKNEYSIPKHINPVA 278
Cdd:cd14000 166 QCCRMG--AKGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPM------VGHLKF-PNEFDIHGGLRPPL 236
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21359873 279 A-----------SLIQKMLQTDPTARPT---INELLND 302
Cdd:cd14000 237 KqyecapwpeveVLMKKCWKENPQQRPTavtVVSILNS 274
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
59-299 3.47e-14

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) 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 of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA 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: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 73.08  E-value: 3.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAK-----CFEISDADTKEVFAGKIVPKSlllKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05092  13 LGEGAFGKvflaeCHNLLPEQDKMLVAVKALKEA---TESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSL---LELH------------KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA 198
Cdd:cd05092  90 RHGDLnrfLRSHgpdakildggegQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 199 TKV-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPP-FETSCLKETYLRIKKNEYSIPKHI 274
Cdd:cd05092 170 RDIySTDYYRVGGRTMLPiRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPwYQLSNTEAIECITQGRELERPRTC 249
                       250       260
                ....*....|....*....|....*
gi 21359873 275 NPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05092 250 PPEVYAIMQGCWQREPQQRHSIKDI 274
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
59-302 3.84e-14

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: 72.66  E-value: 3.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAkcfeisdadtkEVFAGKIVPKSLL---------LKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVV 129
Cdd:cd05084   4 IGRGNFG-----------EVFSGRLRADNTPvavkscretLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLaTKVEYDGERK 208
Cdd:cd05084  73 MELVQGGDFLTfLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGM-SREEEDGVYA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 209 KT--LCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMY-TLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAA-SLIQ 283
Cdd:cd05084 152 ATggMKQIPvKWTAPEALNYGRYSSESDVWSFGILLWeTFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVyRLME 231
                       250
                ....*....|....*....
gi 21359873 284 KMLQTDPTARPTINELLND 302
Cdd:cd05084 232 QCWEYDPRKRPSFSTVHQD 250
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
59-258 4.23e-14

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: 73.93  E-value: 4.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06649  13 LGAGNGGVVTKVQHKPSGLIMARKLI--HLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYL-HRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeyDGERKKTLCGTPNY 217
Cdd:cd06649  91 DQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQL--IDSMANSFVGTRSY 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21359873 218 IAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKE 258
Cdd:cd06649 169 MSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKE 209
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
59-301 5.01e-14

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: 72.31  E-value: 5.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFE-ISDADTKEVfAGKIVPKSLLLK----PHQrEKMSMEISIHRSLAhqhvVGFHG------FFEDNDFVF 127
Cdd:cd14100   8 LGSGGFGSVYSgIRVADGAPV-AIKHVEKDRVSEwgelPNG-TRVPMEIVLLKKVG----SGFRGvirlldWFERPDSFV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 128 VVLELCRR-RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLneDL---EVKIGDFG----LAT 199
Cdd:cd14100  82 LVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI--DLntgELKLIDFGsgalLKD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 200 KVEYDGErkktlcGTPNYIAPE-VLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSclketyLRIKKNEYSIPKHINPVA 278
Cdd:cd14100 160 TVYTDFD------GTRVYSPPEwIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHD------EEIIRGQVFFRQRVSSEC 227
                       250       260
                ....*....|....*....|...
gi 21359873 279 ASLIQKMLQTDPTARPTINELLN 301
Cdd:cd14100 228 QHLIKWCLALRPSDRPSFEDIQN 250
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
59-307 6.06e-14

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: 72.41  E-value: 6.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLllkphQREKMSMEISIHRSLAHQHVVGFHGFFEDNDfVFVVLELCRRRSL 138
Cdd:cd05071  17 LGQGCFGEVWMGTWNGTTRVAIKTLKPGTM-----SPEAFLQEAQVMKKLRHEKLVQLYAVVSEEP-IYIVTEYMSKGSL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP- 215
Cdd:cd05071  91 LDFLKGEmgKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPi 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKNeYSIPKHiNPVAASLIQKMLQ---TDPT 291
Cdd:cd05071 171 KWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERG-YRMPCP-PECPESLHDLMCQcwrKEPE 248
                       250
                ....*....|....*...
gi 21359873 292 ARPTINEL--LNDEFFTS 307
Cdd:cd05071 249 ERPTFEYLqaFLEDYFTS 266
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
101-299 6.91e-14

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: 71.87  E-value: 6.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDfVFVVLELCRRRSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLK 178
Cdd:cd14203  40 EAQIMKKLRHDKLVQLYAVVSEEP-IYIVTEFMSKGSLLDFLKDGegKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLR 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 179 LGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGcIMYTLLV--GKPPFETSC 255
Cdd:cd14203 119 AANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPiKWTAPEAALYGRFTIKSDVWSFG-ILLTELVtkGRVPYPGMN 197
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21359873 256 LKETYLRIKKNeYSIPKHiNPVAASLIQKMLQT---DPTARPTINEL 299
Cdd:cd14203 198 NREVLEQVERG-YRMPCP-PGCPESLHELMCQCwrkDPEERPTFEYL 242
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
101-305 7.09e-14

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 72.54  E-value: 7.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELcrrrslLELHKRRKALTEPE-------ARYYLRQIVLGCQYLHRNRVI 173
Cdd:PLN00009  51 EISLLKEMQHGNIVRLQDVVHSEKRLYLVFEY------LDLDLKKHMDSSPDfaknprlIKTYLYQILRGIAYCHSHRVL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  174 HRDLKLGNLFLNEDLE-VKIGDFGLATKVEYDGERKKTLCGTPNYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKP-- 249
Cdd:PLN00009 125 HRDLKPQNLLIDRRTNaLKLADFGLARAFGIPVRTFTHEVVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPlf 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  250 ------------------PFETSC--------LKETYLRIK-KNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:PLN00009 205 pgdseidelfkifrilgtPNEETWpgvtslpdYKSAFPKWPpKDLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEH 284

                 ...
gi 21359873  303 EFF 305
Cdd:PLN00009 285 EYF 287
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
156-302 7.56e-14

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl 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 its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 72.35  E-value: 7.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 156 YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeYDGE--RKKTLCGTP-NYIAPEVLSKKGHSFEV 232
Cdd:cd05075 118 FMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKI-YNGDyyRQGRISKMPvKWIAIESLADRVYTTKS 196
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21359873 233 DVWSIGCIMYTLLV-GKPPF---ETSCLKEtYLRiKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd05075 197 DVWSFGVTMWEIATrGQTPYpgvENSEIYD-YLR-QGNRLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCE 268
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
59-301 8.86e-14

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (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, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R 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: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 71.99  E-value: 8.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFE-ISDADTKEVFAGKIVPKSLLLKPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd05062  14 LGQGSFGMVYEgIAKGVVKDEPETRVAIKTVNEAASMRERIEFlnEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 -------RSLLELHKRRKALTEPEARYYLR---QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKV-EYD 204
Cdd:cd05062  94 gdlksylRSLRPEMENNPVQAPPSLKKMIQmagEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIyETD 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTL-LVGKPPFEtSCLKETYLR--IKKNEYSIPKHINPVAAS 280
Cdd:cd05062 174 YYRKGGKGLLPvRWMSPESLKDGVFTTYSDVWSFGVVLWEIaTLAEQPYQ-GMSNEQVLRfvMEGGLLDKPDNCPDMLFE 252
                       250       260
                ....*....|....*....|.
gi 21359873 281 LIQKMLQTDPTARPTINELLN 301
Cdd:cd05062 253 LMRMCWQYNPKMRPSFLEIIS 273
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
59-306 9.58e-14

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: 72.19  E-value: 9.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEvfagKIVPKslLLKPHQREKMSMEISIHRSLA-HQHVVGFHGFFEDND-----FVFVVLEL 132
Cdd:cd14132  26 IGRGKYSEVFEGINIGNNE----KVVIK--VLKPVKKKKIKREIKILQNLRgGPNIVKLLDVVKDPQsktpsLIFEYVNN 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLElhkrrkALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL-EVKIGDFGLAtkvEY--DGERKK 209
Cdd:cd14132 100 TDFKTLYP------TLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKrKLRLIDWGLA---EFyhPGQEYN 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 210 TLCGTPNYIAPEVL-SKKGHSFEVDVWSIGCIMYTLLVGKPP-FETSCLKETYLRIKK-----------NEYSIP----- 271
Cdd:cd14132 171 VRVASRYYKGPELLvDYQYYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVKIAKvlgtddlyaylDKYGIElpprl 250
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 272 -------------KHIN--------PVAASLIQKMLQTDPTARPTINELLNDEFFT 306
Cdd:cd14132 251 ndilgrhskkpweRFVNsenqhlvtPEALDLLDKLLRYDHQERITAKEAMQHPYFD 306
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
90-301 9.76e-14

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: 71.54  E-value: 9.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  90 LKP----HQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGC 164
Cdd:cd05063  41 LKPgyteKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGALDKyLRDHDGEFSSYQLVGMLRGIAAGM 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 165 QYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP---NYIAPEVLSKKGHSFEVDVWSIGCIM 241
Cdd:cd05063 121 KYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDPEGTYTTSGGKipiRWTAPEAIAYRKFTSASDVWSFGIVM 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21359873 242 YTLLV-GKPPFETSCLKETYLRIKKNeYSIPKHINpVAASLIQKMLQT---DPTARPTINELLN 301
Cdd:cd05063 201 WEVMSfGERPYWDMSNHEVMKAINDG-FRLPAPMD-CPSAVYQLMLQCwqqDRARRPRFVDIVN 262
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
159-305 9.89e-14

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. 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 serine/threonine residues. The CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 72.58  E-value: 9.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNRVIHRDLKLGN-LFLNEDL------------------EVKIGDFGLATkveYDGERKKTLCGTPNYIA 219
Cdd:cd14213 124 QICKSVNFLHHNKLTHTDLKPENiLFVQSDYvvkynpkmkrdertlknpDIKVVDFGSAT---YDDEHHSTLVSTRHYRA 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 220 PEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHI------------------------- 274
Cdd:cd14213 201 PEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPLPKHMiqktrkrkyfhhdqldwdehssagr 280
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21359873 275 ------NPVAA-------------SLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd14213 281 yvrrrcKPLKEfmlsqdvdheqlfDLIQKMLEYDPAKRITLDEALKHPFF 330
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
59-305 1.07e-13

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: 72.18  E-value: 1.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKI---------VPKSLLLKPHQREKMSMEISIHRSLAHQHVvgfhgffEDN--DFVF 127
Cdd:cd07837   9 IGEGTYGKVYKARDKNTGKLVALKKtrlemeeegVPSTALREVSLLQMLSQSIYIVRLLDVEHV-------EENgkPLLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 128 VVLELCRR--RSLLELHKRRKA--LTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEV-KIGDFGLATKVE 202
Cdd:cd07837  82 LVFEYLDTdlKKFIDSYGRGPHnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGLGRAFT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 203 YDGERKKTLCGTPNYIAPEVLSKKGH-SFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKK-----NEYSIP----- 271
Cdd:cd07837 162 IPIKSYTHEIVTLWYRAPEVLLGSTHySTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRllgtpNEEVWPgvskl 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 21359873 272 ------------------KHINPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07837 242 rdwheypqwkpqdlsravPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPYF 293
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
58-301 1.46e-13

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: 70.75  E-value: 1.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEisDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGffedndfVFVVLELCRRRS 137
Cdd:cd14068   1 LLGDGGFGSVYR--AVYRGEDVAVKIFNKHTSFRLLRQELVVLSHLHHPSLVALLAAGTAP-------RMLVMELAPKGS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKRRKA-LTEPEARYYLRQIVLGCQYLHRNRVIHRDLK-----LGNLFLNEDLEVKIGDFGLATKVEYDGerKKTL 211
Cdd:cd14068  72 LDALLQQDNAsLTRTLQHRIALHVADGLRYLHSAMIIYRDLKphnvlLFTLYPNCAIIAKIADYGIAQYCCRMG--IKTS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTPNYIAPEVlsKKG---HSFEVDVWSIGCIMYTLLVG--------KPPFETSclketYLRIKKNEYSIPKHIN----P 276
Cdd:cd14068 150 EGTPGFRAPEV--ARGnviYNQQADVYSFGLLLYDILTCgeriveglKFPNEFD-----ELAIQGKLPDPVKEYGcapwP 222
                       250       260
                ....*....|....*....|....*...
gi 21359873 277 VAASLIQKMLQTDPTARPT---INELLN 301
Cdd:cd14068 223 GVEALIKDCLKENPQCRPTsaqVFDILN 250
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
59-299 1.67e-13

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: 70.99  E-value: 1.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNdfVFVVLELCRRRSL 138
Cdd:cd14025   4 VGSGGFGQVYKVRHKHWKTWLAIKCPP-SLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELhkrrkALTEP---EARY-YLRQIVLGCQYLH--RNRVIHRDLKLGNLFLNEDLEVKIGDFGLA--------TKVEYD 204
Cdd:cd14025  81 EKL-----LASEPlpwELRFrIIHETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGLAkwnglshsHDLSRD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 205 GerkktLCGTPNYIAPEVLSKKGHSFEV--DVWSIGCIMYTLLVGKPPF-ETSCLKETYLRIKKN---EYSIPKHINPVA 278
Cdd:cd14025 156 G-----LRGTIAYLPPERFKEKNRCPDTkhDVYSFAIVIWGILTQKKPFaGENNILHIMVKVVKGhrpSLSPIPRQRPSE 230
                       250       260
                ....*....|....*....|....*
gi 21359873 279 AS----LIQKMLQTDPTARPTINEL 299
Cdd:cd14025 231 CQqmicLMKRCWDQDPRKRPTFQDI 255
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
101-304 1.78e-13

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: 70.47  E-value: 1.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGF----FEDND--FVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIH 174
Cdd:cd14012  48 ELESLKKLRHPNLVSYLAFsierRGRSDgwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVH 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 175 RDLKLGNLFLNEDLE---VKIGDFGL-ATKVEYDGERKKTLCGTPNYIAPEV------LSKKGhsfevDVWSIGCIMYTL 244
Cdd:cd14012 128 KSLHAGNVLLDRDAGtgiVKLTDYSLgKTLLDMCSRGSLDEFKQTYWLPPELaqgsksPTRKT-----DVWDLGLLFLQM 202
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 245 LVGKPPFEtsclKETYLrikkNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEF 304
Cdd:cd14012 203 LFGLDVLE----KYTSP----NPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHEF 254
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
110-302 1.80e-13

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: 71.58  E-value: 1.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 110 HQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKRRKALTE--------PEARYYLR-------QIVLGCQYLHRNRVI 173
Cdd:cd05101  89 HKNIINLLGACTQDGPLYVIVEYASKGNLREyLRARRPPGMEysydinrvPEEQMTFKdlvsctyQLARGMEYLASQKCI 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG--TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPP 250
Cdd:cd05101 169 HRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFtLGGSP 248
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 21359873 251 FETSCLKETYLRIKK-NEYSIPKHINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd05101 249 YPGIPVEELFKLLKEgHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVED 301
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
64-305 2.36e-13

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: 71.17  E-value: 2.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  64 FAKCFEisdaDTKEVFAGKIVPKSLLL--KPHQREKMSM--------EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd08216   6 IGKCFK----GGGVVHLAKHKPTNTLVavKKINLESDSKedlkflqqEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKRRKALTEPEA--RYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTL 211
Cdd:cd08216  82 AYGSCRDLLKTHFPEGLPELaiAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRVV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 CGTP-------NYIAPEVLSK--KGHSFEVDVWSIG---C---------------IMYTLLV-GKPP--FETSCLKETYL 261
Cdd:cd08216 162 HDFPksseknlPWLSPEVLQQnlLGYNEKSDIYSVGitaCelangvvpfsdmpatQMLLEKVrGTTPqlLDCSTYPLEED 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 262 RIKKNEYSIPKHINPVAA--------------SLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd08216 242 SMSQSEDSSTEHPNNRDTrdipyqrtfseafhQFVELCLQRDPELRPSASQLLAHSFF 299
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
59-245 2.47e-13

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: 70.69  E-value: 2.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCfEISDAD-----TKEVFAGKIVPKSlllKPHQREKMSMEISIHRSLAHQHVVGFHG--FFEDNDFVFVVLE 131
Cdd:cd05081  12 LGKGNFGSV-ELCRYDplgdnTGALVAVKQLQHS---GPDQQRDFQREIQILKALHSDFIVKYRGvsYGPGRRSLRLVME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE---- 206
Cdd:cd05081  88 YLPSGCLRDfLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDyyvv 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21359873 207 RKKTlcGTPNY-IAPEVLSKKGHSFEVDVWSIGCIMYTLL 245
Cdd:cd05081 168 REPG--QSPIFwYAPESLSDNIFSRQSDVWSFGVVLYELF 205
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
152-253 2.57e-13

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. 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 serine/threonine residues. The CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 71.20  E-value: 2.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 152 EARYYLRQIVLGCQYLHRNRVIHRDLKLGN-LFLNEDLE------------------VKIGDFGLATkveYDGERKKTLC 212
Cdd:cd14215 117 QVRHMAFQVCQAVKFLHDNKLTHTDLKPENiLFVNSDYEltynlekkrdersvkstaIRVVDFGSAT---FDHEHHSTIV 193
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21359873 213 GTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFET 253
Cdd:cd14215 194 STRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQT 234
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
59-314 2.69e-13

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: 70.88  E-value: 2.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEisdadTKEVFAGKIVP-KSLLLKPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd07869  13 LGEGSYATVYK-----GKSKVNGKLVAlKVIRLQEEEGTPFTAirEASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP 215
Cdd:cd07869  88 DLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 216 NYIAPEV-LSKKGHSFEVDVWSIGCIMYTLLVGKPPFE-----TSCLKETYLRI-KKNE------YSIPkHINPV----- 277
Cdd:cd07869 168 WYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPgmkdiQDQLERIFLVLgTPNEdtwpgvHSLP-HFKPErftly 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 21359873 278 -----------------AASLIQKMLQTDPTARPTINELLNDEFFTSgyIPARL 314
Cdd:cd07869 247 spknlrqawnklsyvnhAEDLASKLLQCFPKNRLSAQAALSHEYFSD--LPPRL 298
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
59-299 2.74e-13

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 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: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 70.37  E-value: 2.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFeisdadTKEVFA----GKIVPKSLLLK--PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd14206   5 IGNGWFGKVI------LGEIFSdytpAQVVVKELRVSagPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLE-LHKRRKA------LTEPEARYYLR---QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAtkve 202
Cdd:cd14206  79 CQLGDLKRyLRAQRKAdgmtpdLPTRDLRTLQRmayEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLS---- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 203 yDGERKKTLCGTPN-------YIAPEVLSKKGHSF-------EVDVWSIGCIMYTLL-VGKPPFE--------TSCLKET 259
Cdd:cd14206 155 -HNNYKEDYYLTPDrlwiplrWVAPELLDELHGNLivvdqskESNVWSLGVTIWELFeFGAQPYRhlsdeevlTFVVREQ 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21359873 260 YLRIKKNEYSIPKhinpvaASLIQKMLQT---DPTARPTINEL 299
Cdd:cd14206 234 QMKLAKPRLKLPY------ADYWYEIMQScwlPPSQRPSVEEL 270
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
66-293 3.00e-13

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: 70.27  E-value: 3.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  66 KCFEISDADTKEVFAGKIVPKSlllKPHQREKMSMeisIHRSLAHqhVVGFHGFFEDNDFVFVVLE----------LCRR 135
Cdd:cd05576  14 KVLLVMDTRTQETFILKGLRKS---SEYSRERKTI---IPRCVPN--MVCLRKYIISEESVFLVLQhaeggklwsyLSKF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRKALTE---PEARYYLRQ---------IVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE- 202
Cdd:cd05576  86 LNDKEIHQLFADLDErlaAASRFYIPEeciqrwaaeMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEd 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 203 -YDGERKKTLcgtpnYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFE---TSCLKETYLrikkneySIPKHINPVA 278
Cdd:cd05576 166 sCDSDAIENM-----YCAPEVGGISEETEACDWWSLGALLFELLTGKALVEchpAGINTHTTL-------NIPEWVSEEA 233
                       250
                ....*....|....*
gi 21359873 279 ASLIQKMLQTDPTAR 293
Cdd:cd05576 234 RSLLQQLLQFNPTER 248
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
159-251 3.95e-13

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: 70.06  E-value: 3.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCgTPNYIAPEVLSKKGHSFEVDVWSIG 238
Cdd:cd07862 118 QLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVV-TLWYRAPEVLLQSSYATPVDLWSVG 196
                        90
                ....*....|...
gi 21359873 239 CIMYTLLVGKPPF 251
Cdd:cd07862 197 CIFAEMFRRKPLF 209
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
110-302 4.45e-13

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: 70.82  E-value: 4.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 110 HQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRK---------ALTEPEARYYLR-------QIVLGCQYLHRNRVI 173
Cdd:cd05100  77 HKNIINLLGACTQDGPLYVLVEYASKGNLREYLRARRppgmdysfdTCKLPEEQLTFKdlvscayQVARGMEYLASQKCI 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG--TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPP 250
Cdd:cd05100 157 HRDLAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSP 236
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 21359873 251 FETSCLKETYLRIKK-NEYSIPKHINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd05100 237 YPGIPVEELFKLLKEgHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVED 289
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
101-299 4.88e-13

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: 69.67  E-value: 4.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEdNDFVFVVLELCRRRSLLELHKRRKALTEPEARY--YLRQIVLGCQYLHRNRVIHRDLK 178
Cdd:cd05073  56 EANVMKTLQHDKLVKLHAVVT-KEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLidFSAQIAEGMAFIEQRNYIHRDLR 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 179 LGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCL 256
Cdd:cd05073 135 AANILVSASLVCKIADFGLARVIEDNEYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSN 214
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21359873 257 KETyLRIKKNEYSIPKhINPVAASLIQKMLQ---TDPTARPTINEL 299
Cdd:cd05073 215 PEV-IRALERGYRMPR-PENCPEELYNIMMRcwkNRPEERPTFEYI 258
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
59-307 5.64e-13

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: 69.71  E-value: 5.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAkcfeisdadtkEVFAG------KIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDfVFVVLEL 132
Cdd:cd05070  17 LGNGQFG-----------EVWMGtwngntKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEP-IYIVTEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLELHK--RRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKT 210
Cdd:cd05070  85 MSKGSLLDFLKdgEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 211 LCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKNeYSIP-KHINPVAA-SLIQKML 286
Cdd:cd05070 165 GAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERG-YRMPcPQDCPISLhELMIHCW 243
                       250       260
                ....*....|....*....|...
gi 21359873 287 QTDPTARPTINELLN--DEFFTS 307
Cdd:cd05070 244 KKDPEERPTFEYLQGflEDYFTA 266
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
94-301 6.03e-13

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: 69.12  E-value: 6.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  94 QREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRV 172
Cdd:cd05066  48 QRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENGSLDAfLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGY 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 173 IHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP---NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGK 248
Cdd:cd05066 128 VHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKipiRWTAPEAIAYRKFTSASDVWSYGIVMWEVMsYGE 207
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 249 PPFETSCLKETYLRIKKNeYSIPKHINpVAASLIQKML---QTDPTARPTINELLN 301
Cdd:cd05066 208 RPYWEMSNQDVIKAIEEG-YRLPAPMD-CPAALHQLMLdcwQKDRNERPKFEQIVS 261
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
89-251 6.15e-13

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: 70.46  E-value: 6.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  89 LLKPHQRE----KMSMEISIHRSLAHQHVVGFHGFF------EDNDFVFVVLEL-----CRRRSLLELHKRRKaltepea 153
Cdd:cd07875  57 LSRPFQNQthakRAYRELVLMKCVNHKNIIGLLNVFtpqkslEEFQDVYIVMELmdanlCQVIQMELDHERMS------- 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 154 rYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCgTPNYIAPEVLSKKGHSFEVD 233
Cdd:cd07875 130 -YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVV-TRYYRAPEVILGMGYKENVD 207
                       170
                ....*....|....*...
gi 21359873 234 VWSIGCIMYTLLVGKPPF 251
Cdd:cd07875 208 IWSVGCIMGEMIKGGVLF 225
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
58-248 6.20e-13

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: 69.94  E-value: 6.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFA---KCFEiSDADTKEVfAGKIVpkslllkphqREKMSM------EISIHRSLA------HQHVVGFHGFFED 122
Cdd:cd14135   7 YLGKGVFSnvvRARD-LARGNQEV-AIKII----------RNNELMhkaglkELEILKKLNdadpddKKHCIRLLRHFEH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 123 NDFVFVVLELCRR--RSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED-LEVKIGDFGLAT 199
Cdd:cd14135  75 KNHLCLVFESLSMnlREVLKKYGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKkNTLKLCDFGSAS 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21359873 200 KVEyDGERkktlcgTPN-----YIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGK 248
Cdd:cd14135 155 DIG-ENEI------TPYlvsrfYRAPEIILGLPYDYPIDMWSVGCTLYELYTGK 201
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
59-299 6.97e-13

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: 69.00  E-value: 6.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAkcfeisdADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14058   1 VGRGSFG-------VVCKARWRNQIVAVKIIESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LE-LH--KRRKALTEPEARYYLRQIVLGCQYLHR---NRVIHRDLKLGNLFL-NEDLEVKIGDFGLATKVEYDGERKKtl 211
Cdd:cd14058  74 YNvLHgkEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLtNGGTVLKICDFGTACDISTHMTNNK-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 212 cGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETscLKETYLRIKKNEYS---------IPKHINpvaaSLI 282
Cdd:cd14058 152 -GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDH--IGGPAFRIMWAVHNgerppliknCPKPIE----SLM 224
                       250
                ....*....|....*..
gi 21359873 283 QKMLQTDPTARPTINEL 299
Cdd:cd14058 225 TRCWSKDPEKRPSMKEI 241
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
80-296 7.40e-13

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: 68.96  E-value: 7.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  80 AGKIVPKSLLLKPHQREkmsmEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARY-YLR 158
Cdd:cd13992  29 AIKHITFSRTEKRTILQ----ELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDWMFKSsFIK 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNRVI-HRDLKLGNLFLNEDLEVKIGDFGLA------TKVEYDG--ERKKTLcgtpnYIAPEVLSKKGHS 229
Cdd:cd13992 105 DIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFGLRnlleeqTNHQLDEdaQHKKLL-----WTAPELLRGSLLE 179
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 230 FEV----DVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIP--------KHINPVAASLIQKMLQTDPTARPTI 296
Cdd:cd13992 180 VRGtqkgDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKPFrpelavllDEFPPRLVLLVKQCWAENPEKRPSF 258
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
110-299 8.10e-13

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: 69.47  E-value: 8.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 110 HQHVVGFHGFFEDNDFVFVVLELCRRRSL---LELHKRRKALTEPEARYYLRQIVLGCQYLHRNR--VIHRDLKLGNLFL 184
Cdd:cd14159  51 HPNIVDLAGYSAQQGNYCLIYVYLPNGSLedrLHCQVSCPCLSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILL 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 185 NEDLEVKIGDFGLATKVEYDGE--------RKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFET-SC 255
Cdd:cd14159 131 DAALNPKLGDFGLARFSRRPKQpgmsstlaRTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVdSC 210
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 256 LKETYLR--IKKNE----------YSIPKHINPVAASLIQKMLqtDPTARPTINEL 299
Cdd:cd14159 211 SPTKYLKdlVKEEEeaqhtpttmtHSAEAQAAQLATSICQKHL--DPQAGPCPPEL 264
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
96-300 8.19e-13

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: 68.82  E-value: 8.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  96 EKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEAryyLRQIVL----GCQYLHRNR 171
Cdd:cd05112  44 EDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFSAET---LLGMCLdvceGMAYLEEAS 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 172 VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKP 249
Cdd:cd05112 121 VIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTGTKFPvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKI 200
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 250 PFETSCLKE------TYLRIKKNEYSiPKHInpvaASLIQKMLQTDPTARPTINELL 300
Cdd:cd05112 201 PYENRSNSEvvedinAGFRLYKPRLA-STHV----YEIMNHCWKERPEDRPSFSLLL 252
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
59-299 8.68e-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: 69.44  E-value: 8.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLL---LKPHQREKMSMEISIHRSLAHQ-HVVGFHGF-FEDNDFVFVVLELC 133
Cdd:cd05054  15 LGRGAFGKVIQASAFGIDKSATCRTVAVKMLkegATASEHKALMTELKILIHIGHHlNVVNLLGAcTKPGGPLMVIVEFC 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 R----------RRSLLELHKRRKALTEPEARY----------------YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED 187
Cdd:cd05054  95 KfgnlsnylrsKREEFVPYRDKGARDVEEEEDddelykepltledlicYSFQVARGMEFLASRKCIHRDLAARNILLSEN 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 188 LEVKIGDFGLATKVEYDGER-KKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPF------ETSC--L 256
Cdd:cd05054 175 NVVKICDFGLARDIYKDPDYvRKGDARLPlKWMAPESIFDKVYTTQSDVWSFGVLLWEIFsLGASPYpgvqmdEEFCrrL 254
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 21359873 257 KETYlRIKKNEYSIPkhinpvaaSLIQKML---QTDPTARPTINEL 299
Cdd:cd05054 255 KEGT-RMRAPEYTTP--------EIYQIMLdcwHGEPKERPTFSEL 291
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
152-245 9.75e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 70.88  E-value: 9.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  152 EARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE-RKKTLCGTPNYIAPEVLSKKGHSF 230
Cdd:PHA03210 268 QTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREaFDYGWVGTVATNSPEILAGDGYCE 347
                         90
                 ....*....|....*
gi 21359873  231 EVDVWSIGCIMYTLL 245
Cdd:PHA03210 348 ITDIWSCGLILLDML 362
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
82-301 1.02e-12

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated 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. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK 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: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 68.97  E-value: 1.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  82 KIVPKSlllKPHQR----EKMSMEISIHRSLAHQHVVGFHGFFEDND-FVFVVLELCrRRSLLEL-HKRRKALTEP-EAR 154
Cdd:cd14001  35 KINSKC---DKGQRslyqERLKEEAKILKSLNHPNIVGFRAFTKSEDgSLCLAMEYG-GKSLNDLiEERYEAGLGPfPAA 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 155 YYLR---QIVLGCQYLHRN-RVIHRDLKLGNLFLNEDLE-VKIGDFGLATKVEYDGE--RKKTLC--GTPNYIAPEVLSK 225
Cdd:cd14001 111 TILKvalSIARALEYLHNEkKILHGDIKSGNVLIKGDFEsVKLCDFGVSLPLTENLEvdSDPKAQyvGTEPWKAKEALEE 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 226 KGH-SFEVDVWSIGCIMYTLLVGKPP------FETSCLKETYLRIKKNEY-------SIPKHINPVAASLIQKML----- 286
Cdd:cd14001 191 GGViTDKADIFAYGLVLWEMMTLSVPhlnlldIEDDDEDESFDEDEEDEEayygtlgTRPALNLGELDDSYQKVIelfya 270
                       250
                ....*....|....*..
gi 21359873 287 --QTDPTARPTINELLN 301
Cdd:cd14001 271 ctQEDPKDRPSAAHIVE 287
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
156-300 1.07e-12

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: 69.62  E-value: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 156 YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE--RKKTLCGTPNYIAPEVLSKKGHSFEVD 233
Cdd:cd05102 177 YSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDyvRKGSARLPLKWMAPESIFDKVYTTQSD 256
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 234 VWSIGCIMYTLL-VGKPPFETSCLKETYL-RIKK-NEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd05102 257 VWSFGVLLWEIFsLGASPYPGVQINEEFCqRLKDgTRMRAPEYATPEIYRIMLSCWHGDPKERPTFSDLV 326
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
75-307 1.36e-12

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: 68.55  E-value: 1.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  75 TKEVFAGKIVPKSLLLKPHQREKMSMEIsIHRSLAHQHVVGFHGFFEDNDFVFVVLEL---CrrrslLELHKRRKALTEP 151
Cdd:cd06618  39 TGHVMAVKQMRRSGNKEENKRILMDLDV-VLKSHDCPYIVKCYGYFITDSDVFICMELmstC-----LDKLLKRIQGPIP 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 152 E------------ARYYLRQivlgcqylhRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTlCGTPNYIA 219
Cdd:cd06618 113 EdilgkmtvsivkALHYLKE---------KHGVIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTRS-AGCAAYMA 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 220 PEVLSKKGHS-FEV--DVWSIGCIMYTLLVGKPPFETSCLK-ETYLRIKKNEYSIP---KHINPVAASLIQKMLQTDPTA 292
Cdd:cd06618 183 PERIDPPDNPkYDIraDVWSLGISLVELATGQFPYRNCKTEfEVLTKILNEEPPSLppnEGFSPDFCSFVDLCLTKDHRY 262
                       250
                ....*....|....*
gi 21359873 293 RPTINELLNDEFFTS 307
Cdd:cd06618 263 RPKYRELLQHPFIRR 277
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
82-307 1.46e-12

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: 67.99  E-value: 1.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  82 KIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEdNDFVFVVLELCRRRSLLELHKRRKALTEPEARY--YLRQ 159
Cdd:cd05067  33 KVAIKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVT-QEPIYIITEYMENGSLVDFLKTPSGIKLTINKLldMAAQ 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 160 IVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIG 238
Cdd:cd05067 112 IAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPiKWTAPEAINYGTFTIKSDVWSFG 191
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 239 cIMYTLLV--GKPPFETSCLKETYLRIKKNeYSIPKHINpVAASLIQKMLQ---TDPTARPT---INELLNDeFFTS 307
Cdd:cd05067 192 -ILLTEIVthGRIPYPGMTNPEVIQNLERG-YRMPRPDN-CPEELYQLMRLcwkERPEDRPTfeyLRSVLED-FFTA 264
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
59-251 1.90e-12

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: 68.82  E-value: 1.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpKSlllKPHQREKMSMEISIHRSL-------AHQHVVGFHGFFEDNDFVFVVLE 131
Cdd:cd14212   7 LGQGTFGQVVKCQDLKTNKLVAVKVL-KN---KPAYFRQAMLEIAILTLLntkydpeDKHHIVRLLDHFMHHGHLCIVFE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRRrSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL--EVKIGDFGLA-----TKVE 202
Cdd:cd14212  83 LLGV-NLYELLKQNqfRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDspEIKLIDFGSAcfenyTLYT 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21359873 203 YDGERkktlcgtpNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd14212 162 YIQSR--------FYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLF 202
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
98-248 2.06e-12

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: 67.52  E-value: 2.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  98 MSMEISIHRSLA-HQHVVGFHGFFEDNDF-------VFVVLELCRRrsllELHKRRKA-LTEPEARYYLRQIVLGCQYLH 168
Cdd:cd13975  44 LALEFHYTRSLPkHERIVSLHGSVIDYSYgggssiaVLLIMERLHR----DLYTGIKAgLSLEERLQIALDVVEGIRFLH 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 169 RNRVIHRDLKLGNLFLNEDLEVKIGDFGLA-TKVEYDGerkkTLCGTPNYIAPEVLSKKGHSfEVDVWSIGCIMYTLLVG 247
Cdd:cd13975 120 SQGLVHRDIKLKNVLLDKKNRAKITDLGFCkPEAMMSG----SIVGTPIHMAPELFSGKYDN-SVDVYAFGILFWYLCAG 194

                .
gi 21359873 248 K 248
Cdd:cd13975 195 H 195
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
89-314 2.23e-12

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: 68.58  E-value: 2.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  89 LLKPHQRE----KMSMEISIHRSLAHQHVVGFHGFF------EDNDFVFVVLEL-----CRRRSLLELHKRRKaltepea 153
Cdd:cd07874  50 LSRPFQNQthakRAYRELVLMKCVNHKNIISLLNVFtpqkslEEFQDVYLVMELmdanlCQVIQMELDHERMS------- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 154 rYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCgTPNYIAPEVLSKKGHSFEVD 233
Cdd:cd07874 123 -YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVV-TRYYRAPEVILGMGYKENVD 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 234 VWSIGCIMYTLLVGKPPFE----------------TSC---LKETYLRIKKNEYSIPKHI-------------------N 275
Cdd:cd07874 201 IWSVGCIMGEMVRHKILFPgrdyidqwnkvieqlgTPCpefMKKLQPTVRNYVENRPKYAgltfpklfpdslfpadsehN 280
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 21359873 276 PVAAS----LIQKMLQTDPTARPTINELLNDEFFTSGYIPARL 314
Cdd:cd07874 281 KLKASqardLLSKMLVIDPAKRISVDEALQHPYINVWYDPAEV 323
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
101-300 2.91e-12

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: 67.36  E-value: 2.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELCRRRSLL----ELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHR 175
Cdd:cd14138  54 EVYAHAVLGqHSHVVRYYSAWAEDDHMLIQNEYCNGGSLAdaisENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHM 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 176 DLKLGNLFL-------------NEDLE------VKIGDFGLATKVEYDGERKktlcGTPNYIAPEVLSKK-GHSFEVDVW 235
Cdd:cd14138 134 DIKPSNIFIsrtsipnaaseegDEDEWasnkviFKIGDLGHVTRVSSPQVEE----GDSRFLANEVLQENyTHLPKADIF 209
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 236 SIGCIMYTlLVGKPPFETSclKETYLRIKKNEY-SIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd14138 210 ALALTVVC-AAGAEPLPTN--GDQWHEIRQGKLpRIPQVLSQEFLDLLKVMIHPDPERRPSAVALV 272
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
59-315 3.32e-12

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: 67.85  E-value: 3.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpkSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd06615   9 LGAGNGGVVTKVLHRPSGLIMARKLI--HLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPearyYLRQI----VLGCQYLHRNR-VIHRDLKLGNLFLNEDLEVKIGDFGLATkvEYDGERKKTLCG 213
Cdd:cd06615  87 DQVLKKAGRIPEN----ILGKIsiavLRGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSG--QLIDSMANSFVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGK---PPFETSCLkETYLRIKKNEYSIPKHINPVAASliqkmlQTDP 290
Cdd:cd06615 161 TRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRypiPPPDAKEL-EAMFGRPVSEGEAKESHRPVSGH------PPDS 233
                       250       260
                ....*....|....*....|....*....
gi 21359873 291 TARPTINELLNdefftsgYI----PARLP 315
Cdd:cd06615 234 PRPMAIFELLD-------YIvnepPPKLP 255
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
159-302 3.64e-12

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 66.73  E-value: 3.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKV---EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDV 234
Cdd:cd05058 106 QVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIydkEYYSVHNHTGAKLPvKWMALESLQTQKFTTKSDV 185
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 235 WSIGCIMYTLLV-GKPPF-ETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd05058 186 WSFGVLLWELMTrGAPPYpDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWHPKPEMRPTFSELVSR 255
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
59-302 4.43e-12

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: 66.91  E-value: 4.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAK-----CFEISDADTKEVFAGKIVPKSlllkPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLE 131
Cdd:cd05045   8 LGEGEFGKvvkatAFRLKGRAGYTTVAVKMLKEN----ASSSELRDLlsEFNLLKQVNHPHVIKLYGACSQDGPLLLIVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LCRR---RSLLELHKR---------------------RKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED 187
Cdd:cd05045  84 YAKYgslRSFLRESRKvgpsylgsdgnrnssyldnpdERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 188 LEVKIGDFGLATKV-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-------GKPPFETSCLKE 258
Cdd:cd05045 164 RKMKISDFGLSRDVyEEDSYVKRSKGRIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIAPERLFNLLK 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 21359873 259 TYLRIKKneysiPKHINPVAASLIQKMLQTDPTARPTINELLND 302
Cdd:cd05045 244 TGYRMER-----PENCSEEMYNLMLTCWKQEPDKRPTFADISKE 282
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
101-306 4.87e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 67.95  E-value: 4.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELcRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLG 180
Cdd:PHA03207 136 EIDILKTISHRAIINLIHAYRWKSTVCMVMPK-YKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTE 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  181 NLFLNEDLEVKIGDFGLATKVEYDGERKKTL--CGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF------- 251
Cdd:PHA03207 215 NIFLDEPENAVLGDFGAACKLDAHPDTPQCYgwSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLfgkqvks 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  252 -----------------------ETSCLKE--TYLRIKKNEYSIP----KHINPVAAS-LIQKMLQTDPTARPTINELLN 301
Cdd:PHA03207 295 sssqlrsiircmqvhplefpqngSTNLCKHfkQYAIVLRPPYTIPpvirKYGMHMDVEyLIAKMLTFDQEFRPSAQDILS 374

                 ....*
gi 21359873  302 DEFFT 306
Cdd:PHA03207 375 LPLFT 379
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
59-251 5.18e-12

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) 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 of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 66.96  E-value: 5.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAK-----CFEISDADTKEVFAGKIVPKSLLlkpHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05094  13 LGEGAFGKvflaeCYNLSPTKDKMLVAVKTLKDPTL---AARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSL---LELH-------------KRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGL 197
Cdd:cd05094  90 KHGDLnkfLRAHgpdamilvdgqprQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGM 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 198 ATKV-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPF 251
Cdd:cd05094 170 SRDVySTDYYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPW 226
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
160-299 9.05e-12

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: 66.02  E-value: 9.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 160 IVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeYDGE--RKKTLCGTP-NYIAPEVLSKKGHSFEVDVWS 236
Cdd:cd05035 122 IAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKI-YSGDyyRQGRISKMPvKWIALESLADNVYTSKSDVWS 200
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 237 IGCIMYTLLV-GKPPFETSCLKETY-LRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05035 201 FGVTMWEIATrGQTPYPGVENHEIYdYLRNGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKL 265
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
94-300 9.54e-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: 65.94  E-value: 9.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  94 QREKMSMEISIHRSLAHQHVVG-FHGFFEDNDFVFVVLELCRRRSL-LELHKRR-------KALTEPEARYYLRQIVLGC 164
Cdd:cd05043  50 QVTMLLQESSLLYGLSHQNLLPiLHVCIEDGEKPMVLYPYMNWGNLkLFLQQCRlseannpQALSTQQLVHMALQIACGM 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 165 QYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKV---EY----DGERKKTlcgtpNYIAPEVLSKKGHSFEVDVWSI 237
Cdd:cd05043 130 SYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLfpmDYhclgDNENRPI-----KWMSLESLVNKEYSSASDVWSF 204
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21359873 238 GCIMYTL--LVGKP-----PFETsclkETYLrikKNEYSIPKHINpVAASLIQKML---QTDPTARPTINELL 300
Cdd:cd05043 205 GVLLWELmtLGQTPyveidPFEM----AAYL---KDGYRLAQPIN-CPDELFAVMAccwALDPEERPSFQQLV 269
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
107-313 1.22e-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: 65.75  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 107 SLAHQHVVGFHGFFEDNDFVFVVlELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLN 185
Cdd:cd05111  65 SLDHAYIVRLLGICPGASLQLVT-QLLPLGSLLDhVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLK 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 186 EDLEVKIGDFGLATKVEYDGerKKTL---CGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLKETY 260
Cdd:cd05111 144 SPSQVQVADFGVADLLYPDD--KKYFyseAKTPiKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPYAGMRLAEVP 221
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21359873 261 LRIKKNEYSIPKHINPVAASLIQ-KMLQTDPTARPTINELLNdEFFTSGYIPAR 313
Cdd:cd05111 222 DLLEKGERLAQPQICTIDVYMVMvKCWMIDENIRPTFKELAN-EFTRMARDPPR 274
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
59-241 1.24e-11

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: 65.19  E-value: 1.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIvpKSLllkPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKM--NTL---SSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 139 LELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNED---LEVKIGDFGLATKVEYDGERKKTL--CG 213
Cdd:cd14155  76 EQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDengYTAVVGDFGLAEKIPDYSDGKEKLavVG 155
                       170       180
                ....*....|....*....|....*...
gi 21359873 214 TPNYIAPEVLSKKGHSFEVDVWSIGCIM 241
Cdd:cd14155 156 SPYWMAPEVLRGEPYNEKADVFSYGIIL 183
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
59-247 1.33e-11

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: 66.06  E-value: 1.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVpKSlllKPHQREKMSMEISIHRSLAH--------QHVVGFHGFFEDND------ 124
Cdd:cd14136  18 LGWGHFSTVWLCWDLQNKRFVALKVV-KS---AQHYTEAALDEIKLLKCVREadpkdpgrEHVVQLLDDFKHTGpngthv 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 -FVFVVLElcrrRSLLELHKRR--KALTEPEARYYLRQIVLGCQYLHRN-RVIHRDLKLGNLFLNE-DLEVKIGDFGLAT 199
Cdd:cd14136  94 cMVFEVLG----PNLLKLIKRYnyRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCIsKIEVKIADLGNAC 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21359873 200 KVEydgERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVG 247
Cdd:cd14136 170 WTD---KHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATG 214
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
59-251 1.43e-11

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: 66.31  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllKPHQREKMSmEISIHRSLAHQHVVGFHGFFEDND-FVF-----VVLEL 132
Cdd:cd14224  73 IGKGSFGQVVKAYDHKTHQHVALKMVRNE---KRFHRQAAE-EIRILEHLKKQDKDNTMNVIHMLEsFTFrnhicMTFEL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRrSLLELHKRRK--ALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE--VKIGDFGLATkveYDGERK 208
Cdd:cd14224 149 LSM-NLYELIKKNKfqGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSSC---YEHQRI 224
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21359873 209 KTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd14224 225 YTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLF 267
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
92-299 1.97e-11

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: 64.68  E-value: 1.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  92 PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVfVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR 171
Cdd:cd05060  37 KAGKKEFLREASVMAQLDHPCIVRLIGVCKGEPLM-LVMELAPLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKH 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 172 VIHRDLKLGNLFLNEDLEVKIGDFGL--ATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VG 247
Cdd:cd05060 116 FVHRDLAARNVLLVNRHQAKISDFGMsrALGAGSDYYRATTAGRWPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFsYG 195
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 248 KPPF------ETSCLKETYLRIKKNEySIPKHInpvaASLIQKMLQTDPTARPTINEL 299
Cdd:cd05060 196 AKPYgemkgpEVIAMLESGERLPRPE-ECPQEI----YSIMLSCWKYRPEDRPTFSEL 248
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
90-253 2.45e-11

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function 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. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 64.64  E-value: 2.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  90 LKPHQREKMSmeisiHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTE-PEARYYLRQIVLGCQYLH 168
Cdd:cd14153  40 LKAFKREVMA-----YRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKVVLDvNKTRQIAQEIVKGMGYLH 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 169 RNRVIHRDLKLGNLFLNEDlEVKIGDFGLAT--KVEYDGERKKTL---CGTPNYIAPEVL---------SKKGHSFEVDV 234
Cdd:cd14153 115 AKGILHKDLKSKNVFYDNG-KVVITDFGLFTisGVLQAGRREDKLriqSGWLCHLAPEIIrqlspeteeDKLPFSKHSDV 193
                       170
                ....*....|....*....
gi 21359873 235 WSIGCIMYTLLVGKPPFET 253
Cdd:cd14153 194 FAFGTIWYELHAREWPFKT 212
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
101-299 2.54e-11

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl 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: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 64.36  E-value: 2.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKR--RKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLK 178
Cdd:cd05052  52 EAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDYLREcnREELNAVVLLYMATQIASAMEYLEKKNFIHRDLA 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 179 LGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCL 256
Cdd:cd05052 132 ARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPiKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPGIDL 211
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21359873 257 KETYLRIKKNeYSI--PKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05052 212 SQVYELLEKG-YRMerPEGCPPKVYELMRACWQWNPSDRPSFAEI 255
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
156-299 2.56e-11

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: 64.55  E-value: 2.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 156 YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeYDGERKKTLCGTP---NYIAPEVLSKKGHSFEV 232
Cdd:cd05074 128 FMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKI-YSGDYYRQGCASKlpvKWLALESLADNVYTTHS 206
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 233 DVWSIGCIMYTLLV-GKPPFETSCLKETY-LRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05074 207 DVWAFGVTMWEIMTrGQTPYAGVENSEIYnYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHL 275
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
58-255 2.92e-11

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: 65.16  E-value: 2.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGF---AKCFEISdadTKEVFAGKIvpksllLK--PHQREKMSMEISIHRSLAHQ-----HVVGFHGFFEDNDFVF 127
Cdd:cd14211   6 FLGRGTFgqvVKCWKRG---TNEIVAIKI------LKnhPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 128 VVLELCRRrSLLELHKRRK--ALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDL----EVKIGDFGLATKV 201
Cdd:cd14211  77 LVFEMLEQ-NLYDFLKQNKfsPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFGSASHV 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21359873 202 EydgerkKTLCGT----PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSC 255
Cdd:cd14211 156 S------KAVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSS 207
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
101-300 2.99e-11

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: 64.13  E-value: 2.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKL 179
Cdd:cd05113  49 EAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNyLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAA 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 180 GNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPFETSCLK 257
Cdd:cd05113 129 RNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYsLGKMPYERFTNS 208
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21359873 258 ETYLRIKKN-EYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd05113 209 ETVEHVSQGlRLYRPHLASEKVYTIMYSCWHEKADERPTFKILL 252
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
58-249 4.07e-11

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: 64.66  E-value: 4.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  58 FLGKGGFAKCFEISDADTKEVFAGKIVPKslllKPHQREKMSMEISIHRSLA------HQHVVGFHGFFEDND--FVFVV 129
Cdd:cd14229   7 FLGRGTFGQVVKCWKRGTNEIVAVKILKN----HPSYARQGQIEVGILARLSnenadeFNFVRAYECFQHRNHtcLVFEM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 130 LElcrrRSLLELHKRRK--ALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL----NEDLEVKIGDFGLATKVEy 203
Cdd:cd14229  83 LE----QNLYDFLKQNKfsPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHVS- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21359873 204 dgerkKTLCGT----PNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKP 249
Cdd:cd14229 158 -----KTVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWP 202
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
159-343 4.22e-11

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: 64.27  E-value: 4.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGL-----ATKVEYDGERKKtlcgTP-NYIAPEVLSKKGHSFEV 232
Cdd:cd05108 117 QIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLakllgAEEKEYHAEGGK----VPiKWMALESILHRIYTHQS 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 233 DVWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKNEySIPKhiNPVAA----SLIQKMLQTDPTARPTINELLNdEFFTS 307
Cdd:cd05108 193 DVWSYGVTVWELMTfGSKPYDGIPASEISSILEKGE-RLPQ--PPICTidvyMIMVKCWMIDADSRPKFRELII-EFSKM 268
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 21359873 308 GYIPARLPITCLTIPprfSIAPSSLDPSNRKPLTVL 343
Cdd:cd05108 269 ARDPQRYLVIQGDER---MHLPSPTDSNFYRALMDE 301
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
59-299 4.75e-11

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: 63.85  E-value: 4.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFeisdadTKEVFAG----KIVPKSLLLKPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd05087   5 IGHGWFGKVF------LGEVNSGlsstQVVVKELKASASVQDQMQFleEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSL---LELHKRRKALTePEARYYLR---QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA-TKVEYDG 205
Cdd:cd05087  79 CPLGDLkgyLRSCRAAESMA-PDPLTLQRmacEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLShCKYKEDY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 206 ERKKTLCGTP-NYIAPEVLSK-KGHSFEVD------VWSIGCIMYTLL-VGKPPFETSCLKE--TYlRIKKNEYSIPKHI 274
Cdd:cd05087 158 FVTADQLWVPlRWIAPELVDEvHGNLLVVDqtkqsnVWSLGVTIWELFeLGNQPYRHYSDRQvlTY-TVREQQLKLPKPQ 236
                       250       260
                ....*....|....*....|....*....
gi 21359873 275 NPVAAS----LIQKMLQTDPTARPTINEL 299
Cdd:cd05087 237 LKLSLAerwyEVMQFCWLQPEQRPTAEEV 265
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
110-300 5.21e-11

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie 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: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 63.52  E-value: 5.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 110 HQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKRRKALTEP---------------EARYYLRQIVLGCQYLHRNRVI 173
Cdd:cd05047  55 HPNIINLLGACEHRGYLYLAIEYAPHGNLLDfLRKSRVLETDPafaianstastlssqQLLHFAADVARGMDYLSQKQFI 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYdgERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPF 251
Cdd:cd05047 135 HRDLAARNILVGENYVAKIADFGLSRGQEV--YVKKTMGRLPvRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPY 212
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21359873 252 ETSCLKETYLRIKKN-EYSIPKHINPVAASLIQKMLQTDPTARPTINELL 300
Cdd:cd05047 213 CGMTCAELYEKLPQGyRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 262
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
160-252 5.33e-11

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: 63.89  E-value: 5.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 160 IVLGCQYLHRNR----------VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTL--CGTPNYIAPEVL---- 223
Cdd:cd14053 101 MARGLAYLHEDIpatngghkpsIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGKSCGDTHgqVGTRRYMAPEVLegai 180
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21359873 224 SKKGHSF-EVDVWSIGCIMYTLL-----VGKP------PFE 252
Cdd:cd14053 181 NFTRDAFlRIDMYAMGLVLWELLsrcsvHDGPvdeyqlPFE 221
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
159-313 6.79e-11

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: 63.50  E-value: 6.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG-TP-NYIAPEVLSKKGHSFEVDVWS 236
Cdd:cd05109 117 QIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGkVPiKWMALESILHRRFTHQSDVWS 196
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 237 IGCIMYTLLV-GKPPFETSCLKETYLRIKKNE-YSIPKHINPVAASLIQKMLQTDPTARPTINELLnDEFFTSGYIPAR 313
Cdd:cd05109 197 YGVTVWELMTfGAKPYDGIPAREIPDLLEKGErLPQPPICTIDVYMIMVKCWMIDSECRPRFRELV-DEFSRMARDPSR 274
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
59-301 7.07e-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: 63.25  E-value: 7.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCF-----EISDADTKEVfagkIVPKSLLLKPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLE 131
Cdd:cd05046  13 LGRGEFGEVFlakakGIEEEGGETL----VLVKALQKTKDENLQSEFrrELDMFRKLSHKNVVRLLGLCREAEPHYMILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 132 LC---------RRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLaTKVE 202
Cdd:cd05046  89 YTdlgdlkqflRATKSKDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSL-SKDV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 203 YDGE--RKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKNEYSIPKHINpvAA 279
Cdd:cd05046 168 YNSEyyKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELPVPEG--CP 245
                       250       260
                ....*....|....*....|....*.
gi 21359873 280 SLIQKMLQT----DPTARPTINELLN 301
Cdd:cd05046 246 SRLYKLMTRcwavNPKDRPSFSELVS 271
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
101-313 7.10e-11

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: 63.20  E-value: 7.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 101 EISIHRSLAHQHVVGFHGFFEDNDfVFVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKL 179
Cdd:cd05057  59 EAYVMASVDHPHLVRLLGICLSSQ-VQLITQLMPLGCLLDyVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAA 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 180 GNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCG-TP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPPFETSCL 256
Cdd:cd05057 138 RNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEGGkVPiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEGIPA 217
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21359873 257 KETYLRIKKNEySIPKhinPVAASLIQKML-----QTDPTARPTINELLNdEFFTSGYIPAR 313
Cdd:cd05057 218 VEIPDLLEKGE-RLPQ---PPICTIDVYMVlvkcwMIDAESRPTFKELAN-EFSKMARDPQR 274
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
110-299 7.59e-11

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; 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. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 63.48  E-value: 7.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 110 HQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKAL-TEP------------EARYYLR---QIVLGCQYLHRNRVI 173
Cdd:cd05089  62 HPNIINLLGACENRGYLYIAIEYAPYGNLLDFLRKSRVLeTDPafakehgtastlTSQQLLQfasDVAKGMQYLSEKQFI 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 174 HRDLKLGNLFLNEDLEVKIGDFGLATKVEYdgERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VGKPPF 251
Cdd:cd05089 142 HRDLAARNVLVGENLVSKIADFGLSRGEEV--YVKKTMGRLPvRWMAIESLNYSVYTTKSDVWSFGVLLWEIVsLGGTPY 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21359873 252 ETSCLKETYLRIKKN-EYSIPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05089 220 CGMTCAELYEKLPQGyRMEKPRNCDDEVYELMRQCWRDRPYERPPFSQI 268
pknD PRK13184
serine/threonine-protein kinase PknD;
59-302 7.62e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 65.18  E-value: 7.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873   59 LGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSL 138
Cdd:PRK13184  10 IGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGYTL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  139 LELHKR-------RKALTEPEA-RYYLR---QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE- 206
Cdd:PRK13184  90 KSLLKSvwqkeslSKELAEKTSvGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFKKLEEEd 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  207 ------RKKTLC-----------GTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLR---IKKN 266
Cdd:PRK13184 170 lldidvDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKISYRdviLSPI 249
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 21359873  267 EYSIPKHINPVAASLIQKMLQTDPTAR-PTINELLND 302
Cdd:PRK13184 250 EVAPYREIPPFLSQIAMKALAVDPAERySSVQELKQD 286
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
59-305 1.03e-10

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 63.16  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEvfagkivPKSLLLKPHQREKMSM----EISIHRSLAHQHVVGFHGFF--EDNDFVFVVLEL 132
Cdd:cd07867  10 VGRGTYGHVYKAKRKDGKD-------EKEYALKQIEGTGISMsacrEIALLRELKHPNVIALQKVFlsHSDRKVWLLFDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRR--SLLELHKRRKALTEPE------ARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL----NEDLEVKIGDFGLATK 200
Cdd:cd07867  83 AEHDlwHIIKFHRASKANKKPMqlprsmVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 201 VEYDGERKKTL---CGTPNYIAPE-VLSKKGHSFEVDVWSIGCIMYTLLVGKPPF------------------------- 251
Cdd:cd07867 163 FNSPLKPLADLdpvVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFhcrqediktsnpfhhdqldrifsvm 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 252 ---------------ETSCLKETYLRIKKNEYSIPKHINPVAAS-------LIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07867 243 gfpadkdwedirkmpEYPTLQKDFRRTTYANSSLIKYMEKHKVKpdskvflLLQKLLTMDPTKRITSEQALQDPYF 318
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
159-294 1.03e-10

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: 62.67  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNRVIHRDLKLGNLFL-----NEDLEVKIGDFGLATKVEYDGERKktLCGTPNYIAPEVLSKKGHSFEVD 233
Cdd:cd14067 122 QIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINIKLSDYGISRQSFHEGALG--VEGTPGYQAPEIRPRIVYDEKVD 199
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21359873 234 VWSIGCIMYTLLVGKPPfetsCLKETYLRIKKNeysIPKHINPVAA-----------SLIQKMLQTDPTARP 294
Cdd:cd14067 200 MFSYGMVLYELLSGQRP----SLGHHQLQIAKK---LSKGIRPVLGqpeevqffrlqALMMECWDTKPEKRP 264
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
141-242 1.08e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 64.14  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  141 LHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEydGERKKT----LCGTPN 216
Cdd:PHA03211 250 LGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFAR--GSWSTPfhygIAGTVD 327
                         90       100
                 ....*....|....*....|....*.
gi 21359873  217 YIAPEVLSKKGHSFEVDVWSIGCIMY 242
Cdd:PHA03211 328 TNAPEVLAGDPYTPSVDIWSAGLVIF 353
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
59-254 1.18e-10

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: 62.48  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGF-----AKCFEISDADTKEVFAGKIVPKSLLlkPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELC 133
Cdd:cd05049  13 LGEGAFgkvflGECYNLEPEQDKMLVAVKTLKDASS--PDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFEYM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 134 RRRSLLELHKR-----RKALTEPEARYYLR---------QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLAT 199
Cdd:cd05049  91 EHGDLNKFLRShgpdaAFLASEDSAPGELTlsqllhiavQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGMSR 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21359873 200 KV-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLLV-GKPP-FETS 254
Cdd:cd05049 171 DIySTDYYRVGGHTMLPiRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPwFQLS 229
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
92-294 1.18e-10

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: 62.29  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  92 PHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVfVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNR 171
Cdd:cd05116  37 PALKDELLREANVMQQLDNPYIVRMIGICEAESWM-LVMEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESN 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 172 VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGE--RKKTLCGTP-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL-VG 247
Cdd:cd05116 116 FVHRDLAARNVLLVTQHYAKISDFGLSKALRADENyyKAQTHGKWPvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFsYG 195
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21359873 248 KPPFETSCLKETYLRIKKNE-YSIPKHINPVAASLIQKMLQTDPTARP 294
Cdd:cd05116 196 QKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLMKLCWTYDVDERP 243
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
153-297 1.52e-10

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: 62.51  E-value: 1.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 153 ARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE----VKIGDFGLATKVEYDGER------KKTLCGTPNYIAPEV 222
Cdd:cd14018 140 ARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDgcpwLVIADFGCCLADDSIGLQlpfsswYVDRGGNACLMAPEV 219
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 223 LSKKGHSFEV------DVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEY--SIPKHINPVAASLIQKMLQTDPTARP 294
Cdd:cd14018 220 STAVPGPGVVinyskaDAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQlpALPSAVPPDVRQVVKDLLQRDPNKRV 299

                ...
gi 21359873 295 TIN 297
Cdd:cd14018 300 SAR 302
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
93-301 2.01e-10

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: 61.81  E-value: 2.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  93 HQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLE-LHKRRKALTEPEARYYLRQIVLGCQYLHRNR 171
Cdd:cd05065  47 KQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENGALDSfLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMN 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 172 VIHRDLKLGNLFLNEDLEVKIGDFGLATKVEyDGERKKTLCGT-----P-NYIAPEVLSKKGHSFEVDVWSIGCIMYTLL 245
Cdd:cd05065 127 YVHRDLAARNILVNSNLVCKVSDFGLSRFLE-DDTSDPTYTSSlggkiPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVM 205
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 246 -VGKPPFETSCLKETYLRIKKnEYSIPKHINpVAASLIQKML---QTDPTARPTINELLN 301
Cdd:cd05065 206 sYGERPYWDMSNQDVINAIEQ-DYRLPPPMD-CPTALHQLMLdcwQKDRNLRPKFGQIVN 263
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
59-260 2.31e-10

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: 61.50  E-value: 2.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKIVPKSlllkpHQREKMSMEISIHRSLA-HQHVVGFHGFFEDNDFVFVVLELCRRrS 137
Cdd:cd14017   8 IGGGGFGEIYKVRDVVDGEEVAMKVESKS-----QPKQVLKMEVAVLKKLQgKPHFCRLIGCGRTERYNYIVMTLLGP-N 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 138 LLELHKR--RKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGN----LFLNEDLEVKIGDFGLA---TKVEYDGERK 208
Cdd:cd14017  82 LAELRRSqpRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNfaigRGPSDERTVYILDFGLArqyTNKDGEVERP 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21359873 209 KT----LCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVG-------KPPFETSCLKETY 260
Cdd:cd14017 162 PRnaagFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGqlpwrklKDKEEVGKMKEKI 224
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
59-305 5.67e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 61.23  E-value: 5.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEvfagkivPKSLLLKPHQREKMSM----EISIHRSLAHQHVVGFHGFF--EDNDFVFVVLEL 132
Cdd:cd07868  25 VGRGTYGHVYKAKRKDGKD-------DKDYALKQIEGTGISMsacrEIALLRELKHPNVISLQKVFlsHADRKVWLLFDY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRR--SLLELHKRRKALTEP------EARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFL----NEDLEVKIGDFGLATK 200
Cdd:cd07868  98 AEHDlwHIIKFHRASKANKKPvqlprgMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARL 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 201 VEYDGERKKTL---CGTPNYIAPE-VLSKKGHSFEVDVWSIGCIMYTLLVGKPPF------------------------- 251
Cdd:cd07868 178 FNSPLKPLADLdpvVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFhcrqediktsnpyhhdqldrifnvm 257
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 252 ---------------ETSCLKETYLRIKKNEYSIPKHI-------NPVAASLIQKMLQTDPTARPTINELLNDEFF 305
Cdd:cd07868 258 gfpadkdwedikkmpEHSTLMKDFRRNTYTNCSLIKYMekhkvkpDSKAFHLLQKLLTMDPIKRITSEQAMQDPYF 333
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
156-299 6.49e-10

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer 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 Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 60.33  E-value: 6.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 156 YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVeYDGE--RKKTLCGTP-NYIAPEVLSKKGHSFEV 232
Cdd:cd14204 125 FMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKI-YSGDyyRQGRIAKMPvKWIAVESLADRVYTVKS 203
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21359873 233 DVWSIGCIMYTLLV-GKPPFETSCLKETY------LRIKKNEYSIPKhinpvAASLIQKMLQTDPTARPTINEL 299
Cdd:cd14204 204 DVWAFGVTMWEIATrGMTPYPGVQNHEIYdyllhgHRLKQPEDCLDE-----LYDIMYSCWRSDPTDRPTFTQL 272
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
59-251 9.05e-10

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: 59.98  E-value: 9.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFeisdadtKEVFAGKIVPKSLLLKPHQREKMSM---EISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd14152   8 IGQGRWGKVH-------RGRWHGEVAIRLLEIDGNNQDHLKLfkkEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 136 RSLLELHKRRK-ALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDlEVKIGDFGL--ATKVEYDGERKKTLC 212
Cdd:cd14152  81 RTLYSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGLfgISGVVQEGRRENELK 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21359873 213 GTPN---YIAPEVLSKKG---------HSFEVDVWSIGCIMYTLLVGKPPF 251
Cdd:cd14152 160 LPHDwlcYLAPEIVREMTpgkdedclpFSKAADVYAFGTIWYELQARDWPL 210
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
59-242 1.31e-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: 59.31  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKcfeisdadtkeVFAGKIVPK-------SLLLK-------PHQREKMSMEISIHRSLAHQHVVGFHGFFEDND 124
Cdd:cd05048  13 LGEGAFGK-----------VYKGELLGPsseesaiSVAIKtlkenasPKTQQDFRREAELMSDLQHPNIVCLLGVCTKEQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 FVFVVLELCRRRSLLELHKRRKALTEPEARYYLR----------------QIVLGCQYLHRNRVIHRDLKLGNLFLNEDL 188
Cdd:cd05048  82 PQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDgtassldqsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLVGDGL 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21359873 189 EVKIGDFGLATKVeYDGERKKTLCGTP---NYIAPEVLSKKGHSFEVDVWSIGCIMY 242
Cdd:cd05048 162 TVKISDFGLSRDI-YSSDYYRVQSKSLlpvRWMPPEAILYGKFTTESDVWSFGVVLW 217
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
59-251 1.38e-09

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: 59.14  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFeisdadTKEVFAG----KIVPKSLLLKPHQREKMSM--EISIHRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd05042   3 IGNGWFGKVL------LGEIYSGtsvaQVVVKELKASANPKEQDTFlkEGQPYRILQHPNILQCLGQCVEAIPYLLVMEF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRRSLLE-LHKRRKA-LTEPEARYYLR---QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA---TKVEYD 204
Cdd:cd05042  77 CDLGDLKAyLRSEREHeRGDSDTRTLQRmacEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAhsrYKEDYI 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21359873 205 gERKKTLCGTPNYIAPEVLSKKGHSFEV-------DVWSIGCIMYTLL-VGKPPF 251
Cdd:cd05042 157 -ETDDKLWFPLRWTAPELVTEFHDRLLVvdqtkysNIWSLGVTLWELFeNGAQPY 210
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
59-301 1.59e-09

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: 59.19  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEisdADTKE------VFAgkIVPKSLLLKPHQRekMSMEISIhRSLAHQHVVGFHGFFEDNDFVFVVLEL 132
Cdd:cd13980   8 LGSTRFLKVAR---ARHDEglvvvkVFV--KPDPALPLRSYKQ--RLEEIRD-RLLELPNVLPFQKVIETDKAAYLIRQY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 133 CRRrSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVE---------- 202
Cdd:cd13980  80 VKY-NLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKPTYlpednpadfs 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 203 --YDGERKKTlCgtpnYIAPE-------VLSKKGHSF-----EVDVWSIGC-IMYTLLVGKPPFETSCLketyLRIKKNE 267
Cdd:cd13980 159 yfFDTSRRRT-C----YIAPErfvdaltLDAESERRDgeltpAMDIFSLGCvIAELFTEGRPLFDLSQL----LAYRKGE 229
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21359873 268 YSIPKHI----NPVAASLIQKMLQTDPTARPTINELLN 301
Cdd:cd13980 230 FSPEQVLekieDPNIRELILHMIQRDPSKRLSAEDYLK 267
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
125-299 1.81e-09

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L 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: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 59.49  E-value: 1.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 125 FVFVVLELCRRRSLLELHKRRKaltePEARY---YLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLE---VKIGDFGLA 198
Cdd:cd13977 109 YLWFVMEFCDGGDMNEYLLSRR----PDRQTntsFMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGepiLKVADFGLS 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 199 TKVEYDGERKK-----------TLCGTPNYIAPEVLskKGH-SFEVDVWSIGCIMYTL--------------LVG---KP 249
Cdd:cd13977 185 KVCSGSGLNPEepanvnkhflsSACGSDFYMAPEVW--EGHyTAKADIFALGIIIWAMveritfrdgetkkeLLGtyiQQ 262
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21359873 250 PFETSCLKETYLRIKKNEYSIP----KHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd13977 263 GKEIVPLGEALLENPKLELQIPlkkkKSMNDDMKQLLRDMLAANPQERPDAFQL 316
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
59-196 2.07e-09

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: 55.91  E-value: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873  59 LGKGGFAKCFEISDADTKEVFAGKI---VPKSLLLKPHQREKMSMEISIHRslahQHVVGFHGFFEDNDFVFVVLELCRR 135
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIgddVNNEEGEDLESEMDILRRLKGLE----LNIPKVLVTEDVDGPNILLMELVKG 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21359873 136 RSLLELHKRRKaLTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFG 196
Cdd:cd13968  77 GTLIAYTQEEE-LDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
159-299 2.09e-09

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: 58.87  E-value: 2.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21359873 159 QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKV---EYDGERKKTLCGTpNYIAPEVLSKKGHSFEVDVW 235
Cdd:cd05090 132 QIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSREIyssDYYRVQNKSLLPI-RWMPPEAIMYGKFSSDSDIW 210
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21359873 236 SIGCIMYTLL-VGKPPFETSCLKETYLRIKKNE-YSIPKHINPVAASLIQKMLQTDPTARPTINEL 299
Cdd:cd05090 211 SFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQlLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
 
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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