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Conserved domains on  [gi|1024249297|ref|NP_001311255|]
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serine/threonine-protein kinase PAK 3 isoform a [Homo sapiens]

Protein Classification

serine/threonine-protein kinase PAK 3( domain architecture ID 11108711)

serine/threonine-protein kinase PAK 3 (p21-activated kinase 3) catalyzes 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
248-544 0e+00

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: 608.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 248 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 327
Cdd:cd06656     1 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 328 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 407
Cdd:cd06656    81 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 408 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 487
Cdd:cd06656   161 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 488 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR 544
Cdd:cd06656   241 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR 297
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
69-126 2.92e-25

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


:

Pssm-ID: 395634  Cd Length: 59  Bit Score: 98.54  E-value: 2.92e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297  69 EISLPSDFEHTIHVGFDAVTGEFTGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFY 126
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFTGLPPEWAKLLDSSGITEDEQKENPKAVLDVLKFY 58
 
Name Accession Description Interval E-value
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
248-544 0e+00

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: 608.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 248 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 327
Cdd:cd06656     1 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 328 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 407
Cdd:cd06656    81 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 408 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 487
Cdd:cd06656   161 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 488 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR 544
Cdd:cd06656   241 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR 297
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
268-519 2.26e-103

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 311.00  E-value: 2.26e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  347 GGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQsKRSTMVGT 425
Cdd:smart00220  81 GGDLFDLLKKRgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-KLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  426 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPE-RLSAVFRDFLNRCLEMDV 504
Cdd:smart00220 160 PEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDISPEAKDLIRKLLVKDP 239
                          250
                   ....*....|....*
gi 1024249297  505 DRRGSAKELLQHPFL 519
Cdd:smart00220 240 EKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
268-519 5.73e-68

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 218.65  E-value: 5.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDknILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTE-TCMDEGQIAAVCREclqaldflhsnqvihrdiksdnILLGMDGSVKLTDFgfcaqitpeqskrstmVG 424
Cdd:pfam00069  81 EGGSLFDLLSEkGAFSEREAKFIMKQ----------------------ILEGLESGSSLTTF----------------VG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDV 504
Cdd:pfam00069 123 TPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKKDP 202
                         250
                  ....*....|....*
gi 1024249297 505 DRRGSAKELLQHPFL 519
Cdd:pfam00069 203 SKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
267-515 2.71e-65

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 220.27  E-value: 2.71e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:COG0515     8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpeLAADPEaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-T 421
Cdd:COG0515    88 YVEGESLADLLRRRgPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTgT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN-GTPELQNPERLSAVFRDFLNRCL 500
Cdd:COG0515   168 VVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREpPPPPSELRPDLPPALDAIVLRAL 247
                         250
                  ....*....|....*.
gi 1024249297 501 EMDVDRR-GSAKELLQ 515
Cdd:COG0515   248 AKDPEERyQSAAELAA 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
272-518 3.79e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 139.95  E-value: 3.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQ---QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:PTZ00263   24 ETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREilkMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTETCMDEGQIAAV-CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeqSKRSTMVGTPY 427
Cdd:PTZ00263  104 ELFTHLRKAGRFPNDVAKFyHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP---DRTFTLCGTPE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMDVDRR 507
Cdd:PTZ00263  181 YLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAG---RLKFPNWFDGRARDLVKGLLQTDHTKR 257
                         250
                  ....*....|....*.
gi 1024249297 508 -GSAK----ELLQHPF 518
Cdd:PTZ00263  258 lGTLKggvaDVKNHPY 273
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
272-467 2.79e-28

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 118.74  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIINEILVMR---ENKN------PNIVNYLDsylVGDE---LW 339
Cdd:NF033483   13 ERIGRGGMAEVYLAKDTRLDRDVAVKVL------RPDLARDPEFVARfrrEAQSaaslshPNIVSVYD---VGEDggiPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGGSLTDVVTEtcmdEG-----QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG---FCAQ 411
Cdd:NF033483   84 IVMEYVDGRTLKDYIRE----HGplspeEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiarALSS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 412 ITPEQSkrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENP 467
Cdd:NF033483  160 TTMTQT--NSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSP 213
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
69-126 2.92e-25

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 98.54  E-value: 2.92e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297  69 EISLPSDFEHTIHVGFDAVTGEFTGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFY 126
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFTGLPPEWAKLLDSSGITEDEQKENPKAVLDVLKFY 58
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
68-113 8.02e-23

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


Pssm-ID: 238526  Cd Length: 46  Bit Score: 91.18  E-value: 8.02e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297  68 PEISLPSDFEHTIHVGFDAVTGEFTGIPEQWARLLQTSNITKLEQK 113
Cdd:cd01093     1 PEISSPTNFKHRVHVGFDPQTGEFTGLPEEWQRLLKSSGITKEEQK 46
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
70-105 5.91e-14

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 65.69  E-value: 5.91e-14
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1024249297   70 ISLPSDFEHTIHVGFDAVTGEFTGIPEQWARLLQTS 105
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTGGFTGLPTEWKSLLKTS 36
 
Name Accession Description Interval E-value
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
248-544 0e+00

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: 608.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 248 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 327
Cdd:cd06656     1 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 328 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 407
Cdd:cd06656    81 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 408 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 487
Cdd:cd06656   161 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 488 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR 544
Cdd:cd06656   241 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNSSR 297
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
247-542 0e+00

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: 588.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 247 TDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIV 326
Cdd:cd06654     1 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 327 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 406
Cdd:cd06654    81 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 407 GFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPE 486
Cdd:cd06654   161 GFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 487 RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNS 542
Cdd:cd06654   241 KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNN 296
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
260-520 0e+00

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: 579.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 260 SVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 339
Cdd:cd06647     1 SVGDPKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 419
Cdd:cd06647    81 VVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRC 499
Cdd:cd06647   161 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRC 240
                         250       260
                  ....*....|....*....|.
gi 1024249297 500 LEMDVDRRGSAKELLQHPFLK 520
Cdd:cd06647   241 LEMDVEKRGSAKELLQHPFLK 261
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
248-542 0e+00

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: 561.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 248 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 327
Cdd:cd06655     1 DEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 328 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 407
Cdd:cd06655    81 FLDSFLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 408 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 487
Cdd:cd06655   161 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1024249297 488 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIKNS 542
Cdd:cd06655   241 LSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLILAAKEAMKSN 295
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
267-520 6.79e-172

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: 485.95  E-value: 6.79e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQ-NKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTET--CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG 424
Cdd:cd06614    80 GGSLTDIITQNpvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNSVVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDV 504
Cdd:cd06614   160 TPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKNPEKWSPEFKDFLNKCLVKDP 239
                         250
                  ....*....|....*.
gi 1024249297 505 DRRGSAKELLQHPFLK 520
Cdd:cd06614   240 EKRPSAEELLQHPFLK 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
267-519 1.60e-140

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: 406.20  E-value: 1.60e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSkRSTMVG 424
Cdd:cd05122    81 GGSLKDLLKNTNktLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKT-RNTFVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDV 504
Cdd:cd05122   160 TPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPKKWSKEFKDFLKKCLQKDP 239
                         250
                  ....*....|....*
gi 1024249297 505 DRRGSAKELLQHPFL 519
Cdd:cd05122   240 EKRPTAEQLLKHPFI 254
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
260-520 9.51e-135

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: 391.81  E-value: 9.51e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 260 SVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 339
Cdd:cd06648     1 SPGDPRSDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 419
Cdd:cd06648    81 VVMEFLEGGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRC 499
Cdd:cd06648   161 KSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHKVSPRLRSFLDRM 240
                         250       260
                  ....*....|....*....|.
gi 1024249297 500 LEMDVDRRGSAKELLQHPFLK 520
Cdd:cd06648   241 LVRDPAQRATAAELLNHPFLA 261
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
246-532 1.85e-114

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: 341.19  E-value: 1.85e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 246 MTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNI 325
Cdd:cd06659     1 VTHEQFKAALRMVVDQGDPRQLLENYVKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 326 VNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTD 405
Cdd:cd06659    81 VEMYKSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 406 FGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP 485
Cdd:cd06659   161 FGFCAQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNS 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1024249297 486 ERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLI 532
Cdd:cd06659   241 HKASPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLPECLVPLI 287
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
245-532 2.20e-107

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: 323.14  E-value: 2.20e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 245 KMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPN 324
Cdd:cd06658     1 RVSHEQFRAALQLVVSPGDPREYLDSFIKIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 325 IVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLT 404
Cdd:cd06658    81 VVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 405 DFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQN 484
Cdd:cd06658   161 DFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKD 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249297 485 PERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLI 532
Cdd:cd06658   241 SHKVSSVLRGFLDLMLVREPSQRATAQELLQHPFLKLAGPPSCIVPLM 288
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
266-532 2.88e-106

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: 319.19  E-value: 2.88e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEiEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG 424
Cdd:cd06609    81 CGGGSVLDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNTFVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPErLSAVFRDFLNRCLEMDV 504
Cdd:cd06609   161 TPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGNK-FSKPFKDFVELCLNKDP 239
                         250       260
                  ....*....|....*....|....*...
gi 1024249297 505 DRRGSAKELLQHPFLKLAKPLSSLTPLI 532
Cdd:cd06609   240 KERPSAKELLKHKFIKKAKKTSYLTLLI 267
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
247-532 9.08e-105

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: 316.19  E-value: 9.08e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 247 TDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIV 326
Cdd:cd06657     1 SHEQFRAALQMVVDPGDPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 327 NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 406
Cdd:cd06657    81 EMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 407 GFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPE 486
Cdd:cd06657   161 GFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLH 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 487 RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLI 532
Cdd:cd06657   241 KVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPSCIVPLM 286
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
268-519 2.26e-103

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 311.00  E-value: 2.26e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDrERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  347 GGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQsKRSTMVGT 425
Cdd:smart00220  81 GGDLFDLLKKRgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGE-KLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  426 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPE-RLSAVFRDFLNRCLEMDV 504
Cdd:smart00220 160 PEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEwDISPEAKDLIRKLLVKDP 239
                          250
                   ....*....|....*
gi 1024249297  505 DRRGSAKELLQHPFL 519
Cdd:smart00220 240 EKRLTAEEALQHPFF 254
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
267-518 3.54e-103

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: 310.78  E-value: 3.54e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT 425
Cdd:cd06613    81 GGSLQDIYQVTGpLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSFIGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PYWMAPEV--VTRK-AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQNPERLSAVFRDFLNRCL 500
Cdd:cd06613   161 PYWMAPEVaaVERKgGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNfdPPKLKDKEKWSPDFHDFIKKCL 240
                         250
                  ....*....|....*...
gi 1024249297 501 EMDVDRRGSAKELLQHPF 518
Cdd:cd06613   241 TKNPKKRPTATKLLQHPF 258
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
264-519 2.67e-101

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: 306.11  E-value: 2.67e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQqqPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd06612     1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVE--EDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd06612    79 YCGAGSVSDIMKITNktLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLE 501
Cdd:cd06612   159 VIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKWSPEFNDFVKKCLV 238
                         250
                  ....*....|....*...
gi 1024249297 502 MDVDRRGSAKELLQHPFL 519
Cdd:cd06612   239 KDPEERPSAIQLLQHPFI 256
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
267-519 4.42e-94

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: 287.49  E-value: 4.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELeaLEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI----TPEQSKr 419
Cdd:cd06606    81 VPGGSLASLLkKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLaeiaTGEGTK- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 sTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGT-PELqnPERLSAVFRDFLN 497
Cdd:cd06606   160 -SLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIGSSGEpPPI--PEHLSEEAKDFLR 236
                         250       260
                  ....*....|....*....|..
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06606   237 KCLQRDPKKRPTADELLQHPFL 258
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
263-519 1.41e-89

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: 276.49  E-value: 1.41e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKElIINEILVMRENKN-PNIVNYLDSYL------VG 335
Cdd:cd06608     3 DPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEE-IKLEINILRKFSNhPNIATFYGAFIkkdppgGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 DELWVVMEYLAGGSLTDVVTET-----CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA 410
Cdd:cd06608    82 DQLWLVMEYCGGGSVTDLVKGLrkkgkRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 QITPEQSKRSTMVGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP 485
Cdd:cd06608   162 QLDSTLGRRNTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKSP 241
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024249297 486 ERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06608   242 EKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
266-518 1.45e-89

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: 276.16  E-value: 1.45e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKcQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDV----VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI-TPEQSK- 418
Cdd:cd06610    81 LSGGSLLDImkssYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLaTGGDRTr 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 --RSTMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQN---PERLSAVF 492
Cdd:cd06610   161 kvRKTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETgadYKKYSKSF 240
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd06610   241 RKMISLCLQKDPSKRPTAEELLKHKF 266
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
267-519 2.65e-85

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: 264.86  E-value: 2.65e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLksVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd06627    81 VENGSLASIIKKfGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPERLSAVFRDFLNRCLEMD 503
Cdd:cd06627   161 GTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPPL--PENISPELRDFLLQCFQKD 238
                         250
                  ....*....|....*.
gi 1024249297 504 VDRRGSAKELLQHPFL 519
Cdd:cd06627   239 PTLRPSAKELLKHPWL 254
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
274-519 5.29e-84

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: 262.37  E-value: 5.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd06611    13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGALDSI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 V--TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAP 431
Cdd:cd06611    93 MleLERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGTPYWMAP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 432 EVV---TRK--AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDR 506
Cdd:cd06611   173 EVVaceTFKdnPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLDQPSKWSSSFNDFLKSCLVKDPDD 252
                         250
                  ....*....|...
gi 1024249297 507 RGSAKELLQHPFL 519
Cdd:cd06611   253 RPTAAELLKHPFV 265
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
268-532 1.03e-83

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: 261.64  E-value: 1.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQqPKKEL--IINEILVM---RENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDT-DDDDVsdIQKEVALLsqlKLGQPKNIIKYYGSYLKGPSLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd06917    82 DYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRSTF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqNPERLSAVFRDFLNRCLE 501
Cdd:cd06917   162 VGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRL-EGNGYSPLLKEFVAACLD 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1024249297 502 MDVDRRGSAKELLQHPFLKL--AKPLSSLTPLI 532
Cdd:cd06917   241 EEPKDRLSADELLKSKWIKQhsKTPTSVLKELI 273
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
263-532 3.23e-77

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: 244.58  E-value: 3.23e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd06642     1 DPEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEaEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd06642    81 MEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNpeRLSAVFRDFLNRCLE 501
Cdd:cd06642   161 FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEG--QHSKPFKEFVEACLN 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024249297 502 MDVDRRGSAKELLQHPFL-KLAKPLSSLTPLI 532
Cdd:cd06642   239 KDPRFRPTAKELLKHKFItRYTKKTSFLTELI 270
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
263-536 7.31e-76

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: 241.47  E-value: 7.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd06643     2 NPEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS 420
Cdd:cd06643    82 EFCAGGAVDAVMLEleRPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVV-----TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDF 495
Cdd:cd06643   162 SFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSPEFKDF 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1024249297 496 LNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAK 536
Cdd:cd06643   242 LRKCLEKNVDARWTTSQLLQHPFVSVLVSNKPLRELIAEAK 282
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
263-532 9.92e-76

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: 240.72  E-value: 9.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd06640     1 DPEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEaEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd06640    81 MEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNpeRLSAVFRDFLNRCLE 501
Cdd:cd06640   161 FVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTLVG--DFSKPFKEFIDACLN 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024249297 502 MDVDRRGSAKELLQHPFL-KLAKPLSSLTPLI 532
Cdd:cd06640   239 KDPSFRPTAKELLKHKFIvKNAKKTSYLTELI 270
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
266-519 1.70e-75

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: 239.66  E-value: 1.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNL---QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd06607     1 KIFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYsgkQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGgSLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSkrs 420
Cdd:cd06607    81 EYCLG-SASDIveVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCPANS--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 tMVGTPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPErLSAVFRDFLN 497
Cdd:cd06607   157 -FVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLSSGE-WSDDFRNFVD 234
                         250       260
                  ....*....|....*....|..
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06607   235 SCLQKIPQDRPSAEDLLKHPFV 256
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
274-517 6.88e-75

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: 236.40  E-value: 6.88e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 352
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKlLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG--TPYW 428
Cdd:cd00180    81 LLKEnkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGttPPYY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMvegeppylnenplralyliatngtpelqnperlsAVFRDFLNRCLEMDVDRRG 508
Cdd:cd00180   161 APPELLGGRYYGPKVDIWSLGVILYEL----------------------------------EELKDLIRRMLQYDPKKRP 206

                  ....*....
gi 1024249297 509 SAKELLQHP 517
Cdd:cd00180   207 SAKELLEHL 215
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
263-532 6.63e-74

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: 236.12  E-value: 6.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd06641     1 DPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEaEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd06641    81 MEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN* 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNpeRLSAVFRDFLNRCLE 501
Cdd:cd06641   161 FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEG--NYSKPLKEFVEACLN 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024249297 502 MDVDRRGSAKELLQHPF-LKLAKPLSSLTPLI 532
Cdd:cd06641   239 KEPSFRPTAKELLKHKFiLRNAKKTSYLTELI 270
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
267-518 1.38e-70

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: 226.59  E-value: 1.38e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEdeEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFcAQITPEQSKRS 420
Cdd:cd05117    81 CTGGELFDrIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGL-AKIFEEGEKLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNPE--RLSAVFRDFLNR 498
Cdd:cd05117   160 TVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKI-LKGKYSFDSPEwkNVSEEAKDLIKR 238
                         250       260
                  ....*....|....*....|
gi 1024249297 499 CLEMDVDRRGSAKELLQHPF 518
Cdd:cd05117   239 LLVVDPKKRLTAAEALNHPW 258
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
267-519 4.35e-70

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: 225.42  E-value: 4.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEreEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETC-----MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 419
Cdd:cd08215    81 ADGGDLAQKIKKQKkkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPElQNPERLSAVFRDFLNRC 499
Cdd:cd08215   161 KTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANN-LPALVYKIVKGQYP-PIPSQYSSELRDLVNSM 238
                         250       260
                  ....*....|....*....|
gi 1024249297 500 LEMDVDRRGSAKELLQHPFL 519
Cdd:cd08215   239 LQKDPEKRPSANEILSSPFI 258
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
263-539 4.68e-69

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: 224.14  E-value: 4.68e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd06644     9 DPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTEtcMDEG----QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 418
Cdd:cd06644    89 EFCPGGAVDAIMLE--LDRGltepQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 RSTMVGTPYWMAPEVV---TRK--AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFR 493
Cdd:cd06644   167 RDSFIGTPYWMAPEVVmceTMKdtPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQPSKWSMEFR 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAI 539
Cdd:cd06644   247 DFLKTALDKHPETRPSAAQLLEHPFVSSVTSNRPLRELVAEAKAEV 292
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
256-519 5.79e-69

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: 223.73  E-value: 5.79e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 256 RSIV--SVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYL 333
Cdd:cd06638     6 KTIIfdSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKFYGMYY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 334 -----VGDELWVVMEYLAGGSLTDVVTETC-----MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKL 403
Cdd:cd06638    86 kkdvkNGDQLWLVLELCNGGSVTDLVKGFLkrgerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 404 TDFGFCAQITPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG 478
Cdd:cd06638   166 VDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNP 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1024249297 479 TPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06638   246 PPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
263-519 7.20e-69

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: 222.60  E-value: 7.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd06646     6 NPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd06646    86 EYCGGGSLQDIYHVTGpLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRKS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQNPERLSAVFRDFL 496
Cdd:cd06646   166 FIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNfqPPKLKDKTKWSSTFHNFV 245
                         250       260
                  ....*....|....*....|...
gi 1024249297 497 NRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06646   246 KISLTKNPKKRPTAERLLTHLFV 268
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
273-520 2.29e-68

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: 221.31  E-value: 2.29e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQQP-KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd06623     8 VLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEeFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTET-CMDEGQIAAVCRECLQALDFLHSN-QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWM 429
Cdd:cd06623    88 DLLKKVgKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNTFVGTVTYM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 430 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLR--ALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRR 507
Cdd:cd06623   168 SPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSffELMQAICDGPPPSLPAEEFSPEFRDFISACLQKDPKKR 247
                         250
                  ....*....|...
gi 1024249297 508 GSAKELLQHPFLK 520
Cdd:cd06623   248 PSAAELLQHPFIK 260
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
263-540 2.52e-68

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: 222.99  E-value: 2.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNL---QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 339
Cdd:cd06633    18 DPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYsgkQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAW 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGgSLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:cd06633    98 LVMEYCLG-SASDLleVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 krstMVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPErLSAVFRD 494
Cdd:cd06633   177 ----FVGTPYWMAPEVIlamDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLQSNE-WTDSFRG 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIK 540
Cdd:cd06633   252 FVDYCLQKIPQERPSSAELLRHDFVRRERPPRVLIDLIQRTKDAVR 297
Pkinase pfam00069
Protein kinase domain;
268-519 5.73e-68

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 218.65  E-value: 5.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDknILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTE-TCMDEGQIAAVCREclqaldflhsnqvihrdiksdnILLGMDGSVKLTDFgfcaqitpeqskrstmVG 424
Cdd:pfam00069  81 EGGSLFDLLSEkGAFSEREAKFIMKQ----------------------ILEGLESGSSLTTF----------------VG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDV 504
Cdd:pfam00069 123 TPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEAKDLLKKLLKKDP 202
                         250
                  ....*....|....*
gi 1024249297 505 DRRGSAKELLQHPFL 519
Cdd:pfam00069 203 SKRLTATQALQHPWF 217
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
263-519 8.72e-68

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: 219.92  E-value: 8.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd06645     8 NPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd06645    88 EFCGGGSLQDIYHVTGpLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEV--VTRK-AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQNPERLSAVFRDFL 496
Cdd:cd06645   168 FIGTPYWMAPEVaaVERKgGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNfqPPKLKDKMKWSNSFHHFV 247
                         250       260
                  ....*....|....*....|...
gi 1024249297 497 NRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06645   248 KMALTKNPKKRPTAEKLLQHPFV 270
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
258-519 3.71e-66

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: 216.03  E-value: 3.71e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 258 IVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV--- 334
Cdd:cd06636     8 LSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKksp 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 335 ---GDELWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF 408
Cdd:cd06636    88 pghDDQLWLVMEFCGAGSVTDLVKNTkgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 CAQITPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQ 483
Cdd:cd06636   168 SAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPKLK 247
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1024249297 484 NpERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06636   248 S-KKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
267-515 4.16e-66

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: 215.14  E-value: 4.16e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI---INEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRerfLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd14014    81 YVEGGSLADLLRErGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 V-GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN-GTPELQNPERLSAVFRDFLNRCL 500
Cdd:cd14014   161 VlGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEaPPPPSPLNPDVPPALDAIILRAL 240
                         250
                  ....*....|....*.
gi 1024249297 501 EMDVDRR-GSAKELLQ 515
Cdd:cd14014   241 AKDPEERpQSAAELLA 256
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
273-519 1.82e-65

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: 213.70  E-value: 1.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQ--QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd06626     7 KIGEGTFGKVYTAVNLDTGELMAMKEIRFQdnDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVTETCM-DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGfCAQI------TPEQSKRSTMV 423
Cdd:cd06626    87 EELLRHGRIlDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG-SAVKlknnttTMAPGEVNSLV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVT---RKAYGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGTPELQNPERLSAVFRDFLNRC 499
Cdd:cd06626   166 GTPAYMAPEVITgnkGEGHGRAADIWSLGCVVLEMATGKRPWSElDNEWAIMYHVGMGHKPPIPDSLQLSPEGKDFLSRC 245
                         250       260
                  ....*....|....*....|
gi 1024249297 500 LEMDVDRRGSAKELLQHPFL 519
Cdd:cd06626   246 LESDPKKRPTASELLDHPFI 265
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
260-520 2.66e-65

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: 214.09  E-value: 2.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 260 SVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKElIINEILVMRENKN-PNIVN-----YLDSYL 333
Cdd:cd06639    16 SLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEE-IEAEYNILRSLPNhPNVVKfygmfYKADQY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 334 VGDELWVVMEYLAGGSLTDVVTETC-----MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF 408
Cdd:cd06639    95 VGGQLWLVLELCNGGSVTELVKGLLkcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 CAQITPEQSKRSTMVGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQ 483
Cdd:cd06639   175 SAQLTSARLRRNTSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPPPTLL 254
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1024249297 484 NPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd06639   255 NPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
267-515 2.71e-65

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 220.27  E-value: 2.71e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:COG0515     8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpeLAADPEaRERFRREARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-T 421
Cdd:COG0515    88 YVEGESLADLLRRRgPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTgT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN-GTPELQNPERLSAVFRDFLNRCL 500
Cdd:COG0515   168 VVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREpPPPPSELRPDLPPALDAIVLRAL 247
                         250
                  ....*....|....*.
gi 1024249297 501 EMDVDRR-GSAKELLQ 515
Cdd:COG0515   248 AKDPEERyQSAAELAA 263
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
271-520 1.44e-64

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: 210.79  E-value: 1.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FE---KIGQGASGTVYTALDIATGQEVAIKQM---NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14007     2 FEigkPLGKGKFGNVYLAREKKSGFIVALKVIsksQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPeqSKRSTMV 423
Cdd:cd14007    82 APNGELyKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPS--NRRKTFC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPERLSAVFRDFLNRCLEMD 503
Cdd:cd14007   160 GTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQ---NVDIKFPSSVSPEAKDLISKLLQKD 236
                         250
                  ....*....|....*..
gi 1024249297 504 VDRRGSAKELLQHPFLK 520
Cdd:cd14007   237 PSKRLSLEQVLNHPWIK 253
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
274-518 4.97e-64

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: 209.90  E-value: 4.97e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQ---QPKKELII--NEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPintEASKEVKAleCEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpeQSKRS-----TM 422
Cdd:cd06625    88 SVKDEIKAYgALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRL---QTICSstgmkSV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT-PELqnPERLSAVFRDFLNRCLE 501
Cdd:cd06625   165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTnPQL--PPHVSEDARDFLSLIFV 242
                         250
                  ....*....|....*..
gi 1024249297 502 MDVDRRGSAKELLQHPF 518
Cdd:cd06625   243 RNKKQRPSAEELLSHSF 259
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
263-540 9.18e-64

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: 211.06  E-value: 9.18e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNL---QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 339
Cdd:cd06635    22 DPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYsgkQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAW 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGgSLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:cd06635   102 LVMEYCLG-SASDLleVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANS 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 krstMVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPErLSAVFRD 494
Cdd:cd06635   181 ----FVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNE-WSDYFRN 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIK 540
Cdd:cd06635   256 FVDSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVR 301
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
267-519 3.07e-63

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: 207.64  E-value: 3.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK-----ELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd06632     1 RWQKGQLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKsresvKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpEQSKRS 420
Cdd:cd06632    81 LEYVPGGSIHKLLQRyGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVE-AFSFAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRK--AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG-TPELqnPERLSAVFRDFLN 497
Cdd:cd06632   160 SFKGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGeLPPI--PDHLSPDAKDFIR 237
                         250       260
                  ....*....|....*....|..
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06632   238 LCLQRDPEDRPTASQLLEHPFV 259
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
274-518 6.55e-63

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: 206.60  E-value: 6.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNlqqqpKKELI--------INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLR-----KKEIIkrkevehtLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG 424
Cdd:cd05123    76 PGGELFSHLsKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMDV 504
Cdd:cd05123   156 TPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKS---PLKFPEYVSPEAKSLISGLLQKDP 232
                         250
                  ....*....|....*..
gi 1024249297 505 DRR---GSAKELLQHPF 518
Cdd:cd05123   233 TKRlgsGGAEEIKAHPF 249
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
272-518 1.28e-61

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: 203.13  E-value: 1.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd14003     6 KTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEieEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEqSKRSTMVGTPYW 428
Cdd:cd14003    86 LFDyIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGG-SLLKTFCGTPAY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELqnPERLSAVFRDFLNRCLEMDVDRR 507
Cdd:cd14003   165 AAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDN-DSKLFRKILKGKYPI--PSHLSPDARDLIRRMLVVDPSKR 241
                         250
                  ....*....|.
gi 1024249297 508 GSAKELLQHPF 518
Cdd:cd14003   242 ITIEEILNHPW 252
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
268-519 6.34e-61

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: 201.90  E-value: 6.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALdIATGQEVAIKQMNL--------QQQPKKelIINEILVMRENKNPNIVNYLDSYLVGDELW 339
Cdd:cd06631     3 WKKGNVLGKGAYGTVYCGL-TSTGQLIAVKQVELdtsdkekaEKEYEK--LQEEVDLLKTLKHVNIVGYLGTCLEDNVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGfCAQITPEQSK 418
Cdd:cd06631    80 IFMEFVPGGSIASILARfGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFG-CAKRLCINLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 RST-------MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAV 491
Cdd:cd06631   159 SGSqsqllksMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLPDKFSPE 238
                         250       260
                  ....*....|....*....|....*...
gi 1024249297 492 FRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06631   239 ARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
263-540 1.03e-60

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: 202.95  E-value: 1.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNL---QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELW 339
Cdd:cd06634    12 DPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYsgkQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGgSLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:cd06634    92 LVMEYCLG-SASDLleVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPANS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 krstMVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNpERLSAVFRD 494
Cdd:cd06634   171 ----FVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQS-GHWSEYFRN 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTPLIIAAKEAIK 540
Cdd:cd06634   246 FVDSCLQKIPQDRPTSDVLLKHRFLLRERPPTVIMDLIQRTKDAVR 291
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
263-520 2.83e-60

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: 201.10  E-value: 2.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYL------VGD 336
Cdd:cd06637     3 DPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIkknppgMDD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 413
Cdd:cd06637    83 QLWLVMEFCGAGSVTDLIKNTkgnTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 414 PEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNpERL 488
Cdd:cd06637   163 RTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKS-KKW 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024249297 489 SAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd06637   242 SKKFQSFIESCLVKNHSQRPSTEQLMKHPFIR 273
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
267-519 1.26e-59

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: 198.53  E-value: 1.26e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNL------QQQPKKELI---INEILVMRENKNPNIVNYLDSYLVGDE 337
Cdd:cd06628     1 KWIKGALIGSGSFGSVYLGMNASSGELMAVKQVELpsvsaeNKDRKKSMLdalQREIALLRELQHENIVQYLGSSSDANH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI---- 412
Cdd:cd06628    81 LNIFLEYVPGGSVATLLNNyGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLeans 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 --TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPERLSA 490
Cdd:cd06628   161 lsTKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTI--PSNISS 238
                         250       260
                  ....*....|....*....|....*....
gi 1024249297 491 VFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06628   239 EARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
267-519 1.30e-57

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: 192.47  E-value: 1.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14002     2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELrnLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 lAGGSLTDVVT-ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeqskRSTMV 423
Cdd:cd14002    82 -AQGELFQILEdDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMS-----CNTLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 -----GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNR 498
Cdd:cd14002   156 ltsikGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKD---PVKWPSNMSPEFKSFLQG 232
                         250       260
                  ....*....|....*....|.
gi 1024249297 499 CLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14002   233 LLNKDPSKRLSWPDLLEHPFV 253
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
267-519 3.39e-57

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: 191.99  E-value: 3.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ--QPKKELIINEILVMRENKNPNIVNYLDSYLVGDE--LWVVM 342
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKmsEKEKQQLVSEVNILRELKHPNIVRYYDRIVDRANttLYIVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVV-----TETCMDEGQIAAVCRECLQALDFLH-----SNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 412
Cdd:cd08217    81 EYCEGGDLAQLIkkckkENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLARVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPERLSAVF 492
Cdd:cd08217   161 SHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRI--PSRYSSEL 238
                         250       260
                  ....*....|....*....|....*..
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd08217   239 NEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
274-515 1.70e-56

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: 189.29  E-value: 1.70e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTAldIATGQEVAIKQMNLQ--QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd13999     1 IGSGSFGEVYKG--KWRGTDVAIKKLKVEddNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWM 429
Cdd:cd13999    79 DLLHKkkIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPRWM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 430 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPeLQNPERLSAVFRDFLNRCLEMDVDRRGS 509
Cdd:cd13999   159 APEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLR-PPIPPDCPPELSKLIKRCWNEDPEKRPS 237

                  ....*.
gi 1024249297 510 AKELLQ 515
Cdd:cd13999   238 FSEIVK 243
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
274-519 7.06e-56

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: 188.77  E-value: 7.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQM---NLQQ-QPKKEliinEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEIperDSREvQPLHE----EIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTET----CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM-DGSVKLTDFGFCAQITPEQSKRSTMVG 424
Cdd:cd06624    92 LSALLRSKwgplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGINPCTETFTG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPYLNE-NPLRALYLIATNGT-PELqnPERLSAVFRDFLNRCL 500
Cdd:cd06624   172 TLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFIELgEPQAAMFKVGMFKIhPEI--PESLSEEAKSFILRCF 249
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd06624   250 EPDPDKRATASDLLQDPFL 268
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
348-527 2.20e-54

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 181.44  E-value: 2.20e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  348 GSLTDVVT--ETCMDEGQIAAVCRECLQALDFLHSNQvihrdiKSDNILLGMDGSVKLtdFGFCAQITPEQSKrstmvGT 425
Cdd:smart00750   1 VSLADILEvrGRPLNEEEIWAVCLQCLGALRELHRQA------KSGNILLTWDGLLKL--DGSVAFKTPEQSR-----PD 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  426 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPEL-----QNPERLSA--VFRDFLNR 498
Cdd:smart00750  68 PYFMAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERELSAILEILLNGMPADdprdrSNLEGVSAarSFEDFMRL 147
                          170       180
                   ....*....|....*....|....*....
gi 1024249297  499 CLEMDVDRRGSAKELLQHPFLKLAKPLSS 527
Cdd:smart00750 148 CASRLPQRREAANHYLAHCRALFAETLEL 176
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
267-519 1.06e-53

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: 182.97  E-value: 1.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNL------QQQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGD 336
Cdd:cd06629     2 KWVKGELIGKGTYGRVYLAMNATTGEMLAVKQVELpktssdRADSRQKTVVDalksEIDTLKDLDHPNIVQYLGFEETED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcaqitpe 415
Cdd:cd06629    82 YFSIFLEYVPGGSIGSCLrKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGI------- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 qSKRS----------TMVGTPYWMAPEVV--TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPEL 482
Cdd:cd06629   155 -SKKSddiygnngatSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgNKRSAPPV 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1024249297 483 QNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd06629   234 PEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
274-519 2.28e-53

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: 181.98  E-value: 2.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMN-----------LQQQPKK---ELIINEILVMRENKNPNIVN-Y--LDSyLVGD 336
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNksrlrkrregkNDRGKIKnalDDVRREIAIMKKLDHPNIVRlYevIDD-PESD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG---FCA 410
Cdd:cd14008    80 KLYLVLEYCEGGPVMELDSGDrvpPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGvseMFE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 QITPEQSKRstmVGTPYWMAPEV--VTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLrALYLIATNGTPELQNPER 487
Cdd:cd14008   160 DGNDTLQKT---AGTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNIL-ELYEAIQNQNDEFPIPPE 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024249297 488 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14008   236 LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
267-519 1.54e-51

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: 176.65  E-value: 1.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRF-EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVM- 342
Cdd:cd13983     1 RYLKFnEVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERqrFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 -EYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILL-GMDGSVKLTDFGFCAQItpEQS 417
Cdd:cd13983    81 tELMTSGTLKQYLKRfKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFInGNTGEVKIGDLGLATLL--RQS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 KRSTMVGTPYWMAPEVVTRKaYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPelqnPERLSAV----FR 493
Cdd:cd13983   159 FAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIK----PESLSKVkdpeLK 233
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 494 DFLNRCLEmDVDRRGSAKELLQHPFL 519
Cdd:cd13983   234 DFIEKCLK-PPDERPSARELLEHPFF 258
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
268-519 3.99e-51

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: 176.52  E-value: 3.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQpkKELI----INEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNE--EEGIpstaLREISLLKELKHPNIVKLLDVIHTENKLYLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAggslTDV-----VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 418
Cdd:cd07829    79 YCD----QDLkkyldKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLRT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 RSTMVGTPYWMAPEVVTR-KAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI-ATNGTPELQN----------- 484
Cdd:cd07829   155 YTHEVVTLWYRAPEILLGsKHYSTAVDIWSVGcIFA-ELITGKPLFPGDSEIDQLFKIfQILGTPTEESwpgvtklpdyk 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1024249297 485 -------PERLSAVF-------RDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07829   234 ptfpkwpKNDLEKVLprldpegIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
274-520 1.27e-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: 174.71  E-value: 1.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQM--------NLQQQPKKEliiNEILVMreNKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVIkkrdmirkNQVDSVLAE---RNILSQ--AQNPFVVKLYYSFQGKKNLYLVMEYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGG---SLTDVVTetCMDEgQIAAVC-RECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF------------- 408
Cdd:cd05579    76 PGGdlySLLENVG--ALDE-DVARIYiAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLskvglvrrqikls 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 --CAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQNPE 486
Cdd:cd05579   153 iqKKSNGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETP-EEIFQNILNGKIEWPEDP 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1024249297 487 RLSAVFRDFLNRCLEMDVDRR---GSAKELLQHPFLK 520
Cdd:cd05579   232 EVSDEAKDLISKLLTPDPEKRlgaKGIEEIKNHPFFK 268
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
274-522 1.31e-50

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: 174.46  E-value: 1.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE-LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 352
Cdd:cd06605     9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQkQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSLDK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTET-CMDEGQIAAVCRECLQALDFLHSN-QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeQSKRSTMVGTPYWMA 430
Cdd:cd06605    89 ILKEVgRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLV--DSLAKTFVGTRSYMA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 431 PEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN------PLRALYLIATNGTPELQNpERLSAVFRDFLNRCLEMDV 504
Cdd:cd06605   167 PERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNakpsmmIFELLSYIVDEPPPLLPS-GKFSPDFQDFVSQCLQKDP 245
                         250
                  ....*....|....*...
gi 1024249297 505 DRRGSAKELLQHPFLKLA 522
Cdd:cd06605   246 TERPSYKELMEHPFIKRY 263
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
267-519 2.58e-50

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: 174.43  E-value: 2.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd07833     2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEdvKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LaGGSLTDVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT-PEQSKRST 421
Cdd:cd07833    82 V-ERTLLELLEAspGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTaRPASPLTD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEV-VTRKAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI---------------------ATNG 478
Cdd:cd07833   161 YVATRWYRAPELlVGDTNYGKPVDVWAIGcIMA-ELLDGEPLFPGDSDIDQLYLIqkclgplppshqelfssnprfAGVA 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1024249297 479 TPELQNPERLSAVFR--------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07833   240 FPEPSQPESLERRYPgkvsspalDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
272-519 3.99e-49

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: 170.28  E-value: 3.99e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd08529     6 NKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRkmREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAENGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTETC---MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTP 426
Cdd:cd08529    86 LHSLIKSQRgrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQTIVGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 427 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPERLSAVFRDFLNRCLEMDVDR 506
Cdd:cd08529   166 YYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPI--SASYSQDLSQLIDSCLTKDYRQ 243
                         250
                  ....*....|...
gi 1024249297 507 RGSAKELLQHPFL 519
Cdd:cd08529   244 RPDTTELLRNPSL 256
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
268-520 7.49e-49

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: 169.92  E-value: 7.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL------IINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd06630     2 WLKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQeevveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS-VKLTDFGFCAQITPEQSK- 418
Cdd:cd06630    82 VEWMAGGSVASLLSKyGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAAARLASKGTGa 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 ---RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE---NPLRALYLIAT-NGTPELqnPERLSAV 491
Cdd:cd06630   162 gefQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEkisNHLALIFKIASaTTPPPI--PEHLSPG 239
                         250       260
                  ....*....|....*....|....*....
gi 1024249297 492 FRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd06630   240 LRDVTLRCLELQPEDRPPARELLKHPVFT 268
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
274-407 7.75e-49

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: 165.31  E-value: 7.75e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNP--NIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKGLelNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 352 DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 407
Cdd:cd13968    81 AYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
266-519 1.36e-47

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: 166.19  E-value: 1.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd14099     1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKvvpKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd14099    81 ELCSNGSLMELLkRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRK-AYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYL-IATNgtpELQNPERL--SAVFRDFLN 497
Cdd:cd14099   161 LCGTPNYIAPEVLEKKkGHSFEVDIWSLGVILYTLLVGKPPF-ETSDVKETYKrIKKN---EYSFPSHLsiSDEAKDLIR 236
                         250       260
                  ....*....|....*....|..
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14099   237 SMLQPDPTKRPSLDEILSHPFF 258
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
274-518 1.41e-47

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: 165.86  E-value: 1.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKlqENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVV-TETCMDEgqiaAVCRECLQ----ALDFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFcAQITPEQSKRSTMV 423
Cdd:cd14009    81 QYIrKRGRLPE----AVARHFMQqlasGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGF-ARSLQPASMAETLC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPERLSAVFRDFLNRCLEM 502
Cdd:cd14009   156 GSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIeRSDAVIPFPIAAQLSPDCKDLLRRLLRR 235
                         250
                  ....*....|....*.
gi 1024249297 503 DVDRRGSAKELLQHPF 518
Cdd:cd14009   236 DPAERISFEEFFAHPF 251
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
273-519 1.66e-47

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


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 165.89  E-value: 1.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd14081     8 TLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVlmkVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVSGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRSTMVGTPYW 428
Cdd:cd14081    88 LFDyLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGM-ASLQPEGSLLETSCGSPHY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELqnPERLSAVFRDFLNRCLEMDVDRR 507
Cdd:cd14081   167 ACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDN-LRQLLEKVKRGVFHI--PHFISPDAQDLLRRMLEVNPEKR 243
                         250
                  ....*....|..
gi 1024249297 508 GSAKELLQHPFL 519
Cdd:cd14081   244 ITIEEIKKHPWF 255
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
272-518 3.04e-47

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: 165.85  E-value: 3.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd05581     7 KPLGEGSYSTVVLAKEKETGKEYAIKVLDkrhIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAPNG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG----FCA------------- 410
Cdd:cd05581    87 DLLEYIRKyGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvLGPdsspestkgdads 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 QITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGtpELQNPERLSA 490
Cdd:cd05581   167 QIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKI-VKL--EYEFPENFPP 243
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024249297 491 VFRDFLNRCLEMDVDRR------GSAKELLQHPF 518
Cdd:cd05581   244 DAKDLIQKLLVLDPSKRlgvnenGGYDELKAHPF 277
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
268-519 3.49e-47

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: 164.72  E-value: 3.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMnLQQQPKKELIINEILVMRE----NKNPNIVNYLDSYL--VGDELWVV 341
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI-KNDFRHPKAALREIKLLKHlndvEGHPNIVKLLDVFEhrGGNHLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLaGGSLTDVV--TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL-GMDGSVKLTDFGFCAQITPEQSk 418
Cdd:cd05118    80 FELM-GMNLYELIkdYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILInLELGQLKLADFGLARSFTSPPY- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 rSTMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPElqnperlsavFRDFL 496
Cdd:cd05118   158 -TPYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIvRLLGTPE----------ALDLL 226
                         250       260
                  ....*....|....*....|...
gi 1024249297 497 NRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd05118   227 SKMLKYDPAKRITASQALAHPYF 249
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
267-518 4.08e-47

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: 166.01  E-value: 4.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQ-MNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd07847     2 KYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKfVESEDDPViKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd07847    82 CDHTVLNELEKNPrGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDYV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI---------------ATNG------TPE 481
Cdd:cd07847   162 ATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIrktlgdliprhqqifSTNQffkglsIPE 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1024249297 482 LQNPERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07847   242 PETREPLESKFPnisspalSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
274-518 2.04e-46

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: 163.27  E-value: 2.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQ---QQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDE--LWVVMEYLA 346
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGRELAVKQVPFDpdsQETSKEVnaLECEIQLLKNLRHDRIVQYYGCLRDPEEkkLSIFVEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP---EQSKRSTM 422
Cdd:cd06653    90 GGSVKDQLkAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQTicmSGTGIKSV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT-PELqnPERLSAVFRDFLNRcLE 501
Cdd:cd06653   170 TGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTkPQL--PDGVSDACRDFLRQ-IF 246
                         250
                  ....*....|....*..
gi 1024249297 502 MDVDRRGSAKELLQHPF 518
Cdd:cd06653   247 VEEKRRPTAEFLLRHPF 263
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
273-532 3.00e-46

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: 164.39  E-value: 3.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASG--TVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd08216     5 EIGKCFKGggVVHLAKHKPTNTLVAVKKINLESDSKEDLkfLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTETCMD---EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT 425
Cdd:cd08216    85 SCRDLLKTHFPEglpELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRVVHDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 P-------YWMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGTP--------------EL 482
Cdd:cd08216   165 PksseknlPWLSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPF-SDMPATQMLLEKVRGTTpqlldcstypleedSM 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 483 QNPE-------------------RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLS-SLTPLI 532
Cdd:cd08216   244 SQSEdsstehpnnrdtrdipyqrTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQCRRSNtSLLDLL 313
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
271-520 6.45e-46

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: 164.77  E-value: 6.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEK---IGQGASGTVYTALDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05573     3 FEVikvIGRGAFGEVWLVRDKDTGQVYAMKILRksdMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLT------DVVTETcMDEGQIAavcrECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI------ 412
Cdd:cd05573    83 MPGGDLMnllikyDVFPEE-TARFYIA----ELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMnksgdr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 -------------------TPEQSKR----STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLR 469
Cdd:cd05573   158 esylndsvntlfqdnvlarRRPHKQRrvraYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 470 AlYLIATNGTPELQNP--ERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd05573   238 T-YSKIMNWKESLVFPddPDVSPEAIDLIRRLLCDPEDRLGSAEEIKAHPFFK 289
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
267-517 8.87e-46

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: 161.34  E-value: 8.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKcKGKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDG----SVKLTDFGFcAQITPEQSkrS 420
Cdd:cd14095    81 KGGDLFDAITSSTkFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGL-ATEVKEPL--F 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRA-LYLIATNGTPELQNP--ERLSAVFRDFLN 497
Cdd:cd14095   158 TVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQEeLFDLILAGEFEFLSPywDNISDSAKDLIS 237
                         250       260
                  ....*....|....*....|
gi 1024249297 498 RCLEMDVDRRGSAKELLQHP 517
Cdd:cd14095   238 RMLVVDPEKRYSAGQVLDHP 257
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
266-519 1.06e-45

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: 162.06  E-value: 1.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIK-------QMNLQQ-QPKKELIINEILVMRENKN-PNIVNYLDSYLVGD 336
Cdd:cd14181    10 QKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKiievtaeRLSPEQlEEVRSSTLKEIHILRQVSGhPSIITLIDSYESST 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 415
Cdd:cd14181    90 FIFLVFDLMRRGELFDYLTEkVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRStMVGTPYWMAPEVV------TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNPE--R 487
Cdd:cd14181   170 EKLRE-LCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMI-MEGRYQFSSPEwdD 247
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024249297 488 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14181   248 RSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
272-515 1.06e-45

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 161.16  E-value: 1.06e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  272 EKIGQGASGTVY----TALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:smart00219   5 KKLGEGAFGEVYkgklKGKGGKKKVEVAVKTLKEDASEQqIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  347 GGSLTDVVTET----CMDE-----GQIAAvcreclqALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:smart00219  85 GGDLLSYLRKNrpklSLSDllsfaLQIAR-------GMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  418 KRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGTPELqnPERLSAVFRDF 495
Cdd:smart00219 158 YRKRGGKLPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYRLPQ--PPNCPPELYDL 235
                          250       260
                   ....*....|....*....|
gi 1024249297  496 LNRCLEMDVDRRGSAKELLQ 515
Cdd:smart00219 236 MLQCWAEDPEDRPTFSELVE 255
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
273-517 2.71e-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: 2.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNL--QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd08530     7 KLGKGSYGSVYKVKRLSDNQVYALKEVNLgsLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPFGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVV-----TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKrsTMVGT 425
Cdd:cd08530    87 SKLIskrkkKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLAK--TQIGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGT-PELqnPERLSAVFRDFLNRCLEMDV 504
Cdd:cd08530   165 PLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPF-EARTMQELRYKVCRGKfPPI--PPVYSQDLQQIIRSLLQVNP 241
                         250
                  ....*....|...
gi 1024249297 505 DRRGSAKELLQHP 517
Cdd:cd08530   242 KKRPSCDKLLQSP 254
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
267-519 3.02e-45

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: 160.60  E-value: 3.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK--------KELIINEILVMRE-NKNPNIVNYLDSYLVGDE 337
Cdd:cd14093     4 KYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSseneaeelREATRREIEILRQvSGHPNIIELHDVFESPTF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ 416
Cdd:cd14093    84 IFLVFELCRKGELFDYLTEVVtLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 sKRSTMVGTPYWMAPEVVTRK------AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNPE--RL 488
Cdd:cd14093   164 -KLRELCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNI-MEGKYEFGSPEwdDI 241
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 489 SAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14093   242 SDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
266-520 3.29e-45

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: 160.67  E-value: 3.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN------LQQQPKKELIINeilvmRENKNPNIVNYLDSYLvgDE-- 337
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITtdpnpdVQKQILRELEIN-----KSCASPYIVKYYGAFL--DEqd 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 --LWVVMEYLAGGSLTDVVTETCMDEGQIA-----AVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA 410
Cdd:cd06621    74 ssIGIAMEYCEGGSLDSIYKKVKKKGGRIGekvlgKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 QITpeQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN-----PLRALYLIATNGTPELQNP 485
Cdd:cd06621   154 ELV--NSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGepplgPIELLSYIVNMPNPELKDE 231
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1024249297 486 E----RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd06621   232 PengiKWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIK 270
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
274-517 5.19e-45

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: 158.97  E-value: 5.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQqPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD- 352
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRD-KKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL--GMDGSVKLTDFGFCAQITPEQSKRSTMvGTPYWMA 430
Cdd:cd14006    80 LAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLadRPSPQIKIIDFGLARKLNPGEELKEIF-GTPEFVA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 431 PEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQNP--ERLSAVFRDFLNRCLEMDVDRRG 508
Cdd:cd14006   159 PEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDD-QETLANISACRVDFSEEyfSSVSQEAKDFIRKLLVKEPRKRP 237

                  ....*....
gi 1024249297 509 SAKELLQHP 517
Cdd:cd14006   238 TAQEALQHP 246
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
274-518 5.38e-45

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: 159.44  E-value: 5.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQ-QQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGDE--LWVVMEYLA 346
Cdd:cd06652    10 LGQGAFGRVYLCYDADTGRELAVKQVQFDpESPETSKEVNalecEIQLLKNLLHERIVQYYGCLRDPQErtLSIFMEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ---ITPEQSKRSTM 422
Cdd:cd06652    90 GGSIKDQLKSyGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRlqtICLSGTGMKSV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT-PELqnPERLSAVFRDFLNRCLe 501
Cdd:cd06652   170 TGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTnPQL--PAHVSDHCRDFLKRIF- 246
                         250
                  ....*....|....*..
gi 1024249297 502 MDVDRRGSAKELLQHPF 518
Cdd:cd06652   247 VEAKLRPSADELLRHTF 263
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
274-519 5.87e-45

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: 159.34  E-value: 5.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd05578     8 IGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDsvrNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 -----TDVVtetcMDEGQIAA-VCRECLqALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRSTMVG 424
Cdd:cd05578    88 ryhlqQKVK----FSEETVKFyICEIVL-ALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNI-ATKLTDGTLATSTSG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-----ENPLRALYLIATNGTPELQNPErlsavFRDFLNRC 499
Cdd:cd05578   162 TKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIhsrtsIEEIRAKFETASVLYPAGWSEE-----AIDLINKL 236
                         250       260
                  ....*....|....*....|.
gi 1024249297 500 LEMDVDRR-GSAKELLQHPFL 519
Cdd:cd05578   237 LERDPQKRlGDLSDLKNHPYF 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
272-515 7.36e-45

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: 158.87  E-value: 7.36e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  272 EKIGQGASGTVY----TALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:smart00221   5 KKLGEGAFGEVYkgtlKGKGDGKEVEVAVKTLKEDASEQqIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  347 GGSLTDVVTETCMDEGQIAAVCRECLQA---LDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:smart00221  85 GGDLLDYLRKNRPKELSLSDLLSFALQIargMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYKVKGG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  424 GTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGTPELqnPERLSAVFRDFLNRCLE 501
Cdd:smart00221 165 KLPIrWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYRLPK--PPNCPPELYKLMLQCWA 242
                          250
                   ....*....|....
gi 1024249297  502 MDVDRRGSAKELLQ 515
Cdd:smart00221 243 EDPEDRPTFSELVE 256
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
267-520 1.64e-44

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: 159.27  E-value: 1.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIIN-----EILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKDGINftalrEIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGgSLTDVVTETCMD--EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 419
Cdd:cd07841    81 FEFMET-DLEKVIKDKSIVltPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPNRKM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVV-TRKAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI-ATNGTPELQN------------ 484
Cdd:cd07841   160 THQVVTRWYRAPELLfGARHYGVGVDMWSVGcIFA-ELLLRVPFLPGDSDIDQLGKIfEALGTPTEENwpgvtslpdyve 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249297 485 -----PERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd07841   239 fkpfpPTPLKQIFPaasddalDLLQRLLTLNPNKRITARQALEHPYFS 286
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
271-518 2.35e-44

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: 158.51  E-value: 2.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ---QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd05580     6 LKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiikLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEYVPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPeqsKRSTMVGTP 426
Cdd:cd05580    86 GELfSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKD---RTYTLCGTP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 427 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGtpELQNPERLSAVFRDFLNRCLEMDVDR 506
Cdd:cd05580   163 EYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMK-IYEKILEG--KIRFPSFFDPDAKDLIKRLLVVDLTK 239
                         250
                  ....*....|....*..
gi 1024249297 507 R-----GSAKELLQHPF 518
Cdd:cd05580   240 RlgnlkNGVEDIKNHPW 256
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
266-519 6.18e-44

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: 157.17  E-value: 6.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQP--------KKELIINEILVMRENKNPNIVNYLDSYLVGDE 337
Cdd:cd14084     6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTigsrreinKPRNIETEIEILKKLSHPCIIKIEDFFDAEDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS---VKLTDFGFcAQIT 413
Cdd:cd14084    86 YYIVLELMEGGELFDrVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGL-SKIL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 414 PEQSKRSTMVGTPYWMAPEVVT---RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQNPERL 488
Cdd:cd14084   165 GETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKEQILSGkyTFIPKAWKNV 244
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 489 SAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14084   245 SEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
267-518 6.26e-44

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: 156.87  E-value: 6.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVkrkvAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS--VKLTDFGFcAQITPEQSKR 419
Cdd:cd14098    81 EYVEGGDLMDFIMAWgAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGL-AKVIHTGTFL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRK------AYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGT----PELQNpeRLS 489
Cdd:cd14098   160 VTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPF-DGSSQLPVEKRIRKGRytqpPLVDF--NIS 236
                         250       260
                  ....*....|....*....|....*....
gi 1024249297 490 AVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14098   237 EEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
267-519 7.01e-44

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: 157.11  E-value: 7.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLqqqPKKE-----LIINEILVMRENK-NPNIVNYLDSYLVGDELWV 340
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVAL---RKLEggipnQALREIKALQACQgHPYVVKLRDVFPHGTGFVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLaGGSLTDVV--TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSK 418
Cdd:cd07832    78 VFEYM-LSSLSEVLrdEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGL-ARLFSEEDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 R--STMVGTPYWMAPEVV--TRKaYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRAL-YLIATNGTPELQN-------- 484
Cdd:cd07832   156 RlySHQVATRWYRAPELLygSRK-YDEGVDLWAVGcIFA-ELLNGSPLFPGENDIEQLaIVLRTLGTPNEKTwpeltslp 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 485 -----------PERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07832   234 dynkitfpeskGIRLEEIFPdcspeaiDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
265-517 1.36e-43

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: 155.61  E-value: 1.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd14083     2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKAlKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNIL---LGMDGSVKLTDFGFCAqiTPEQSKR 419
Cdd:cd14083    82 LVTGGELFDrIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK--MEDSGVM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENP-------LRALYliatngtpELQNP--ERLSA 490
Cdd:cd14083   160 STACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDsklfaqiLKAEY--------EFDSPywDDISD 231
                         250       260
                  ....*....|....*....|....*..
gi 1024249297 491 VFRDFLNRCLEMDVDRRGSAKELLQHP 517
Cdd:cd14083   232 SAKDFIRHLMEKDPNKRYTCEQALEHP 258
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
268-519 4.68e-43

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: 155.00  E-value: 4.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI-INEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFYSWEECMnLREVKSLRKlNEHPNIVKLKEVFRENDELYFVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGgSLTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGfCAQITPEQSKRSTM 422
Cdd:cd07830    81 EG-NLYQLMKDrkgKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFG-LAREIRSRPPYTDY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQN-PE--RL--------- 488
Cdd:cd07830   159 VSTRWYRAPEILLRsTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKIcSVLGTPTKQDwPEgyKLasklgfrfp 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 489 --------------SAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07830   239 qfaptslhqlipnaSPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
268-521 5.28e-43

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: 154.47  E-value: 5.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQ-QQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGDE--LWV 340
Cdd:cd06651     9 WRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDpESPETSKEVSalecEIQLLKNLQHERIVQYYGCLRDRAEktLTI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ---ITPEQ 416
Cdd:cd06651    89 FMEYMPGGSVKDQLKAyGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRlqtICMSG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT-PELqnPERLSAVFRDF 495
Cdd:cd06651   169 TGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTnPQL--PSHISEHARDF 246
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 496 LnRCLEMDVDRRGSAKELLQHPFLKL 521
Cdd:cd06651   247 L-GCIFVEARHRPSAEELLRHPFAQL 271
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
267-519 3.06e-42

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: 151.81  E-value: 3.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEErqAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETC---MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS-VKLTDFGFcAQITPEQSKRS 420
Cdd:cd08220    81 APGGTLFEYIQQRKgslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGI-SKILSSKSKAY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGT--PElqnPERLSAVFRDFLNR 498
Cdd:cd08220   160 TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAAN-LPALVLKIMRGTfaPI---SDRYSEELRHLILS 235
                         250       260
                  ....*....|....*....|.
gi 1024249297 499 CLEMDVDRRGSAKELLQHPFL 519
Cdd:cd08220   236 MLHLDPNKRPTLSEIMAQPII 256
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
266-519 4.06e-42

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: 151.98  E-value: 4.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDiATGQEVAIKQMNLQ---QQPKKELIiNEI-LVMRENKNPNIVNYLDsYLVGDE---L 338
Cdd:cd14131     1 KPYEILKQLGKGGSSKVYKVLN-PKKKIYALKRVDLEgadEQTLQSYK-NEIeLLKKLKGSDRIIQLYD-YEVTDEddyL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYlagGSlTDVVT------ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGSVKLTDFGFCAQI 412
Cdd:cd14131    78 YMVMEC---GE-IDLATilkkkrPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIAKAI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQS--KRSTMVGTPYWMAPEVVTRKAY----------GPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGT 479
Cdd:cd14131   153 QNDTTsiVRDSQVGTLNYMSPEAIKDTSAsgegkpkskiGRPSDVWSLGCILYQMVYGKTPFQHiTNPIAKLQAIIDPNH 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1024249297 480 ----PELQNPERLsavfrDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14131   233 eiefPDIPNPDLI-----DVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
268-507 9.40e-42

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: 151.12  E-value: 9.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEV-AIKQMNLQQ----QPKKEL------IINEILVMREN-KNPNIVNYLDSYLVG 335
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRKKSNGQTLlALKEINMTNpafgRTEQERdksvgdIISEVNIIKEQlRHPNIVRYYKTFLEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 DELWVVMEYLAGGSLTDVVT---ETCMD--EGQIAAVCRECLQALDFLH-SNQVIHRDIKSDNILLGMDGSVKLTDFGFC 409
Cdd:cd08528    82 DRLYIVMELIEGAPLGEHFSslkEKNEHftEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 410 AQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNPERLS 489
Cdd:cd08528   162 KQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKI-VEAEYEPLPEGMYS 240
                         250
                  ....*....|....*...
gi 1024249297 490 AVFRDFLNRCLEMDVDRR 507
Cdd:cd08528   241 DDITFVIRSCLTPDPEAR 258
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
272-518 1.44e-41

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: 149.75  E-value: 1.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQE-VAIKQMNlqqqpKKEL-------IINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREvVAVKCVS-----KSSLnkastenLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVV-TETCMDEGqiaaVCRECLQ----ALDFLHSNQVIHRDIKSDNILL--GMDGSVKLTDFGFCAQITPEQ 416
Cdd:cd14121    76 YCSGGDLSRFIrSRRTLPES----TVRRFLQqlasALQFLREHNISHMDLKPQNLLLssRYNPVLKLADFGFAQHLKPND 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRStMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY----LNENPLRalylIATNGTPELQNPERLSAVF 492
Cdd:cd14121   152 EAHS-LRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFasrsFEELEEK----IRSSKPIEIPTRPELSADC 226
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14121   227 RDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
268-518 1.66e-41

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: 150.14  E-value: 1.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKkelIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14010     2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRPE---VLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG---------------FCAQ 411
Cdd:cd14010    79 GDLETLLRQdGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGlarregeilkelfgqFSDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 412 ITPEQ-SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP--ERL 488
Cdd:cd14010   159 GNVNKvSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKvsSKP 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 1024249297 489 SAVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14010   239 SPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
268-527 4.16e-41

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: 149.71  E-value: 4.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQM-NLQQQPKKELiinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIdKSKRDPSEEI---EIL-LRYGQHPNIITLRDVYDDGNSVYLVTELLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDG----SVKLTDFGFCAQITPEQSkrst 421
Cdd:cd14091    78 GGELLDrILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESgdpeSLRICDFGFAKQLRAENG---- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTP-Y---WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN---ENPLRALYLIaTNGTPELQNP--ERLSAVF 492
Cdd:cd14091   154 LLMTPcYtanFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASgpnDTPEVILARI-GSGKIDLSGGnwDHVSDSA 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSS 527
Cdd:cd14091   233 KDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQ 267
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
266-520 5.13e-41

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: 149.49  E-value: 5.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHqkLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFCAQITPEQSKR 419
Cdd:cd14086    81 LVTGGELfEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASkskGAAVKLADFGLAIEVQGDQQAW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNPE--RLSAVFRDFLN 497
Cdd:cd14086   161 FGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHR-LYAQIKAGAYDYPSPEwdTVTPEAKDLIN 239
                         250       260
                  ....*....|....*....|...
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd14086   240 QMLTVNPAKRITAAEALKHPWIC 262
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
274-515 6.40e-41

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: 148.64  E-value: 6.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGD----ELWVVMEYlAGG 348
Cdd:cd13985     8 LGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRlCGHPNIVQYYDSAILSSegrkEVLLLMEY-CPG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTETC---MDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS--- 420
Cdd:cd13985    87 SLVDILEKSPpspLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHYPLERAEevn 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 ------TMVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALyliatNGTPELQNPERLSAV 491
Cdd:cd13985   167 iieeeiQKNTTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIV-----AGKYSIPEQPRYSPE 241
                         250       260
                  ....*....|....*....|....
gi 1024249297 492 FRDFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd13985   242 LHDLIRHMLTPDPAERPDIFQVIN 265
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
272-523 2.36e-40

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: 147.57  E-value: 2.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQM--NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEylaggs 349
Cdd:cd06617     7 EELGRGAYGVVDKMRHVPTGTIMAVKRIraTVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICME------ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 ltdvVTETCMD--------------EGQIAAVCRECLQALDFLHSN-QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP 414
Cdd:cd06617    81 ----VMDTSLDkfykkvydkgltipEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYwMAPEVV----TRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGTPELQNpERLS 489
Cdd:cd06617   157 SVAKTIDAGCKPY-MAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPYDSwKTPFQQLKQVVEEPSPQLPA-EKFS 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024249297 490 AVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAK 523
Cdd:cd06617   235 PEFQDFVNKCLKKNYKERPNYPELLQHPFFELHL 268
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
268-518 3.82e-40

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: 147.33  E-value: 3.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQqpKKE----LIINEILVMRENKNPNIVNYLD------SYLVGDE 337
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN--EKEgfpiTAIREIKLLQKLDHPNVVRLKEivtskgSAKYKGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEY----LAGgsLTDVvTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 413
Cdd:cd07840    79 IYMVFEYmdhdLTG--LLDN-PEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 414 PEQSKRST-MVGTPYWMAPEVV---TRkaYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA-TNGTP-------- 480
Cdd:cd07840   156 KENNADYTnRVITLWYRPPELLlgaTR--YGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFeLCGSPteenwpgv 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 481 -------ELQNPERLSAVFRDFLNRC------------LEMDVDRRGSAKELLQHPF 518
Cdd:cd07840   234 sdlpwfeNLKPKKPYKRRLREVFKNVidpsaldlldklLTLDPKKRISADQALQHEY 290
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
272-516 5.16e-40

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: 146.14  E-value: 5.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTAL---DIATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd00192     1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDaSESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSL----------TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:cd00192    81 GDLldflrksrpvFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 KRSTMvGTP---YWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIaTNGTpELQNPERLSAVFR 493
Cdd:cd00192   161 YRKKT-GGKlpiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYL-RKGY-RLPKPENCPDELY 237
                         250       260
                  ....*....|....*....|...
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQH 516
Cdd:cd00192   238 ELMLSCWQLDPEDRPTFSELVER 260
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
265-519 6.56e-40

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


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 145.60  E-value: 6.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNlqqqpKKEL------IINEILVMRENKNPNIVNYLDSYLVGDEL 338
Cdd:cd14078     2 LKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMD-----KKALgddlprVKTEIEALKNLSHQHICRLYHVIETDNKI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQitPEQS 417
Cdd:cd14078    77 FMVLEYCPGGELFDyIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAK--PKGG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 KRS---TMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGtpELQNPERLSAVFR 493
Cdd:cd14078   155 MDHhleTCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDN-VMALYRKIQSG--KYEEPEWLSPSSK 231
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14078   232 LLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
265-519 9.53e-40

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: 145.56  E-value: 9.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlqqqPKKEL------IINEILVMRENKNPNIVNYLDSYLVGDEL 338
Cdd:cd14167     2 RDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCI-----AKKALegketsIENEIAVLHKIKHPNIVALDDIYESGGHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGGSLTDVVTETCM-DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNIL---LGMDGSVKLTDFGFcAQITP 414
Cdd:cd14167    77 YLIMQLVSGGELFDRIVEKGFyTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL-SKIEG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNP--ERLSAVF 492
Cdd:cd14167   156 SGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAK-LFEQILKAEYEFDSPywDDISDSA 234
                         250       260
                  ....*....|....*....|....*..
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14167   235 KDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
274-519 1.02e-39

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: 145.17  E-value: 1.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14069     9 LGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGdcPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGELF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR--STMVGTPYW 428
Cdd:cd14069    89 DKIEPDVgMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKERllNKMCGTLPY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP-ERLSAVFRDFLNRCLEMDVDR 506
Cdd:cd14069   169 VAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENKKTYLTPwKKIDTAALSLLRKILTENPNK 248
                         250
                  ....*....|...
gi 1024249297 507 RGSAKELLQHPFL 519
Cdd:cd14069   249 RITIEDIKKHPWY 261
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
272-516 1.51e-39

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: 144.56  E-value: 1.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVY----TALDIATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:pfam07714   5 EKLGEGAFGEVYkgtlKGEGENTKIKVAVKTLKEGaDEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG 424
Cdd:pfam07714  85 GGDLLDFLRKhkRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRKRGGG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 -TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNG---TPELqNPERLsavfRDFLNR 498
Cdd:pfam07714 165 kLPIkWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEDGYrlpQPEN-CPDEL----YDLMKQ 239
                         250
                  ....*....|....*...
gi 1024249297 499 CLEMDVDRRGSAKELLQH 516
Cdd:pfam07714 240 CWAYDPEDRPTFSELVED 257
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
267-518 1.74e-39

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: 144.47  E-value: 1.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREgmvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAqiTPEQSKRSTM 422
Cdd:cd14663    81 LVTGGELFSkIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSA--LSEQFRQDGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 V----GTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELqnPERLSAVFRDFLN 497
Cdd:cd14663   159 LhttcGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDEN-LMALYRKIMKGEFEY--PRWFSPGAKSLIK 235
                         250       260
                  ....*....|....*....|.
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14663   236 RILDPNPSTRITVEQIMASPW 256
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
266-520 2.74e-39

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 144.67  E-value: 2.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNL---------QQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVG 335
Cdd:cd14182     3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDItgggsfspeEVQELREATLKEIDILRKvSGHPNIIQLKDTYETN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 DELWVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP 414
Cdd:cd14182    83 TFFFLVFDLMKKGELFDYLTEkVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQsKRSTMVGTPYWMAPEVV------TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNPE-- 486
Cdd:cd14182   163 GE-KLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMI-MSGNYQFGSPEwd 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024249297 487 RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd14182   241 DRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
267-518 2.84e-39

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: 144.87  E-value: 2.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd07846     2 KYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKmvKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDV-VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd07846    82 VDHTVLDDLeKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI---------------------ATNGTPE 481
Cdd:cd07846   162 ATRWYRAPElLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIikclgnliprhqelfqknplfAGVRLPE 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1024249297 482 LQNPE-------RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07846   242 VKEVEplerrypKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
271-520 4.03e-39

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: 145.45  E-value: 4.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FE---KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIIN-----EILVmrENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd05599     3 FEplkVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHvraerDILA--EADNPWVVKLYYSFQDEENLYLIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLT------DVVTEtcmDEGQ--IAavcrECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP 414
Cdd:cd05599    81 EFLPGGDMMtllmkkDTLTE---EETRfyIA----ETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTmVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAlYLIATNGTPELQNPE--RLSAVF 492
Cdd:cd05599   154 SHLAYST-VGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQET-CRKIMNWRETLVFPPevPISPEA 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 493 RDFLNRCLeMDVDRR---GSAKELLQHPFLK 520
Cdd:cd05599   232 KDLIERLL-CDAEHRlgaNGVEEIKSHPFFK 261
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
274-519 4.05e-39

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


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 143.14  E-value: 4.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 VTETCMDEGQIAAV--CRECLQALDFLHSNQVIHRDIKSDNIL-LGMDGS-VKLTDFGFCAQITPEQSKRsTMVGTPYWM 429
Cdd:cd14103    81 VVDDDFELTERDCIlfMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLK-VLFGTPEFV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 430 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNP--ERLSAVFRDFLNRCLEMDVDRR 507
Cdd:cd14103   160 APEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANV-TRAKWDFDDEafDDISDEAKDFISKLLVKDPRKR 238
                         250
                  ....*....|..
gi 1024249297 508 GSAKELLQHPFL 519
Cdd:cd14103   239 MSAAQCLQHPWL 250
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
267-519 4.74e-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: 4.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQmnLQQQPKKELIINE-ILVMRENK------NPNIVNYLDSYLVGDELW 339
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKV--LKEISVGELQPDEtVDANREAKllskldHPAIVKFHDSFVEKESFC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGGSLTDVVTE-----TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGSVKLTDFGFCAQITP 414
Cdd:cd08222    79 IVTEYCEGGDLDDKISEykksgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILMG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELqnPERLSAVFRD 494
Cdd:cd08222   158 TSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSL--PDKYSKELNA 235
                         250       260
                  ....*....|....*....|....*
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd08222   236 IYSRMLNKDPALRPSAAEILKIPFI 260
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
266-518 5.74e-39

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: 143.25  E-value: 5.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE-LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM--DG--SVKLTDFGFCAQItpeQSKR 419
Cdd:cd14184    81 VKGGDLFDAITSsTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEypDGtkSLKLGDFGLATVV---EGPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRA-LYLIATNGTPELQNP--ERLSAVFRDFL 496
Cdd:cd14184   158 YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEdLFDQILLGKLEFPSPywDNITDSAKELI 237
                         250       260
                  ....*....|....*....|..
gi 1024249297 497 NRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14184   238 SHMLQVNVEARYTAEQILSHPW 259
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
268-519 7.79e-39

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: 143.57  E-value: 7.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQ--QQPKKELIINEILVMRENKN---PNIVNYLDSYLVGD-----E 337
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPlsEEGIPLSTIREIALLKQLESfehPNVVRLLDVCHGPRtdrelK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEY----LAGgsLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQIT 413
Cdd:cd07838    81 LTLVFEHvdqdLAT--YLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGL-ARIY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 414 PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPERLSAV 491
Cdd:cd07838   158 SFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGcIFA-ELFNRRPLFRGSSEADQLGKIfDVIGLPSEEEWPRNSAL 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 492 FR-----------------------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07838   237 PRssfpsytprpfksfvpeideeglDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
268-519 1.09e-38

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: 143.35  E-value: 1.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDI-ATGQEVAIK--------QMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDEL 338
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAVPLrNTGKPVAIKvvrkadlsSDNLKGSSRAN-ILKEVQIMKRLSHPNIVKLLDFQESDEYY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL---------------------- 395
Cdd:cd14096    82 YIVLELADGGEIFHqIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkadddetkv 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 396 -----------GMDGSVKLTDFGFCAQITPEQSKrsTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN 464
Cdd:cd14096   162 degefipgvggGGIGIVKLADFGLSKQVWDSNTK--TPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYD 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 465 ENpLRALYLIATNGTPELQNP--ERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14096   240 ES-IETLTEKISRGDYTFLSPwwDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
265-519 1.67e-38

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: 142.82  E-value: 1.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14166     2 RETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNIL-LGMDGSVKL--TDFGFCAQitPEQSKRS 420
Cdd:cd14166    82 VSGGELFDRILERgVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLyLTPDENSKImiTDFGLSKM--EQNGIMS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNP--ERLSAVFRDFLNR 498
Cdd:cd14166   160 TACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESR-LFEKIKEGYYEFESPfwDDISESAKDFIRH 238
                         250       260
                  ....*....|....*....|.
gi 1024249297 499 CLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14166   239 LLEKNPSKRYTCEKALSHPWI 259
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
273-515 1.90e-38

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: 141.64  E-value: 1.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd08224     7 KIGKGQFSVVYRARCLLDGRLVALKKVQifeMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTE-----TCMDEGQI----AAVCReclqALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS 420
Cdd:cd08224    87 LSRLIKHfkkqkRLIPERTIwkyfVQLCS----ALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTTAAH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN-PLRALYLIATNGTPELQNPERLSAVFRDFLNRC 499
Cdd:cd08224   163 SLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKmNLYSLCKKIEKCEYPPLPADLYSQELRDLVAAC 242
                         250
                  ....*....|....*.
gi 1024249297 500 LEMDVDRRGSAKELLQ 515
Cdd:cd08224   243 IQPDPEKRPDISYVLD 258
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
273-524 1.99e-38

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: 142.58  E-value: 1.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLV-GDELWVVMEYLAGGSL 350
Cdd:cd06620    12 DLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSvRKQILRELQILHECHSPYIVSFYGAFLNeNNNIIICMEYMDCGSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 -------TDVVTETCmdeGQIA-AVcrecLQALDFLHS-NQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeQSKRST 421
Cdd:cd06620    92 dkilkkkGPFPEEVL---GKIAvAV----LEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELI--NSIADT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYL-----------IATNGTPELQNPERLSA 490
Cdd:cd06620   163 FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNgpmgildllqrIVNEPPPRLPKDRIFPK 242
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1024249297 491 VFRDFLNRCLEMDVDRRGSAKELLQH-PFLKLAKP 524
Cdd:cd06620   243 DLRDFVDRCLLKDPRERPSPQLLLDHdPFIQAVRA 277
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
274-520 2.46e-38

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: 143.12  E-value: 2.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELII---------NEILVMR-ENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVL------KKEVIIedddvectmTEKRVLAlANRHPFLTGLHACFQTEDRLYFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd05570    77 YVNGGDLMfHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY------------LNENPlraLYliatngtpelqnPERLSA 490
Cdd:cd05570   157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFegddedelfeaiLNDEV---LY------------PRWLSR 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1024249297 491 VFRDFLNRCLEMDVDRR-----GSAKELLQHPFLK 520
Cdd:cd05570   222 EAVSILKGLLTKDPARRlgcgpKGEADIKAHPFFR 256
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
274-518 6.13e-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: 140.08  E-value: 6.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 352
Cdd:cd14185     8 IGDGNFAVVKECRHWNENQEYAMKIIDKSKlKGKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL--GMDGS--VKLTDFGFCAQITpeqSKRSTMVGTPY 427
Cdd:cd14185    88 AIIESVkFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhNPDKSttLKLADFGLAKYVT---GPIFTVCGTPT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGTPELQNP--ERLSAVFRDFLNRCLEMDV 504
Cdd:cd14185   165 YVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQLGHYEFLPPywDNISEAAKDLISRLLVVDP 244
                         250
                  ....*....|....
gi 1024249297 505 DRRGSAKELLQHPF 518
Cdd:cd14185   245 EKRYTAKQVLQHPW 258
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
267-519 9.76e-38

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: 139.71  E-value: 9.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQP--KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPvkEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSV-KLTDFGFCAQITPEQSKRS 420
Cdd:cd08225    81 CDGGDLMKRINRqrgVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGTPELQNPErLSAVFRDFLNRCL 500
Cdd:cd08225   161 TCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPF-EGNNLHQLVLKICQGYFAPISPN-FSRDLRSLISQLF 238
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd08225   239 KVSPRDRPSITSILKRPFL 257
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
267-515 1.29e-37

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: 139.19  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLqkLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPeQSKRSTMV 423
Cdd:cd14072    81 ASGGEVFDyLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTP-GNKLDTFC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-------LNENPLRALYLIatngtpelqnPERLSAVFRDF 495
Cdd:cd14072   160 GSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFdgqnlkeLRERVLRGKYRI----------PFYMSTDCENL 229
                         250       260
                  ....*....|....*....|
gi 1024249297 496 LNRCLEMDVDRRGSAKELLQ 515
Cdd:cd14072   230 LKKFLVLNPSKRGTLEQIMK 249
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
321-520 1.63e-37

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: 141.00  E-value: 1.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 321 KNPNIVNYLDSYLVGDELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDG 399
Cdd:cd05584    58 KHPFIVDLHYAFQTGGKLYLILEYLSGGELfMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQG 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 400 SVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgt 479
Cdd:cd05584   138 HVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKG-- 215
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 480 pELQNPERLSAVFRDFLNRCLEMDVDRR-----GSAKELLQHPFLK 520
Cdd:cd05584   216 -KLNLPPYLTNEARDLLKKLLKRNVSSRlgsgpGDAEEIKAHPFFR 260
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
265-519 2.28e-37

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: 138.99  E-value: 2.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALDIATGQ-EVAIKQMNLQQQPKKE-LIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd14202     1 KFEFSRKDLIGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQtLLGKEIKILKELKHENIVALYDFQEIANSVYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS---------VKLTDFGFcAQI 412
Cdd:cd14202    81 EYCNGGDLADYLhTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGrksnpnnirIKIADFGF-ARY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENP--LRALYLIATNGTPELqnPERLSA 490
Cdd:cd14202   160 LQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPqdLRLFYEKNKSLSPNI--PRETSS 237
                         250       260
                  ....*....|....*....|....*....
gi 1024249297 491 VFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14202   238 HLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
270-520 2.32e-37

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: 139.82  E-value: 2.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RFEKIGQGASGTVYTALDIATGQEVAIKQM--NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAg 347
Cdd:cd06618    19 NLGEIGSGTCGQVYKMRHKKTGHVMAVKQMrrSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDVFICMELMS- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 gsltdvvteTCMD-----------EGQIAAVCRECLQALDFLHSNQ-VIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 415
Cdd:cd06618    98 ---------TCLDkllkriqgpipEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGNVKLCDFGISGRLVDS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKrSTMVGTPYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMVEGEPPY-LNENPLRALYLIATNGTPELQNPERLSAV 491
Cdd:cd06618   169 KAK-TRSAGCAAYMAPERIDPPdnpKYDIRADVWSLGISLVELATGQFPYrNCKTEFEVLTKILNEEPPSLPPNEGFSPD 247
                         250       260
                  ....*....|....*....|....*....
gi 1024249297 492 FRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd06618   248 FCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
267-519 2.79e-37

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: 138.29  E-value: 2.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIIN--------------EILVM---RENKNPNIVNYL 329
Cdd:cd14004     1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFI------FKERILVdtwvrdrklgtvplEIHILdtlNKRSHPNIVKLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 330 DSYLVGDELWVVMEYLAGG-SLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 407
Cdd:cd14004    75 DFFEDDEFYYLVMEKHGSGmDLFDFIeRKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 408 FCAQItpEQSKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNenplralylIATNGTPELQNPE 486
Cdd:cd14004   155 SAAYI--KSGPFDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYN---------IEEILEADLRIPY 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1024249297 487 RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14004   224 AVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
272-518 3.79e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 139.95  E-value: 3.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQ---QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:PTZ00263   24 ETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREilkMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTETCMDEGQIAAV-CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeqSKRSTMVGTPY 427
Cdd:PTZ00263  104 ELFTHLRKAGRFPNDVAKFyHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP---DRTFTLCGTPE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMDVDRR 507
Cdd:PTZ00263  181 YLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAG---RLKFPNWFDGRARDLVKGLLQTDHTKR 257
                         250
                  ....*....|....*.
gi 1024249297 508 -GSAK----ELLQHPF 518
Cdd:PTZ00263  258 lGTLKggvaDVKNHPY 273
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
274-518 4.11e-37

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: 138.13  E-value: 4.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQM------NLQQQpkkELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVkkrhivQTRQQ---EHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTET-CMDEGQ----IAAVcrecLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQsKRSTM 422
Cdd:cd05572    78 GELWTILRDRgLFDEYTarfyTACV----VLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGR-KTWTF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY--LNENPLRaLYLIATNGTPELQNPERLSAVFRDFLNRCL 500
Cdd:cd05572   153 CGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFggDDEDPMK-IYNIILKGIDKIEFPKYIDKNAKNLIKQLL 231
                         250       260
                  ....*....|....*....|...
gi 1024249297 501 EMDVDRR-----GSAKELLQHPF 518
Cdd:cd05572   232 RRNPEERlgylkGGIRDIKKHKW 254
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
272-520 4.57e-37

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: 138.83  E-value: 4.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd06622     7 DELGKGNYGSVYKVLHRPTGVTMAMKEIRLElDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVTETC----MDEGQIAAVCRECLQALDFL-HSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKrsTMVGT 425
Cdd:cd06622    87 DKLYAGGVategIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVASLAK--TNIGC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PYWMAPEVVT------RKAYGPKVDIWSLGIMAIEMVEGEPPYLNE---NPLRALYLIATNGTPELqnPERLSAVFRDFL 496
Cdd:cd06622   165 QSYMAPERIKsggpnqNPTYTVQSDVWSLGLSILEMALGRYPYPPEtyaNIFAQLSAIVDGDPPTL--PSGYSDDAQDFV 242
                         250       260
                  ....*....|....*....|....
gi 1024249297 497 NRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd06622   243 AKCLNKIPNRRPTYAQLLEHPWLV 266
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
272-519 6.81e-37

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: 137.40  E-value: 6.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQ----QPKKELIINEILvmreNKNP-----NIVNYLDSYLVGDELWVVM 342
Cdd:cd14133     5 EVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKdyldQSLDEIRLLELL----NKKDkadkyHIVRLKDVFYFKNHLCIVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLaGGSLTDVVTETC---MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL-GMDGS-VKLTDFGFCAQITPEqs 417
Cdd:cd14133    81 ELL-SQNLYEFLKQNKfqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLaSYSRCqIKIIDFGSSCFLTQR-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 kRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAL-YLIATNGTPelqnPERL-------S 489
Cdd:cd14133   158 -LYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLaRIIGTIGIP----PAHMldqgkadD 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 1024249297 490 AVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14133   233 ELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
274-520 8.09e-37

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: 137.23  E-value: 8.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd05611     4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNvkaeRAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRSTMVGTPYW 428
Cdd:cd05611    84 CASLIkTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGL-SRNGLEKRHNKKFVGTPDY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN--GTPELQNpERLSAVFRDFLNRCLEMDVDR 506
Cdd:cd05611   163 LAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRriNWPEEVK-EFCSPEAVDLINRLLCMDPAK 241
                         250
                  ....*....|....*..
gi 1024249297 507 RGSAK---ELLQHPFLK 520
Cdd:cd05611   242 RLGANgyqEIKSHPFFK 258
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
274-518 2.48e-36

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: 135.57  E-value: 2.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIA-TGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKsQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDG---------SVKLTDFGFcAQITPEQSKRST 421
Cdd:cd14120    81 DYLQAkGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGF-ARFLQDGMMAAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENP--LRALYLIATNGTPELqnPERLSAVFRDFLNRC 499
Cdd:cd14120   160 LCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPqeLKAFYEKNANLRPNI--PSGTSPALKDLLLGL 237
                         250
                  ....*....|....*....
gi 1024249297 500 LEMDVDRRGSAKELLQHPF 518
Cdd:cd14120   238 LKRNPKDRIDFEDFFSHPF 256
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
268-520 3.07e-36

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: 136.38  E-value: 3.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14209     3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLkqvEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpeQSKRSTMV 423
Cdd:cd14209    83 VPGGEMFSHLRRIGrFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV---KGRTWTLC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMD 503
Cdd:cd14209   160 GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG---KVRFPSHFSSDLKDLLRNLLQVD 236
                         250       260
                  ....*....|....*....|..
gi 1024249297 504 VDRR-----GSAKELLQHPFLK 520
Cdd:cd14209   237 LTKRfgnlkNGVNDIKNHKWFA 258
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
268-533 3.12e-36

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: 136.41  E-value: 3.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ---QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEvirLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpeQSKRSTMV 423
Cdd:cd05612    83 VPGGELfSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKL---RDRTWTLC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLrALYLIATNGtpELQNPERLSAVFRDFLNRCLEMD 503
Cdd:cd05612   160 GTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPF-GIYEKILAG--KLEFPRHLDLYAKDLIKKLLVVD 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1024249297 504 VDRR-GSAK----ELLQHPFLKL----AKPLSSLTPLII 533
Cdd:cd05612   237 RTRRlGNMKngadDVKNHRWFKSvdwdDVPQRKLKPPIV 275
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
270-519 3.74e-36

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: 135.21  E-value: 3.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RFE---KIGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIIN---------EILVMRENKNPNIVNYLDSYLVGDE 337
Cdd:cd14073     2 RYElleTLGKGTYGKVKLAIERATGREVAIKSI------KKDKIEDeqdmvrirrEIEIMSSLNHPHIIRIYEVFENKDK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQ 416
Cdd:cd14073    76 IVIVMEYASGGELYDYISERRrLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGL-SNLYSKD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRdf 495
Cdd:cd14073   155 KLLQTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPSDASGLIR-- 232
                         250       260
                  ....*....|....*....|....
gi 1024249297 496 lnRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14073   233 --WMLTVNPKRRATIEDIANHWWV 254
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
268-519 7.52e-36

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: 134.63  E-value: 7.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTET--CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS--VKLTDFGFCAQITPEQSKRSTmV 423
Cdd:cd14114    84 GELFERIAAEhyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSneVKLIDFGLATHLDPKESVKVT-T 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPERLSAVFRDFLNRCLEM 502
Cdd:cd14114   163 GTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVkSCDWNFDDSAFSGISEEAKDFIRKLLLA 242
                         250
                  ....*....|....*..
gi 1024249297 503 DVDRRGSAKELLQHPFL 519
Cdd:cd14114   243 DPNKRMTIHQALEHPWL 259
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
274-519 8.05e-36

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: 136.29  E-value: 8.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKIL------RKEVIIakdevahtvTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd05595    77 ANGGELFfHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMD 503
Cdd:cd05595   157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILME---EIRFPRTLSPEAKSLLAGLLKKD 233
                         250       260
                  ....*....|....*....|.
gi 1024249297 504 VDRR-----GSAKELLQHPFL 519
Cdd:cd05595   234 PKQRlgggpSDAKEVMEHRFF 254
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
268-529 1.30e-35

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: 134.77  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14175     3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEI--EIL-LRYGQHPNIITLKDVYDDGKHVYLVTELMRG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd14175    80 GELLDkILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYvdesGNPESLRICDFGFAKQLRAENGLLMTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN---ENPLRALYLIATNG-TPELQNPERLSAVFRDFLNR 498
Cdd:cd14175   160 CYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANgpsDTPEEILTRIGSGKfTLSGGNWNTVSDAAKDLVSK 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1024249297 499 CLEMDVDRRGSAKELLQHPFL--KLAKPLSSLT 529
Cdd:cd14175   240 MLHVDPHQRLTAKQVLQHPWItqKDKLPQSQLN 272
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
274-519 1.34e-35

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: 133.97  E-value: 1.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEV--AIKQMN------LQQQPKKELIiNEILVMRENKNPNIVNYLDSYLV-GDELWVVMEY 344
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSGVlyAVKEYRrrddesKRKDYVKRLT-SEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETcmdeGQIAAVCREC-----LQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG--FCAQITPEQS 417
Cdd:cd13994    80 CPGGDLFTLIEKA----DSLSLEEKDCffkqiLRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGtaEVFGMPAEKE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 KRST--MVGTPYWMAPEVVTRKAYGPK-VDIWSLGIMAIEMVEGEPPY---LNENPLRALY---LIATNGTPELQNPERL 488
Cdd:cd13994   156 SPMSagLCGSEPYMAPEVFTSGSYDGRaVDVWSCGIVLFALFTGRFPWrsaKKSDSAYKAYeksGDFTNGPYEPIENLLP 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 489 SAVfRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd13994   236 SEC-RRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
268-519 2.45e-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: 133.86  E-value: 2.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELII-NEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVeNEIAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFCAqiTPEQSKRSTM 422
Cdd:cd14169    85 GGELFDRIIERgSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSK--IEAQGMLSTA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNP--ERLSAVFRDFLNRCL 500
Cdd:cd14169   163 CGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSE-LFNQILKAEYEFDSPywDDISESAKDFIRHLL 241
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd14169   242 ERDPEKRFTCEQALQHPWI 260
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
264-520 2.61e-35

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: 134.17  E-value: 2.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlQQQPK---KELIIneilvMRENKNPNIVNYLDSYLVGDE--- 337
Cdd:cd14137     2 VEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKV--LQDKRyknRELQI-----MRRLKHPNIVKLKYFFYSSGEkkd 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 ---LWVVMEYLAGgSLTDVVTETCMDEGQIAAV---------CReclqALDFLHSNQVIHRDIKSDNILL-GMDGSVKLT 404
Cdd:cd14137    75 evyLNLVMEYMPE-TLYRVIRHYSKNKQTIPIIyvklysyqlFR----GLAYLHSLGICHRDIKPQNLLVdPETGVLKLC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 405 DFGFCAQITP-EQSKrsTMVGTPYWMAPEVVTR-KAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLIA-TNGTP 480
Cdd:cd14137   150 DFGSAKRLVPgEPNV--SYICSRYYRAPELIFGaTDYTTAIDIWSAGcVLA-ELLLGQPLFPGESSVDQLVEIIkVLGTP 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024249297 481 ELQ-----NPER------------LSAVFR--------DFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd14137   227 TREqikamNPNYtefkfpqikphpWEKVFPkrtppdaiDLLSKILVYNPSKRLTALEALAHPFFD 291
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
268-519 2.65e-35

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: 133.08  E-value: 2.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTA--LDIATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLekfLPRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR-- 419
Cdd:cd14080    82 EYAEHGDLLEYIqKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDVls 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMVEGEPPYlNENPLRALYLIATN---GTPElqNPERLSAVFRDF 495
Cdd:cd14080   162 KTFCGSAAYAAPEILQGIPYDPKKyDIWSLGVILYIMLCGSMPF-DDSNIKKMLKDQQNrkvRFPS--SVKKLSPECKDL 238
                         250       260
                  ....*....|....*....|....
gi 1024249297 496 LNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14080   239 IDQLLEPDPTKRATIEEILNHPWL 262
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
272-521 2.75e-35

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 134.03  E-value: 2.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQM--NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEyLAGGS 349
Cdd:cd06616    12 GEIGRGAFGTVNKMLHKPSGTIMAVKRIrsTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICME-LMDIS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDV------VTETCMDEGQIAAVCRECLQALDFLHSN-QVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQSKRSTM 422
Cdd:cd06616    91 LDKFykyvyeVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQL--VDSIAKTR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 -VGT-PYwMAPEVVT----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPL-RALYLIATNGTPELQNPERL--SAVFR 493
Cdd:cd06616   169 dAGCrPY-MAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVfDQLTQVVKGDPPILSNSEERefSPSFV 247
                         250       260
                  ....*....|....*....|....*...
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQHPFLKL 521
Cdd:cd06616   248 NFVNLCLIKDESKRPKYKELLKHPFIKM 275
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
274-519 2.77e-35

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: 132.83  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILvmrenKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVEIQACF-----RHENIAELYGALLWEETVHLFMEAGEGGSVLEK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 VtETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAP 431
Cdd:cd13995    87 L-ESCgpMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF-MSTKAVLVDFGLSVQMTEDVYVPKDLRGTEIYMSP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 432 EVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRA----LYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRR 507
Cdd:cd13995   165 EVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQAPPLEDIAQDCSPAMRELLEAALERNPNHR 244
                         250
                  ....*....|..
gi 1024249297 508 GSAKELLQHPFL 519
Cdd:cd13995   245 SSAAELLKHEAL 256
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
272-519 5.32e-35

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: 133.22  E-value: 5.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14178     9 EDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEI--EIL-LRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 D-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFCAQITPEQSKRSTMVGTP 426
Cdd:cd14178    86 DrILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYmdesGNPESIRICDFGFAKQLRAENGLLMTPCYTA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 427 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN---ENPLRALYLIATnGTPELQ--NPERLSAVFRDFLNRCLE 501
Cdd:cd14178   166 NFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpdDTPEEILARIGS-GKYALSggNWDSISDAAKDIVSKMLH 244
                         250
                  ....*....|....*...
gi 1024249297 502 MDVDRRGSAKELLQHPFL 519
Cdd:cd14178   245 VDPHQRLTAPQVLRHPWI 262
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
274-517 5.44e-35

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: 132.00  E-value: 5.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPK----KELIINEILVMRENKNPNIVNYLDsYLVGDE---LWVVMEYLA 346
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRipngEANVKREIQILRRLNHRNVIKLVD-VLYNEEkqkLYMVMEYCV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GG--SLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP--EQSKRSTM 422
Cdd:cd14119    80 GGlqEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLfaEDDTCTTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAY--GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCL 500
Cdd:cd14119   160 QGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKG---EYTIPDDVDPDLQDLLRGML 236
                         250
                  ....*....|....*..
gi 1024249297 501 EMDVDRRGSAKELLQHP 517
Cdd:cd14119   237 EKDPEKRFTIEQIRQHP 253
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
266-519 8.13e-35

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: 131.58  E-value: 8.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIAT-------GQEVAIKQMNLQQQPKKelIINEI-LVMRENKNPNIVNYLDSYLVGDE 337
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPSR--ILNELeCLERLGGSNNVSGLITAFRNEDQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTEtcMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD-GSVKLTDFGFCAQITPEQ 416
Cdd:cd14019    79 VVAVLPYIEHDDFRDFYRK--MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNREtGKGVLVDFGLAQREEDRP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGE-PPYLNENPLRALYLIAT-NGTPELQnperlsavfr 493
Cdd:cd14019   157 EQRAPRAGTRGFRAPEVLFKcPHQTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATiFGSDEAY---------- 226
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14019   227 DLLDKLLELDPSKRITAEEALKHPFF 252
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
222-519 9.43e-35

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 134.18  E-value: 9.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 222 PPSAENANSSTLYRNTDRQRKKSKMTDEeiLEKLRsivsvgdpkkkytrfeKIGQGASGTVYTALDIATGQEVAIKQM-- 299
Cdd:PLN00034   48 PPPSSSSSSSSSSSASGSAPSAAKSLSE--LERVN----------------RIGSGAGGTVYKVIHRPTGRLYALKVIyg 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 300 NLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDvvtETCMDEGQIAAVCRECLQALDFLH 379
Cdd:PLN00034  110 NHEDTVRRQ-ICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEG---THIADEQFLADVARQILSGIAYLH 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 380 SNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV----TRKAY-GPKVDIWSLGIMAIE 454
Cdd:PLN00034  186 RRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERIntdlNHGAYdGYAGDIWSLGVSILE 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 455 MVEGEPPY-LNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:PLN00034  266 FYLGRFPFgVGRQGDWASLMCAICMSQPPEAPATASREFRHFISCCLQREPAKRWSAMQLLQHPFI 331
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
270-519 1.15e-34

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: 132.67  E-value: 1.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RFE---KIGQGASGTVYTALDIATGQEVAIK----QMNLQQQPKKELiinEIL-VMRENK---NPNIVNYLDSYLVGDEL 338
Cdd:cd14210    14 RYEvlsVLGKGSFGQVVKCLDHKTGQLVAIKiirnKKRFHQQALVEV---KILkHLNDNDpddKHNIVRYKDSFIFRGHL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEyLAGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL--GMDGSVKLTDFG---FCA 410
Cdd:cd14210    91 CIVFE-LLSINLYELLKSNnfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLkqPSKSSIKVIDFGsscFEG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 QITPE--QSKrstmvgtpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN--------------PLRALYLI 474
Cdd:cd14210   170 EKVYTyiQSR--------FYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENeeeqlacimevlgvPPKSLIDK 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 475 AT--------NGTPELQNPER----------LSAV-------FRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14210   242 ASrrkkffdsNGKPRPTTNSKgkkrrpgsksLAQVlkcddpsFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
274-520 1.42e-34

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: 132.82  E-value: 1.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIIN---EILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd05601     9 IGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFfeeERDIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVT--ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM-VGTPY 427
Cdd:cd05601    89 LSLLSryDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTVTSKMpVGTPD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVT------RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPE--RLSAVFRDFLNRC 499
Cdd:cd05601   169 YIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFTEDT-VIKTYSNIMNFKKFLKFPEdpKVSESAVDLIKGL 247
                         250       260
                  ....*....|....*....|.
gi 1024249297 500 LEmDVDRRGSAKELLQHPFLK 520
Cdd:cd05601   248 LT-DAKERLGYEGLCCHPFFS 267
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
272-519 1.54e-34

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: 131.03  E-value: 1.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMN--------LQQQPKKELIIN-EILVMREN------KNPNIVNYLDSYLVGD 336
Cdd:cd14077     7 KTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglkKEREKRLEKEISrDIRTIREAalssllNHPHICRLRDFLRTPN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPE 415
Cdd:cd14077    87 HYYMLFEYVDGGQLLDyIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL-SNLYDP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELqnPERLSAVFRD 494
Cdd:cd14077   166 RRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDEN-MPALHAKIKKGKVEY--PSYLSSECKS 242
                         250       260
                  ....*....|....*....|....*
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14077   243 LISRMLVVDPKKRATLEQVLNHPWM 267
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
268-518 1.80e-34

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: 131.45  E-value: 1.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDaEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GG--SLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd07836    82 KDlkKYMDTHGVRGaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNTFSNEV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVT-RKAYGPKVDIWSLG-IMAiEMVEGEPPYL---NENPLRALYLIAtnGTPELQN-------PE----- 486
Cdd:cd07836   162 VTLWYRAPDVLLgSRTYSTSIDIWSVGcIMA-EMITGRPLFPgtnNEDQLLKIFRIM--GTPTESTwpgisqlPEykptf 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 487 -------------RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07836   239 pryppqdlqqlfpHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
268-519 1.85e-34

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: 130.47  E-value: 1.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNrqkIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRSTMV 423
Cdd:cd14079    84 VSGGELFDyIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGL-SNIMRDGEFLKTSC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELqnPERLSAVFRDFLNRCLEM 502
Cdd:cd14079   163 GSPNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEH-IPNLFKKIKSGIYTI--PSHLSPGARDLIKRMLVV 239
                         250
                  ....*....|....*..
gi 1024249297 503 DVDRRGSAKELLQHPFL 519
Cdd:cd14079   240 DPLKRITIPEIRQHPWF 256
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
267-515 2.41e-34

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: 130.55  E-value: 2.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQM---NLQQQPKKELIIN----EI-LVMRENKNPNIVNYLDSYLVGDEL 338
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksGPNSKDGNDFQKLpqlrEIdLHRRVSRHPNIITLHDVFETEVAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGGSLTDVVTETCMDEGQ---IAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD-GSVKLTDFGFCaqiTP 414
Cdd:cd13993    81 YIVLEYCPNGDLFEAITENRIYVGKtelIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLA---TT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVT-----RKAYGPK-VDIWSLGIMAIEMVEGEPPYLNENPLRALYL-IATNGTPELQNPER 487
Cdd:cd13993   158 EKISMDFGVGSEFYMAPECFDevgrsLKGYPCAaGDIWSLGIILLNLTFGRNPWKIASESDPIFYdYYLNSPNLFDVILP 237
                         250       260
                  ....*....|....*....|....*...
gi 1024249297 488 LSAVFRDFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd13993   238 MSDDFYNLLRQIFTVNPNNRILLPELQL 265
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
267-519 2.45e-34

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 130.32  E-value: 2.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd08218     1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEReeSRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTE---TCMDEGQIAA-VCRECLqALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS 420
Cdd:cd08218    81 CDGGDLYKRINAqrgVLFPEDQILDwFVQLCL-ALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGT-PELqnPERLSAVFRDFLNRC 499
Cdd:cd08218   160 TCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGN-MKNLVLKIIRGSyPPV--PSRYSYDLRSLVSQL 236
                         250       260
                  ....*....|....*....|
gi 1024249297 500 LEMDVDRRGSAKELLQHPFL 519
Cdd:cd08218   237 FKRNPRDRPSINSILEKPFI 256
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
261-520 2.68e-34

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: 130.51  E-value: 2.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 261 VGDpkKKYTRFEKIGQGASGTVYTALD-IATGQEVAIKQMNLQQQPKKELII-NEILVMRENKNPNIVNYLDSYLVGDEL 338
Cdd:cd14201     3 VGD--FEYSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQILLgKEIKILKELQHENIVALYDVQEMPNSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS---------VKLTDFGF 408
Cdd:cd14201    81 FLVMEYCNGGDLADYLqAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRkkssvsgirIKIADFGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 cAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENP--LRALYLIATNGTPELqnPE 486
Cdd:cd14201   161 -ARYLQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPqdLRMFYEKNKNLQPSI--PR 237
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024249297 487 RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd14201   238 ETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
264-520 2.70e-34

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: 131.51  E-value: 2.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNL---QQQP--KKELIINEILVMRENKNPNIVNYLDSYLVGDEL 338
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVakfTSSPglSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGGSLT-DVVTET----CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG-MDGS--VKLTDFGFCA 410
Cdd:cd14094    81 YMVFEFMDGADLCfEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAsKENSapVKLGGFGVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 QITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENplRALYLIATNGTPELQNPE--RL 488
Cdd:cd14094   161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKMNPRQwsHI 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024249297 489 SAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd14094   239 SESAKDLVRRMLMLDPAERITVYEALNHPWIK 270
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
268-520 2.87e-34

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: 131.10  E-value: 2.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14085     5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKL--KKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTETCMDEGQIAAVC-RECLQALDFLHSNQVIHRDIKSDNIL---LGMDGSVKLTDFGFcAQITPEQSKRSTMV 423
Cdd:cd14085    83 GELFDRIVEKGYYSERDAADAvKQILEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGL-SKIVDQQVTMKTVC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP--ERLSAVFRDFLNRCLE 501
Cdd:cd14085   162 GTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRILNCDYDFVSPwwDDVSLNAKDLVKKLIV 241
                         250
                  ....*....|....*....
gi 1024249297 502 MDVDRRGSAKELLQHPFLK 520
Cdd:cd14085   242 LDPKKRLTTQQALQHPWVT 260
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
274-519 3.15e-34

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: 129.86  E-value: 3.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd08221     8 LGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERrdALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTETC---MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 428
Cdd:cd08221    88 DKIAQQKnqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESIVGTPYY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNpERLSAVFRDFLNRCLEMDVDRRG 508
Cdd:cd08221   168 MSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKI-VQGEYEDID-EQYSEEIIQLVHDCLHQDPEDRP 245
                         250
                  ....*....|.
gi 1024249297 509 SAKELLQHPFL 519
Cdd:cd08221   246 TAEELLERPLL 256
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
273-517 3.37e-34

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: 129.66  E-value: 3.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQQ------PKKELIINEILVMR---ENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd14005     7 LLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVtewamiNGPVPVPLEIALLLkasKPGVPGVIRLLDWYERPDGFLLIME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGG-SLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD-GSVKLTDFGfCAQITpEQSKRS 420
Cdd:cd14005    87 RPEPCqDLFDFITERgALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFG-CGALL-KDSVYT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPK-VDIWSLGIMAIEMVEGEPPYLNEnplraLYLIatngTPELQNPERLSAVFRDFLNRC 499
Cdd:cd14005   165 DFDGTRVYSPPEWIRHGRYHGRpATVWSLGILLYDMLCGDIPFEND-----EQIL----RGNVLFRPRLSKECCDLISRC 235
                         250
                  ....*....|....*...
gi 1024249297 500 LEMDVDRRGSAKELLQHP 517
Cdd:cd14005   236 LQFDPSKRPSLEQILSHP 253
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
274-518 4.38e-34

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: 131.29  E-value: 4.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK---ELIINEILVMREN-KNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRnevKHIMAERNVLLKNvKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 L-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 428
Cdd:cd05575    83 LfFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGTPEY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN-----------PLRalylIATNGTPELqnperlsavfRDFLN 497
Cdd:cd05575   163 LAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDtaemydnilhkPLR----LRTNVSPSA----------RDLLE 228
                         250       260
                  ....*....|....*....|....*
gi 1024249297 498 RCLEMDVDRR-GSA---KELLQHPF 518
Cdd:cd05575   229 GLLQKDRTKRlGSGndfLEIKNHSF 253
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
272-519 4.89e-34

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: 129.78  E-value: 4.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQ--QPKKELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd14106    14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRrgQDCRNEILHEIAVLELCKdCPRVVNLHEVYETRSELILILELAAGG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDV-VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG---MDGSVKLTDFGFCAQITPEQSKRStMVG 424
Cdd:cd14106    94 ELQTLlDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTsefPLGDIKLCDFGISRVIGEGEEIRE-ILG 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGtpELQNPERL----SAVFRDFLNRCL 500
Cdd:cd14106   173 TPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDK-QETFLNISQC--NLDFPEELfkdvSPLAIDFIKRLL 249
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd14106   250 VKDPEKRLTAKECLEHPWL 268
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
272-519 9.74e-34

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: 128.88  E-value: 9.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 D-VVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS--VKLTDFGFCAQITPEQsKRSTMVGTPY 427
Cdd:cd14190    90 ErIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGhqVKIIDFGLARRYNPRE-KLKVNFGTPE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAL-YLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDR 506
Cdd:cd14190   169 FLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLnNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERSA 248
                         250
                  ....*....|...
gi 1024249297 507 RGSAKELLQHPFL 519
Cdd:cd14190   249 RMSATQCLKHPWL 261
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
272-519 9.94e-34

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: 129.23  E-value: 9.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd06619     7 EILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVElQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 tDVVTEtcMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeQSKRSTMVGTPYWMA 430
Cdd:cd06619    87 -DVYRK--IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV--NSIAKTYVGTNAYMA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 431 PEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL----NEN---PLRALYLIATNGTPELQNPErLSAVFRDFLNRCLEMD 503
Cdd:cd06619   162 PERISGEQYGIHSDVWSLGISFMELALGRFPYPqiqkNQGslmPLQLLQCIVDEDPPVLPVGQ-FSEKFVHFITQCMRKQ 240
                         250
                  ....*....|....*.
gi 1024249297 504 VDRRGSAKELLQHPFL 519
Cdd:cd06619   241 PKERPAPENLMDHPFI 256
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
266-519 1.01e-33

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: 128.96  E-value: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ-QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14183     6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKcRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL--GMDGS--VKLTDFGFCAQItpeQSKR 419
Cdd:cd14183    86 VKGGDLFDAITSTNkYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyeHQDGSksLKLGDFGLATVV---DGPL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE-NPLRALYLIATNGTPELQNP--ERLSAVFRDFL 496
Cdd:cd14183   163 YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSgDDQEVLFDQILMGQVDFPSPywDNVSDSAKELI 242
                         250       260
                  ....*....|....*....|...
gi 1024249297 497 NRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14183   243 TMMLQVDVDQRYSALQVLEHPWV 265
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
267-519 1.40e-33

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: 128.42  E-value: 1.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIE-TKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFCAQIT--PEQSKRS 420
Cdd:cd14087    81 GGELFDrIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLASTRKkgPNCLMKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TmVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP-ERLSAVFRDFLNRC 499
Cdd:cd14087   161 T-CGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPwPSVSNLAKDFIDRL 239
                         250       260
                  ....*....|....*....|
gi 1024249297 500 LEMDVDRRGSAKELLQHPFL 519
Cdd:cd14087   240 LTVNPGERLSATQALKHPWI 259
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
274-519 1.48e-33

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: 130.59  E-value: 1.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05593    23 LGKGTFGKVILVREKASGKYYAMKIL------KKEVIIakdevahtlTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd05593    97 VNGGELFfHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMD 503
Cdd:cd05593   177 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME---DIKFPRTLSADAKSLLSGLLIKD 253
                         250       260
                  ....*....|....*....|.
gi 1024249297 504 VDRR-----GSAKELLQHPFL 519
Cdd:cd05593   254 PNKRlgggpDDAKEIMRHSFF 274
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
272-515 1.73e-33

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: 128.22  E-value: 1.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd08228     8 KKIGRGQFSEVYRATCLLDRKPVALKKVQifeMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVT-----ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd08228    88 DLSQMIKyfkkqKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE--NPLRALYLIATNGTPELQNpERLSAVFRDFLNRCLE 501
Cdd:cd08228   168 GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkmNLFSLCQKIEQCDYPPLPT-EHYSEKLRELVSMCIY 246
                         250
                  ....*....|....
gi 1024249297 502 MDVDRRGSAKELLQ 515
Cdd:cd08228   247 PDPDQRPDIGYVHQ 260
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
268-519 2.51e-33

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: 128.18  E-value: 2.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQpkKELI----INEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETE--DEGVpstaIREISLLKELNHPNIVRLLDVVHSENKLYLVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGG--SLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC-------AQITP 414
Cdd:cd07835    79 FLDLDlkKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLArafgvpvRTYTH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EqskrstmVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQN-------- 484
Cdd:cd07835   159 E-------VVTLWYRAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIfRTLGTPDEDVwpgvtslp 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 485 ----------PERLSAVF-------RDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07835   232 dykptfpkwaRQDLSKVVpsldedgLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
274-518 3.40e-33

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: 129.01  E-value: 3.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELII---------NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKIL------KKEVIIakdevahtlTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd05571    77 VNGGELfFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMD 503
Cdd:cd05571   157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILME---EVRFPSTLSPEAKSLLAGLLKKD 233
                         250       260
                  ....*....|....*....|
gi 1024249297 504 VDRR--GS---AKELLQHPF 518
Cdd:cd05571   234 PKKRlgGGprdAKEIMEHPF 253
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
321-518 4.65e-33

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: 126.71  E-value: 4.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 321 KNPNIVNYLDSYLV---GDELWVV---MEYLAGGSLTDV---VTETCMDegQIAAVCRECLQALDFLHSNQVIHRDIKSD 391
Cdd:cd14012    56 RHPNLVSYLAFSIErrgRSDGWKVyllTEYAPGGSLSELldsVGSVPLD--TARRWTLQLLEALEYLHRNGVVHKSLHAG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 392 NILL---GMDGSVKLTDFGFCAQITPEQSKRSTMVGTP-YWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 466
Cdd:cd14012   134 NVLLdrdAGTGIVKLTDYSLGKTLLDMCSRGSLDEFKQtYWLPPELAQgSKSPTRKTDVWDLGLLFLQMLFGLDVLEKYT 213
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 467 PLRALyliatngtpelQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14012   214 SPNPV-----------LVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHEF 254
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
274-519 5.13e-33

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: 126.61  E-value: 5.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd14116    13 LGKGKFGNVYLAREKQSKFILALKvlfKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQiTPeQSKRSTMVGTPYWM 429
Cdd:cd14116    93 YRELQKlSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVH-AP-SSRRTTLCGTLDYL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 430 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY---LNENPLRALYLIatngtpELQNPERLSAVFRDFLNRCLEMDVDR 506
Cdd:cd14116   171 PPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFeanTYQETYKRISRV------EFTFPDFVTEGARDLISRLLKHNPSQ 244
                         250
                  ....*....|...
gi 1024249297 507 RGSAKELLQHPFL 519
Cdd:cd14116   245 RPMLREVLEHPWI 257
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
274-517 7.87e-33

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: 126.71  E-value: 7.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTV----------YTALDIATGQEVaIKQMNLQQQPKK--------------ELIINEILVMRENKNPNIVNY- 328
Cdd:cd14118     2 IGKGSYGIVklayneedntLYAMKILSKKKL-LKQAGFFRRPPPrrkpgalgkpldplDRVYREIAILKKLDHPNVVKLv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 329 --LDSyLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 406
Cdd:cd14118    81 evLDD-PNEDNLYMVFELVDKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 407 GFCAQITPEQSKRSTMVGTPYWMAPEVVT--RKAYGPK-VDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQ 483
Cdd:cd14118   160 GVSNEFEGDDALLSSTAGTPAFMAPEALSesRKKFSGKaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTD---PVV 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1024249297 484 NPER--LSAVFRDFLNRCLEMDVDRRGSAKELLQHP 517
Cdd:cd14118   237 FPDDpvVSEQLKDLILRMLDKNPSERITLPEIKEHP 272
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
266-519 8.48e-33

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: 126.51  E-value: 8.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQ--QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd14097     1 KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKagSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVT-ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL-------GMDGSVKLTDFGFCAQ-ITP 414
Cdd:cd14097    81 LCEDGELKELLLrKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnNDKLNIKVTDFGLSVQkYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQNP--ERLSAVF 492
Cdd:cd14097   161 GEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSE-EKLFEEIRKGDLTFTQSvwQSVSDAA 239
                         250       260
                  ....*....|....*....|....*..
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14097   240 KNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
267-520 9.12e-33

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: 128.03  E-value: 9.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNL----QQQPKKelIINEILVMRENKNPNIVNYLD-----SYLVGDE 337
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfddLIDAKR--ILREIKILRHLKHENIIGLLDilrppSPEEFND 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYL---------AGGSLTDVVTETCMdeGQIaavcrecLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF 408
Cdd:cd07834    79 VYIVTELMetdlhkvikSPQPLTDDHIQYFL--YQI-------LRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 CAQITPEQSKRsTM---VGTPYWMAPEVV-TRKAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI-ATNGTPEL 482
Cdd:cd07834   150 ARGVDPDEDKG-FLteyVVTRWYRAPELLlSSKKYTKAIDIWSVGcIFA-ELLTRKPLFPGRDYIDQLNLIvEVLGTPSE 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024249297 483 QN--------------------PERLSAVF-------RDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd07834   228 EDlkfissekarnylkslpkkpKKPLSEVFpgaspeaIDLLEKMLVFNPKKRITADEALAHPYLA 292
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
274-519 1.15e-32

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: 125.74  E-value: 1.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd14186     9 LGKGSFACVYRARSLHTGLEVAIKMIDkkaMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 428
Cdd:cd14186    89 SRYLKNRKkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFTMCGTPNY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMDVDRRG 508
Cdd:cd14186   169 ISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLA---DYEMPAFLSREAQDLIHQLLRKNPADRL 245
                         250
                  ....*....|.
gi 1024249297 509 SAKELLQHPFL 519
Cdd:cd14186   246 SLSSVLDHPFM 256
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
261-519 1.16e-32

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: 127.09  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 261 VGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlqqqPKKEL------IINEILVMRENKNPNIVNYLDSYLV 334
Cdd:cd14168     5 VEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCI-----PKKALkgkessIENEIAVLRKIKHENIVALEDIYES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 335 GDELWVVMEYLAGGSLTDVVTETCM-DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL--GMDGS-VKLTDFGFcA 410
Cdd:cd14168    80 PNHLYLVMQLVSGGELFDRIVEKGFyTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsQDEESkIMISDFGL-S 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 QITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRaLYLIATNGTPELQNP--ERL 488
Cdd:cd14168   159 KMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKADYEFDSPywDDI 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 489 SAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14168   238 SDSAKDFIRNLMEKDPNKRYTCEQALRHPWI 268
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
268-519 1.38e-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: 126.67  E-value: 1.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14177     6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEI--EIL-MRYGQHPNIITLKDVYDDGRYVYLVTELMKG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMD-----GSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd14177    83 GELLDrILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILY-MDdsanaDSIRICDFGFAKQLRGENGLLLT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALYLIAtNGTPELQ--NPERLSAVFRDFL 496
Cdd:cd14177   162 PCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIG-SGKFSLSggNWDTVSDAAKDLL 240
                         250       260
                  ....*....|....*....|...
gi 1024249297 497 NRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14177   241 SHMLHVDPHQRYTAEQVLKHSWI 263
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
274-516 1.55e-32

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: 124.91  E-value: 1.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYtaLDIATGQEVAIKQMNLQQQpkkeliiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd14059     1 LGSGAQGAVF--LGKFRGEEVAVKKVRDEKE-------TDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 V-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpEQSKRSTMVGTPYWMAPE 432
Cdd:cd14059    72 LrAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELS-EKSTKMSFAGTVAWMAPE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 433 VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTpELQNPERLSAVFRDFLNRCLEMDVDRRGSAKE 512
Cdd:cd14059   151 VIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSL-QLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQ 229

                  ....
gi 1024249297 513 LLQH 516
Cdd:cd14059   230 ILMH 233
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
273-519 2.19e-32

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: 124.93  E-value: 2.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNlQQQPKKELIINEIL-----VMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14070     9 KLGEGSFAKVREGLHAVTGEKVAIKVID-KKKAKKDSYVTKNLrregrIQQMIRHPNITQLLDILETENSYYLVMELCPG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF--CAQITPEQSKRSTMVG 424
Cdd:cd14070    88 GNLMHRIYDKKrLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLsnCAGILGYSDPFSTQCG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN-PLRALYLIATNGtpELQN-PERLSAVFRDFLNRCLEM 502
Cdd:cd14070   168 SPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPfSLRALHQKMVDK--EMNPlPTDLSPGAISFLRSLLEP 245
                         250
                  ....*....|....*..
gi 1024249297 503 DVDRRGSAKELLQHPFL 519
Cdd:cd14070   246 DPLKRPNIKQALANRWL 262
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
274-519 2.78e-32

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: 124.89  E-value: 2.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEYLAGGS 349
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDfveKFLPRELEILARLNHKSIIKTYEIFETSDgKVYIVMELGVQGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVT-ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR----STMVG 424
Cdd:cd14165    89 LLEFIKlRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRivlsKTFCG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPER--LSAVFRDFLNRCLE 501
Cdd:cd14165   169 SAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEH---RVRFPRSknLTSECKDLIYRLLQ 245
                         250
                  ....*....|....*...
gi 1024249297 502 MDVDRRGSAKELLQHPFL 519
Cdd:cd14165   246 PDVSQRLCIDEVLSHPWL 263
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
272-519 3.20e-32

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: 124.45  E-value: 3.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIK---QMNLQQQPKKELIiNEILVMRENKNPNIVNYldsYLVGD---ELWVVMEYL 345
Cdd:cd14074     9 ETLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDDVSKAHLF-QEVRCMKLVQHPNVVRL---YEVIDtqtKLYLILELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVT--ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL-GMDGSVKLTDFGFCAQITPEQsKRSTM 422
Cdd:cd14074    85 DGGDMYDYIMkhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGE-KLETS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELqnPERLSAVFRDFLNRCLE 501
Cdd:cd14074   164 CGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMI-MDCKYTV--PAHVSPECKDLIRRMLI 240
                         250
                  ....*....|....*...
gi 1024249297 502 MDVDRRGSAKELLQHPFL 519
Cdd:cd14074   241 RDPKKRASLEEIENHPWL 258
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
249-519 4.58e-32

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: 126.68  E-value: 4.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 249 EEILEKLRSIVSVGDpkkkYTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELII---------NEILVMRE 319
Cdd:cd05594    12 EVSLTKPKHKVTMND----FEYLKLLGKGTFGKVILVKEKATGRYYAMKIL------KKEVIVakdevahtlTENRVLQN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 320 NKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQ-VIHRDIKSDNILLGM 397
Cdd:cd05594    82 SRHPFLTALKYSFQTHDRLCFVMEYANGGELFfHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 398 DGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN 477
Cdd:cd05594   162 DGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILME 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1024249297 478 gtpELQNPERLSAVFRDFLNRCLEMDVDRR---GS--AKELLQHPFL 519
Cdd:cd05594   242 ---EIRFPRTLSPEAKSLLSGLLKKDPKQRlggGPddAKEIMQHKFF 285
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
271-518 5.45e-32

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: 124.44  E-value: 5.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEK---IGQGASGTVYTALDIATGQEVAIKQMN-----LQQQPKKELIINEILVMRENknPNIVNYLDSYLVGDELWVVM 342
Cdd:cd05609     2 FETiklISNGAYGAVYLVRHRETRQRFAMKKINkqnliLRNQIQQVFVERDILTFAEN--PFVVSMYCSFETKRHLCMVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGG---SLTDVVTETCMDEGQIAAVcrECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG------------ 407
Cdd:cd05609    80 EYVEGGdcaTLLKNIGPLPVDMARMYFA--ETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGlskiglmslttn 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 408 ----FCAQITPEQSKRStMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGtpELQ 483
Cdd:cd05609   158 lyegHIEKDTREFLDKQ-VCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELFGQVISD--EIE 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1024249297 484 NPER---LSAVFRDFLNRCLEMD-VDRRG--SAKELLQHPF 518
Cdd:cd05609   234 WPEGddaLPDDAQDLITRLLQQNpLERLGtgGAEEVKQHPF 274
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
272-455 6.96e-32

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: 123.94  E-value: 6.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNL-QQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd13996    12 ELLGSGGFGSVYKVRNKVDGVTYAIKKIRLtEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGGTL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVTE----TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD-GSVKLTDFGFCAQIT------------ 413
Cdd:cd13996    92 RDWIDRrnssSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGnqkrelnnlnnn 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1024249297 414 --PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM 455
Cdd:cd13996   172 nnGNTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEM 215
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
268-518 9.61e-32

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: 123.77  E-value: 9.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEgvPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGG--SLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC-AQITPEQSKRSTM 422
Cdd:cd07860    82 HQDlkKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLArAFGVPVRTYTHEV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VgTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTP---------ELQN------- 484
Cdd:cd07860   162 V-TLWYRAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIfRTLGTPdevvwpgvtSMPDykpsfpk 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1024249297 485 --PERLSAVF-------RDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07860   241 waRQDFSKVVppldedgRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
268-518 1.06e-31

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: 123.87  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQmnLQQQPKKELI----INEILVMRENKNPNIVNyLDSYLVG---DELWV 340
Cdd:cd07843     7 YEKLNRIEEGTYGVVYRARDKKTGEIVALKK--LKMEKEKEGFpitsLREINILLKLQHPNIVT-VKEVVVGsnlDKIYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLAGgSLTDVVTEtcMDE----GQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ 416
Cdd:cd07843    84 VMEYVEH-DLKSLMET--MKQpflqSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGSPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVGTPYWMAPEVV-TRKAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI-------------------- 474
Cdd:cd07843   161 KPYTQLVVTLWYRAPELLlGAKEYSTAIDMWSVGcIFA-ELLTKKPLFPGKSEIDQLNKIfkllgtptekiwpgfselpg 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 475 ATNGTPELQNPERLSAVFR---------DFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07843   240 AKKKTFTKYPYNQLRKKFPalslsdngfDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
268-520 1.36e-31

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: 124.74  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNlqqqpKKELIINE----------ILVmrENKNPNIVNYLDSYLVGDE 337
Cdd:cd05598     3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLR-----KKDVLKRNqvahvkaerdILA--EADNEWVVKLYYSFQDKEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTETCMDEGQIAavcR----ECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 413
Cdd:cd05598    76 LYFVMDYIPGGDLMSLLIKKGIFEEDLA---RfyiaELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 414 -PEQSKR---STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNPE--R 487
Cdd:cd05598   153 wTHDSKYylaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKV-INWRTTLKIPHeaN 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1024249297 488 LSAVFRDFLNRcLEMDVDRR---GSAKELLQHPFLK 520
Cdd:cd05598   232 LSPEAKDLILR-LCCDAEDRlgrNGADEIKAHPFFA 266
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
272-517 1.52e-31

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: 122.78  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQmnLQQQPKKEliiNEI-LVMRENKNPNIVNYLDSY--LVGDE--LWVVMEYLA 346
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKV--LRDNPKAR---REVeLHWRASGCPHIVRIIDVYenTYQGRkcLLVVMECME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETC---MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFcAQITPEQSKRS 420
Cdd:cd14089    82 GGELFSRIQERAdsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYsskGPNAILKLTDFGF-AKETTTKKSLQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLG-IMAIeMVEGEPPYLNENPLRalylIA-------TNGTPELQNPE--RLSA 490
Cdd:cd14089   161 TPCYTPYYVAPEVLGPEKYDKSCDMWSLGvIMYI-LLCGYPPFYSNHGLA----ISpgmkkriRNGQYEFPNPEwsNVSE 235
                         250       260
                  ....*....|....*....|....*..
gi 1024249297 491 VFRDFLNRCLEMDVDRRGSAKELLQHP 517
Cdd:cd14089   236 EAKDLIRGLLKTDPSERLTIEEVMNHP 262
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
268-519 2.78e-31

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: 122.02  E-value: 2.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELII---NEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKflpREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF-CAQITPEQSKR--- 419
Cdd:cd14162    82 AENGDLLDYIrKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFaRGVMKTKDGKPkls 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMVEGEPPYLNENpLRALyLIATNGTPELQNPERLSAVFRDFLNR 498
Cdd:cd14162   162 ETYCGSYAYASPEILRGIPYDPFLsDIWSMGVVLYTMVYGRLPFDDSN-LKVL-LKQVQRRVVFPKNPTVSEECKDLILR 239
                         250       260
                  ....*....|....*....|.
gi 1024249297 499 CLeMDVDRRGSAKELLQHPFL 519
Cdd:cd14162   240 ML-SPVKKRITIEEIKRDPWF 259
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
269-525 2.79e-31

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: 123.25  E-value: 2.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 269 TRFEK---IGQGASGTVYTALDIATGQEVAIKQMNLQQQpkKELI----INEILVMRENKNPNIVNYLDsYLVGDEL--- 338
Cdd:cd07845     7 TEFEKlnrIGEGTYGIVYRARDTTSGEIVALKKVRMDNE--RDGIpissLREITLLLNLRHPNIVELKE-VVVGKHLdsi 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEY----LAggSLTDVVTeTCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP 414
Cdd:cd07845    84 FLVMEYceqdLA--SLLDNMP-TPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN-GTP---------ELQ 483
Cdd:cd07845   161 PAKPMTPKVVTLWYRAPELLLgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLlGTPnesiwpgfsDLP 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1024249297 484 NPER-----------------LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKlAKPL 525
Cdd:cd07845   241 LVGKftlpkqpynnlkhkfpwLSEAGLRLLNFLLMYDPKKRATAEEALESSYFK-EKPL 298
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
274-466 4.40e-31

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: 122.99  E-value: 4.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIINE-----------ILVMrENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVL------KKDVILQDddvdctmtekrILAL-AAKHPFLTALHSCFQTKDRLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd05591    76 EYVNGGDLMfQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 466
Cdd:cd05591   156 FCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADN 200
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
273-519 8.71e-31

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: 120.81  E-value: 8.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQ--QPKKELIINEILVMR-ENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd14197    16 ELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRkgQDCRMEIIHEIAVLElAQANPWVINLHEVYETASEMILVLEYAAGGE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVT---ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRSTMv 423
Cdd:cd14197    96 IFNQCVadrEEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEELREIM- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT-NGTPELQNPERLSAVFRDFLNRCLEM 502
Cdd:cd14197   175 GTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQmNVSYSEEEFEHLSESAIDFIKTLLIK 254
                         250
                  ....*....|....*..
gi 1024249297 503 DVDRRGSAKELLQHPFL 519
Cdd:cd14197   255 KPENRATAEDCLKHPWL 271
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
274-467 1.32e-30

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: 121.02  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDsylVGDELWVV--------- 341
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSdknRERWCLEVQIMKKLNHPNVVSARD---VPPELEKLspndlplla 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVT--ETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG-MDGSV--KLTDFGFcAQITP 414
Cdd:cd13989    78 MEYCSGGDLRKVLNqpENCcgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQqGGGRViyKLIDLGY-AKELD 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL-NENP 467
Cdd:cd13989   157 QGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLpNWQP 210
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
268-519 1.41e-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: 119.85  E-value: 1.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVMEY 344
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRErkAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd08223    82 CEGGDLYTRLKEqkgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMATT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRAL-YLIATNGTPELqnPERLSAVFRDFLNRCL 500
Cdd:cd08223   162 LIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAF-NAKDMNSLvYKILEGKLPPM--PKQYSPELGELIKAML 238
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd08223   239 HQDPEKRPSVKRILRQPYI 257
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
272-514 1.63e-30

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: 119.80  E-value: 1.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTAldIATGQEVAIKQMNLQQQPKKEL--IINEILVMREnKNPNIVNYL---DSYLVGDELWVVMEYLA 346
Cdd:cd13979     9 EPLGSGGFGSVYKA--TYKGETVAVKIVRRRRKNRASRqsFWAELNAARL-RHENIVRVLaaeTGTDFASLGLIIMEYCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVtetcmDEGQIAAVCRECLQ-------ALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGfCAQITPE---- 415
Cdd:cd13979    86 NGTLQQLI-----YEGSEPLPLAHRILisldiarALRFCHSHGIVHLDVKPANILISEQGVCKLCDFG-CSVKLGEgnev 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER--LSAVFR 493
Cdd:cd13979   160 GTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRPDLSGLEDseFGQRLR 239
                         250       260
                  ....*....|....*....|.
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELL 514
Cdd:cd13979   240 SLISRCWSAQPAERPNADESL 260
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
265-462 1.74e-30

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: 119.67  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALDiATGQEVAIKQMNLQQ-QPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd14161     2 KHRYEFLETLGKGTYGRVKKARD-SSGRLVAIKSIRKDRiKDEQDLlhIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRS 420
Cdd:cd14161    81 MEYASRGDLYDYISERQrLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGL-SNLYNQDKFLQ 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1024249297 421 TMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd14161   160 TYCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPF 202
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
274-515 2.30e-30

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: 119.08  E-value: 2.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTAldIATGQEVAIKQMNLQQQpkKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd14058     1 VGRGSFGVVCKA--RWRNQIVAVKIIESESE--KKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 ----VTETCMDEGQIAAVCRECLQALDFLHSNQ---VIHRDIKSDNILLGMDGSV-KLTDFGFCAQItpeQSKRSTMVGT 425
Cdd:cd14058    77 lhgkEPKPIYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVlKICDFGTACDI---STHMTNNKGS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGT--PELQN-PERLsavfRDFLNRCLE 501
Cdd:cd14058   154 AAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHiGGPAFRIMWAVHNGErpPLIKNcPKPI----ESLMTRCWS 229
                         250
                  ....*....|....
gi 1024249297 502 MDVDRRGSAKELLQ 515
Cdd:cd14058   230 KDPEKRPSMKEIVK 243
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
272-518 2.47e-30

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 119.44  E-value: 2.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE--LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQesQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHGDM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS---VKLTDFGFcAQITPEQSKRSTMVG 424
Cdd:cd14082    89 LEMILSSEKgrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGF-ARIIGEKSFRRSVVG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY-----LNENPLRALYLIATNGTPELQnperLSAVfrDFLNRC 499
Cdd:cd14082   168 TPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnededINDQIQNAAFMYPPNPWKEIS----PDAI--DLINNL 241
                         250
                  ....*....|....*....
gi 1024249297 500 LEMDVDRRGSAKELLQHPF 518
Cdd:cd14082   242 LQVKMRKRYSVDKSLSHPW 260
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
268-519 2.57e-30

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: 119.35  E-value: 2.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK------KELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd14194     7 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsREDIEREVSILKEIQHPNVITLHEVYENKTDVILI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGSV-----KLTDFGFCAQITPE 415
Cdd:cd14194    87 LELVAGGELFDFLAEKeSLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIML-LDRNVpkpriKIIDFGLAHKIDFG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRStMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPERLSAVFRD 494
Cdd:cd14194   166 NEFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVsAVNYEFEDEYFSNTSALAKD 244
                         250       260
                  ....*....|....*....|....*
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14194   245 FIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
274-520 3.00e-30

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: 120.57  E-value: 3.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIINE-----ILVMRE-----NKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKAL------KKDVVLEDddvecTMIERRvlalaSQHPFLTHLFCTFQTESHLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd05592    77 YLNGGDLMfHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELqnPERLSAVFRDFLNRCLEM 502
Cdd:cd05592   157 CGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDE-DELFWSICNDTPHY--PRWLTKEAASCLSLLLER 233
                         250       260
                  ....*....|....*....|...
gi 1024249297 503 DVDRR-----GSAKELLQHPFLK 520
Cdd:cd05592   234 NPEKRlgvpeCPAGDIRDHPFFK 256
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
263-519 3.56e-30

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: 118.88  E-value: 3.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPK--KKYTRFEKIGQGASGTVYTALDIATGQ----EVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGD 336
Cdd:cd14187     2 DPRtrRRYVRGRFLGKGGFAKCYEITDADTKEvfagKIVPKSLLLKPH-QKEKMSMEIAIHRSLAHQHVVGFHGFFEDND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTDV-VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 415
Cdd:cd14187    81 FVYVVLELCRRRSLLELhKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYL-IATNgtpELQNPERLSAVFRD 494
Cdd:cd14187   161 GERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPF-ETSCLKETYLrIKKN---EYSIPKHINPVAAS 236
                         250       260
                  ....*....|....*....|....*
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14187   237 LIQKMLQTDPTARPTINELLNDEFF 261
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
274-519 3.56e-30

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: 120.46  E-value: 3.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQkktiLKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 L-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ-ITPEQSKrSTMVGTPY 427
Cdd:cd05603    83 LfFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEgMEPEETT-STFCGTPE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPERLSAVfrDFLNRCLEMDVDRR 507
Cdd:cd05603   162 YLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRD-VSQMYDNILHKPLHLPGGKTVAAC--DLLQGLLHKDQRRR 238
                         250
                  ....*....|....*.
gi 1024249297 508 GSAK----ELLQHPFL 519
Cdd:cd05603   239 LGAKadflEIKNHVFF 254
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
271-522 3.82e-30

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: 119.85  E-value: 3.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEKI---GQGASGTVYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd06615     3 FEKLgelGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAiRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSN-QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeQSKRSTMVG 424
Cdd:cd06615    83 GGSLDQVLKKAGrIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--DSMANSFVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEG-------------------EPPYLNENPLRALYLIATNGTP----- 480
Cdd:cd06615   161 TRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrypipppdakeleamfgrpVSEGEAKESHRPVSGHPPDSPRpmaif 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 481 EL------QNPERL-----SAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLA 522
Cdd:cd06615   241 ELldyivnEPPPKLpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRA 293
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
265-520 3.98e-30

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 120.64  E-value: 3.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEK-IGQGASGTVYTALDIATGQEVAIKQMNLQQQPK-----KELI---------INEILVMRENKNPNIVNYL 329
Cdd:PTZ00024    7 SERYIQKGAhLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNdvtkdRQLVgmcgihfttLRELKIMNEIKHENIMGLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 330 DSYLVGDELWVVMEYLAGgSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF 408
Cdd:PTZ00024   87 DVYVEGDFINLVMDIMAS-DLKKVVdRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 -----CAQITPEQSKRSTM---------VGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYL 473
Cdd:PTZ00024  166 arrygYPPYSDTLSKDETMqrreemtskVVTLWYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGR 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 474 I-ATNGTPELQN-----------------PERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:PTZ00024  246 IfELLGTPNEDNwpqakklplyteftprkPKDLKTIFPnasddaiDLLQSLLKLNPLERISAKEALKHEYFK 317
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
273-519 4.15e-30

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: 118.59  E-value: 4.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQ--QPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd14075     9 ELGSGNFSQVKLGIHQLTKEKVAIKILDKTKldQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 -TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQsKRSTMVGTPYWM 429
Cdd:cd14075    89 yTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGE-TLNTFCGSPPYA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 430 APEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-------LNENPLRALYLIatngtpelqnPERLSAVFRDFLNRCLE 501
Cdd:cd14075   168 APELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFraetvakLKKCILEGTYTI----------PSYVSEPCQELIRGILQ 237
                         250
                  ....*....|....*...
gi 1024249297 502 MDVDRRGSAKELLQHPFL 519
Cdd:cd14075   238 PVPSDRYSIDEIKNSEWL 255
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
266-519 4.55e-30

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


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 118.49  E-value: 4.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd14189     1 RSYCKGRLLGKGGFARCYEMTDLATNKTYAVKvipHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDV-VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd14189    81 ELCSRKSLAHIwKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELqnPERLSAVFRDFLNRCLE 501
Cdd:cd14189   161 ICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLD-LKETYRCIKQVKYTL--PASLSLPARHLLAGILK 237
                         250
                  ....*....|....*...
gi 1024249297 502 MDVDRRGSAKELLQHPFL 519
Cdd:cd14189   238 RNPGDRLTLDQILEHEFF 255
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
274-520 5.37e-30

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: 120.03  E-value: 5.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIINEILV---MRENK-------NPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05619    13 LGKGSFGKVFLAELKGTNQFFAIKAL------KKDVVLMDDDVectMVEKRvlslaweHPFLTHLFCTFQTKENLFFVME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVtETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd05619    87 YLNGGDLMFHI-QSChkFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTST 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTpelQNPERLSAVFRDFLNRCLE 501
Cdd:cd05619   166 FCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNP---FYPRWLEKEAKDILVKLFV 242
                         250       260
                  ....*....|....*....|
gi 1024249297 502 MDVDRR-GSAKELLQHPFLK 520
Cdd:cd05619   243 REPERRlGVRGDIRQHPFFR 262
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
270-517 5.73e-30

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: 117.87  E-value: 5.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RFEKIGQGASGTVYTALDIATGQEVAIKQMNLQ-------QQPKKELIINEILvmreNKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd13997     4 ELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPfrgpkerARALREVEAHAAL----GQHPNIVRYYSSWEEGGHLYIQM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTE----TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeqsk 418
Cdd:cd13997    80 ELCENGSLQDALEElspiSKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLE----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 RSTMV--GTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPpyLNEN-----PLRALYLiatngtPELQNPeRLSA 490
Cdd:cd13997   155 TSGDVeeGDSRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEP--LPRNgqqwqQLRQGKL------PLPPGL-VLSQ 225
                         250       260
                  ....*....|....*....|....*..
gi 1024249297 491 VFRDFLNRCLEMDVDRRGSAKELLQHP 517
Cdd:cd13997   226 ELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
274-520 9.35e-30

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: 119.28  E-value: 9.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIINEILV---MRENK-------NPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05620     3 LGKGSFGKVLLAELKGKGEYFAVKAL------KKDVVLIDDDVectMVEKRvlalaweNPFLTHLYCTFQTKEHLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd05620    77 FLNGGDLMFHIQDKGrFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgTPELqnPERLSAVFRDFLNRCLEM 502
Cdd:cd05620   157 CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVD-TPHY--PRWITKESKDILEKLFER 233
                         250
                  ....*....|....*....
gi 1024249297 503 DVDRR-GSAKELLQHPFLK 520
Cdd:cd05620   234 DPTRRlGVVGNIRGHPFFK 252
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
268-519 9.70e-30

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: 119.74  E-value: 9.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14176    21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI--EIL-LRYGQHPNIITLKDVYDDGKYVYVVTELMKG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd14176    98 GELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENGLLMTP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN---ENPLRALYLIATnGTPELQNP--ERLSAVFRDFLN 497
Cdd:cd14176   178 CYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGS-GKFSLSGGywNSVSDTAKDLVS 256
                         250       260
                  ....*....|....*....|..
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14176   257 KMLHVDPHQRLTAALVLRHPWI 278
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
274-520 1.06e-29

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: 119.24  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIINEILV---MRENK-------NPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05590     3 LGKGSFGKVMLARLKESGRLYAVKVL------KKDVILQDDDVectMTEKRilslarnHPFLTQLYCCFQTPDRLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd05590    77 FVNGGDLMFHIQKSRrFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEM 502
Cdd:cd05590   157 CGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILND---EVVYPTWLSQDAVDILKAFMTK 233
                         250       260
                  ....*....|....*....|....
gi 1024249297 503 DVDRR------GSAKELLQHPFLK 520
Cdd:cd05590   234 NPTMRlgsltlGGEEAILRHPFFK 257
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
274-515 1.08e-29

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: 117.76  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALdIATGQEVAIKQMNLQ--QQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMncAASKKEFL-TELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTETCMDE----GQIAAVCRECLQALDFLHS---NQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP--EQSKRSTM 422
Cdd:cd14066    79 DRLHCHKGSPplpwPQRLKIAKGIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPseSVSKTSAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLiatNGTPELQnpERLSAVFRDFLNRCL-E 501
Cdd:cd14066   159 KGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAV-DENRENASRK---DLVEWVE--SKGKEELEDILDKRLvD 232
                         250
                  ....*....|....
gi 1024249297 502 MDVDRRGSAKELLQ 515
Cdd:cd14066   233 DDGVEEEEVEALLR 246
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
275-514 1.23e-29

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: 116.98  E-value: 1.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 275 GQGASGTVYTALDIATGQEVAIKQMNlqqQPKKELIINEILVMRenknpNIVNYLDSYLVGDELWVVMEYLAGGSLTDVV 354
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLL---KIEKEAEILSVLSHR-----NIIQFYGAILEAPNYGIVTEYASYGSLFDYL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 355 TET---CMDEGQIAAVCRECLQALDFLHSN---QVIHRDIKSDNILLGMDGSVKLTDFGfcAQITPEQSKRSTMVGTPYW 428
Cdd:cd14060    74 NSNeseEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFG--ASRFHSHTTHMSLVGTFPW 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTpELQNPERLSAVFRDFLNRCLEMDVDRRG 508
Cdd:cd14060   152 MAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNE-RPTIPSSCPRSFAELMRRCWEADVKERP 230

                  ....*.
gi 1024249297 509 SAKELL 514
Cdd:cd14060   231 SFKQII 236
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
266-519 1.37e-29

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: 119.60  E-value: 1.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd05610     4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMvhqVQAERDALALSKSPFIVHLYYSLQSANNVYLVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC------------ 409
Cdd:cd05610    84 EYLIGGDVKSLLhIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnrelnmmd 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 410 ------------------AQI----------------TPEQSKRST-------MVGTPYWMAPEVVTRKAYGPKVDIWSL 448
Cdd:cd05610   164 ilttpsmakpkndysrtpGQVlslisslgfntptpyrTPKSVRRGAarvegerILGTPDYLAPELLLGKPHGPAVDWWAL 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 449 GIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd05610   244 GVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGEEELSVNAQNAIEILLTMDPTKRAGLKELKQHPLF 314
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
274-520 1.58e-29

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: 118.56  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELII--NEI----------LVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTGELFAIKAL------KKGDIIarDEVeslmcekrifETVNSARHPFLVNLFACFQTPEHVCFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSL-----TDVVTETcmdEGQIAAVCreCLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ 416
Cdd:cd05589    81 MEYAAGGDLmmhihEDVFSEP---RAVFYAAC--VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFL 496
Cdd:cd05589   156 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVND---EVRYPRFLSTEAISIM 232
                         250       260
                  ....*....|....*....|....*....
gi 1024249297 497 NRCLEMDVDRR-GS----AKELLQHPFLK 520
Cdd:cd05589   233 RRLLRKNPERRlGAserdAEDVKKQPFFR 261
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
266-520 1.61e-29

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: 118.94  E-value: 1.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNlqqQPKKELI-----INEILVMRENKNPNIVNYLDSYLVGDEL-- 338
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLS---RPFQSAIhakrtYRELRLLKHMKHENVIGLLDVFTPASSLed 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 ----WVVMEyLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItp 414
Cdd:cd07851    92 fqdvYLVTH-LMGADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHT-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 eQSKRSTMVGTPYWMAPEVV-TRKAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI-ATNGTP--EL------- 482
Cdd:cd07851   169 -DDEMTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGcIMA-ELLTGKTLFPGSDHIDQLKRImNLVGTPdeELlkkisse 246
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 483 --QN-----PER----LSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd07851   247 saRNyiqslPQMpkkdFKEVFSganplaiDLLEKMLVLDPDKRITAAEALAHPYLA 302
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
274-515 1.64e-29

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: 116.72  E-value: 1.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTAldIATGQEVAIKQmnLQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14061     2 IGVGGFGKVYRG--IWRGEEVAVKA--ARQDPDEDISVTLENVRQEARlfwmlrHPNIIALRGVCLQPPNLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTETCMDEG-------QIAavcreclQALDFLHSNQ---VIHRDIKSDNILLG--------MDGSVKLTDFGFC 409
Cdd:cd14061    78 GALNRVLAGRKIPPHvlvdwaiQIA-------RGMNYLHNEApvpIIHRDLKSSNILILeaienedlENKTLKITDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 410 AQITpeQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgTPELQNPERLS 489
Cdd:cd14061   151 REWH--KTTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVN-KLTLPIPSTCP 227
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 490 AVFRDFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd14061   228 EPFAQLMKDCWQPDPHDRPSFADILK 253
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
272-519 1.65e-29

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: 117.33  E-value: 1.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVA---IKQMNLQQQPKKElIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14198    14 KELGRGKFAVVRQCISKSTGQEYAakfLKKRRRGQDCRAE-ILHEIAVLELAKsNPRVVNLHEVYETTSEIILILEYAAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTETCMD---EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd14198    93 GEIFNLCVPDLAEmvsENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRKIGHACELREI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MvGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE-NPLRALYLIATNGTPELQNPERLSAVFRDFLNRCL 500
Cdd:cd14198   173 M-GTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEdNQETFLNISQVNVDYSEETFSSVSQLATDFIQKLL 251
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd14198   252 VKNPEKRPTAEICLSHSWL 270
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
272-519 1.90e-29

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 116.99  E-value: 1.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTETCMDEGQIAAV--CRECLQALDFLHSNQVIHRDIKSDNILL--GMDGSVKLTDFGFCAQITPEQsKRSTMVGTPY 427
Cdd:cd14192    90 DRITDESYQLTELDAIlfTRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQIKIIDFGLARRYKPRE-KLKVNFGTPE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAL-YLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDR 506
Cdd:cd14192   169 FLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMnNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKSC 248
                         250
                  ....*....|...
gi 1024249297 507 RGSAKELLQHPFL 519
Cdd:cd14192   249 RMSATQCLKHEWL 261
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
274-513 2.10e-29

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: 116.98  E-value: 2.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 VTEtcMDE----GQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT--------------PE 415
Cdd:cd14221    81 IKS--MDShypwSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVdektqpeglrslkkPD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM---VEGEPPYLnenPLRALYLIATNGTPELQNPERLSAVF 492
Cdd:cd14221   159 RKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIigrVNADPDYL---PRTMDFGLNVRGFLDRYCPPNCPPSF 235
                         250       260
                  ....*....|....*....|.
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKEL 513
Cdd:cd14221   236 FPIAVLCCDLDPEKRPSFSKL 256
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-520 2.13e-29

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: 116.72  E-value: 2.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIA---TGQEVAIKQMN----LQQQPKKELIINEILVM-RENKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd05583     2 LGTGAYGKVFLVRKVGghdAGKLYAMKVLKkatiVQKAKTAEHTMTERQVLeAVRQSPFLVTLHYAFQTDAKLHLILDYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TMV 423
Cdd:cd05583    82 NGGELfTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAySFC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRK--AYGPKVDIWSLGIMAIEMVEGEPPYLNENplralyliATNGTPELQN---------PERLSAVF 492
Cdd:cd05583   162 GTIEYMAPEVVRGGsdGHDKAVDWWSLGVLTYELLTGASPFTVDG--------ERNSQSEISKrilkshppiPKTFSAEA 233
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1024249297 493 RDFLNRCLEMDVDRR-----GSAKELLQHPFLK 520
Cdd:cd05583   234 KDFILKLLEKDPKKRlgagpRGAHEIKEHPFFK 266
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
273-520 2.99e-29

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: 119.37  E-value: 2.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd05600    18 QVGQGGYGSVFLARKKDTGEICALKIMKkkvLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ------------ 416
Cdd:cd05600    98 FRTLLNNSgILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTLSPKkiesmkirleev 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 -------------------------SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY----LNENP 467
Cdd:cd05600   178 kntafleltakerrniyramrkedqNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFsgstPNETW 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 468 LRALYLIATNGTPELQNPER---LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd05600   258 ANLYHWKKTLQRPVYTDPDLefnLSDEAWDLITKLITDPQDRLQSPEQIKNHPFFK 313
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
268-519 3.08e-29

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: 116.43  E-value: 3.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVA---IKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAakfIKKRRSKASRRgvsREDIEREVSILRQVLHPNIITLHDVFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGSV-----KLTDFGFCAQITPE 415
Cdd:cd14105    87 LELVAGGELFDFLAEKeSLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIML-LDKNVpipriKLIDFGLAHKIEDG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRStMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNP--ERLSAVFR 493
Cdd:cd14105   166 NEFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANI-TAVNYDFDDEyfSNTSELAK 243
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14105   244 DFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
274-463 3.73e-29

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: 116.45  E-value: 3.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 VTEtcMDE----GQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC-------------------- 409
Cdd:cd14154    81 LKD--MARplpwAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerlpsgnmspsetlr 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 410 AQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM---VEGEPPYL 463
Cdd:cd14154   159 HLKSPDRKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIigrVEADPDYL 215
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
266-519 3.76e-29

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: 115.88  E-value: 3.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd14188     1 KRYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKiipHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd14188    81 EYCSRRSMAHILkARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELqnPERLSAVFRDFLNRCLE 501
Cdd:cd14188   161 ICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTN-LKETYRCIREARYSL--PSSLLAPAKHLIASMLS 237
                         250
                  ....*....|....*...
gi 1024249297 502 MDVDRRGSAKELLQHPFL 519
Cdd:cd14188   238 KNPEDRPSLDEIIRHDFF 255
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
274-520 4.47e-29

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: 118.41  E-value: 4.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIIN---EILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd05629     9 IGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHvkaERDVLAESDSPWVVSLYYSFQDAQYLYLIMEFLPGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 -TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA------------------Q 411
Cdd:cd05629    89 mTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhkqhdsayyqkllqgkS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 412 ITPEQSKRSTM-----------------------------VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd05629   169 NKNRIDNRNSVavdsinltmsskdqiatwkknrrlmaystVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIGWPPF 248
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 463 LNENPlRALYLIATNGTPELQNPE--RLSAVFRDFLNRCLEMDVDR--RGSAKELLQHPFLK 520
Cdd:cd05629   249 CSENS-HETYRKIINWRETLYFPDdiHLSVEAEDLIRRLITNAENRlgRGGAHEIKSHPFFR 309
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
273-518 6.33e-29

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: 115.83  E-value: 6.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI-INEILVMRE-NKNPNIVNYLDsyLVGDE----LWVVMEyLA 346
Cdd:cd07831     6 KIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNnLREIQALRRlSPHPNILRLIE--VLFDRktgrLALVFE-LM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVT--ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGSVKLTDFGFCAQITPEQSkRSTMVG 424
Cdd:cd07831    83 DMNLYELIKgrKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDILKLADFGSCRGIYSKPP-YTEYIS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTP-----ELQNPER---------- 487
Cdd:cd07831   161 TRWYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIhDVLGTPdaevlKKFRKSRhmnynfpskk 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1024249297 488 ----------LSAVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07831   241 gtglrkllpnASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
274-518 8.53e-29

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 114.67  E-value: 8.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD- 352
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMK-KKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDy 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 -VVTETCMDEgQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGFCAQITPEQsKRSTMVGTPYW 428
Cdd:cd14115    80 lMNHDELMEE-KVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEDAVQISGHR-HVHHLLGNPEF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPER----LSAVFRDFLNRCLEMDV 504
Cdd:cd14115   158 AAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVC---RVDFSFPDEyfgdVSQAARDFINVILQEDP 234
                         250
                  ....*....|....
gi 1024249297 505 DRRGSAKELLQHPF 518
Cdd:cd14115   235 RRRPTAATCLQHPW 248
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
274-519 1.07e-28

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: 114.41  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14071     8 IGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLkkIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 D-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQsKRSTMVGTPYWMA 430
Cdd:cd14071    88 DyLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGE-LLKTWCGSPPYAA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 431 PEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGtpELQNPERLSAVFRDFLNRCLEMDVDRRGS 509
Cdd:cd14071   167 PEVFEGKEYeGPQLDIWSLGVVLYVLVCGALPF-DGSTLQTLRDRVLSG--RFRIPFFMSTDCEHLIRRMLVLDPSKRLT 243
                         250
                  ....*....|
gi 1024249297 510 AKELLQHPFL 519
Cdd:cd14071   244 IEQIKKHKWM 253
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
268-519 1.17e-28

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: 114.72  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14191     4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTETCMD--EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL--GMDGSVKLTDFGFCAQITPEQSKRsTMV 423
Cdd:cd14191    84 GELFERIIDEDFEltERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLARRLENAGSLK-VLF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTNGTPELQNP--ERLSAVFRDFLNRCLE 501
Cdd:cd14191   163 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV-TSATWDFDDEafDEISDDAKDFISNLLK 241
                         250
                  ....*....|....*...
gi 1024249297 502 MDVDRRGSAKELLQHPFL 519
Cdd:cd14191   242 KDMKARLTCTQCLQHPWL 259
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
272-519 1.21e-28

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: 114.63  E-value: 1.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNIL-LGMDGS-VKLTDFGFCAQITPEQSKRSTMvGTPY 427
Cdd:cd14193    90 DRIIDENynLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANqVKIIDFGLARRYKPREKLRVNF-GTPE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAL-YLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDR 506
Cdd:cd14193   169 FLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLnNILACQWDFEDEEFADISEEAKDFISKLLIKEKSW 248
                         250
                  ....*....|...
gi 1024249297 507 RGSAKELLQHPFL 519
Cdd:cd14193   249 RMSASEALKHPWL 261
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
272-518 1.27e-28

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: 115.20  E-value: 1.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEI-LVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd14090     8 ELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVeTLHQCQGHPNILQLIEYFEDDERFYLVFEKMRGGPL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS---VKLTDFGFCAQI-----------TPE 415
Cdd:cd14090    88 LSHIEKrVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGSGIklsstsmtpvtTPE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QskrSTMVGTPYWMAPEVV---TRKA--YGPKVDIWSLGIMAIEMVEGEPPYLNE----------NPLRAL--YLIATNG 478
Cdd:cd14090   168 L---LTPVGSAEYMAPEVVdafVGEAlsYDKRCDLWSLGVILYIMLCGYPPFYGRcgedcgwdrgEACQDCqeLLFHSIQ 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1024249297 479 TPELQNPER----LSAVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14090   245 EGEYEFPEKewshISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
274-519 1.48e-28

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: 115.75  E-value: 1.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIIN---------EILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTI------RKAHIVSrsevthtlaERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd05585    76 INGGELfHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMD 503
Cdd:cd05585   156 GTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQE---PLRFPDGFDRDAKDLLIGLLNRD 232
                         250
                  ....*....|....*....
gi 1024249297 504 VDRR---GSAKELLQHPFL 519
Cdd:cd05585   233 PTKRlgyNGAQEIKNHPFF 251
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
267-519 1.60e-28

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: 115.06  E-value: 1.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTV----------YTALDIATGQEVaIKQMNLQQQPKK-----------------ELIINEILVMRE 319
Cdd:cd14199     3 QYKLKDEIGKGSYGVVklayneddntYYAMKVLSKKKL-MRQAGFPRRPPPrgaraapegctqprgpiERVYQEIAILKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 320 NKNPNIVNYLDSY--LVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM 397
Cdd:cd14199    82 LDHPNVVKLVEVLddPSEDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 398 DGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV--TRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNEnplRALYLI 474
Cdd:cd14199   162 DGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLseTRKIFsGKALDVWAMGVTLYCFVFGQCPFMDE---RILSLH 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1024249297 475 ATNGTPELQNPER--LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14199   239 SKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
271-520 2.00e-28

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: 115.54  E-value: 2.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEKI---GQGASGTVYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd06650     7 FEKIselGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAiRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETC-MDEGQIAAVCRECLQALDFL-HSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeQSKRSTMVG 424
Cdd:cd06650    87 GGSLDQVLKKAGrIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--DSMANSFVG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM----------------------VEGEP---PYLNENPLRALYLIATNGT 479
Cdd:cd06650   165 TRSYMSPERLQGTHYSVQSDIWSMGLSLVEMavgrypipppdakelelmfgcqVEGDAaetPPRPRTPGRPLSSYGMDSR 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 480 PEL-----------QNPERL-----SAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd06650   245 PPMaifelldyivnEPPPKLpsgvfSLEFQDFVNKCLIKNPAERADLKQLMVHAFIK 301
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
263-521 2.16e-28

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: 115.88  E-value: 2.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFE---KIGQGASGTVYTALDIATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVG 335
Cdd:cd05602     1 NPHAKPSDFHflkVIGKGSFGKVLLARHKSDEKFYAVKVLQkkaiLKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 DELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP 414
Cdd:cd05602    81 DKLYFVLDYINGGELfYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPERLSAVFRD 494
Cdd:cd05602   161 PNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNK---PLQLKPNITNSARH 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 495 FLNRCLEMDVDRRGSAK----ELLQHPFLKL 521
Cdd:cd05602   238 LLEGLLQKDRTKRLGAKddftEIKNHIFFSP 268
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
272-467 2.79e-28

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 118.74  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIINEILVMR---ENKN------PNIVNYLDsylVGDE---LW 339
Cdd:NF033483   13 ERIGRGGMAEVYLAKDTRLDRDVAVKVL------RPDLARDPEFVARfrrEAQSaaslshPNIVSVYD---VGEDggiPY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGGSLTDVVTEtcmdEG-----QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG---FCAQ 411
Cdd:NF033483   84 IVMEYVDGRTLKDYIRE----HGplspeEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiarALSS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 412 ITPEQSkrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENP 467
Cdd:NF033483  160 TTMTQT--NSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSP 213
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
274-520 3.63e-28

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: 113.42  E-value: 3.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd14117    14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVehqLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQiTPEQsKRSTMVGTPYWM 429
Cdd:cd14117    94 YKELQKHGrFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVH-APSL-RRRTMCGTLDYL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 430 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPERLSAVFRDFLNRCLEMDVDRRGS 509
Cdd:cd14117   172 PPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIV---KVDLKFPPFLSDGSRDLISKLLRYHPSERLP 248
                         250
                  ....*....|.
gi 1024249297 510 AKELLQHPFLK 520
Cdd:cd14117   249 LKGVMEHPWVK 259
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
267-521 4.07e-28

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: 114.82  E-value: 4.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLD------SYLVGDEL 338
Cdd:cd07850     1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSrpFQNVTHAKRAYRELVLMKLVNHKNIIGLLNvftpqkSLEEFQDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEyLAGGSLTDVVtETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSK 418
Cdd:cd07850    81 YLVME-LMDANLCQVI-QMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL-ARTAGTSFM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLG-IMAiEMVE---------------------GEPP-------------YL 463
Cdd:cd07850   158 MTPYVVTRYYRAPEVILGMGYKENVDIWSVGcIMG-EMIRgtvlfpgtdhidqwnkiieqlGTPSdefmsrlqptvrnYV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024249297 464 NENPLRALYLIA-----TNGTPELQNPERLSA-VFRDFLNRCLEMDVDRRGSAKELLQHPFLKL 521
Cdd:cd07850   237 ENRPKYAGYSFEelfpdVLFPPDSEEHNKLKAsQARDLLSKMLVIDPEKRISVDDALQHPYINV 300
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
267-518 4.45e-28

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: 113.57  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIK--QMNLQ-QQPKKELII----NEILVMRENKNPNIVNYLDSYLVG-DEL 338
Cdd:cd13990     1 RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKihQLNKDwSEEKKQNYIkhalREYEIHKSLDHPRIVKLYDVFEIDtDSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGGSLtDVVTETC--MDEGQIAAVCRECLQALDFL--HSNQVIHRDIKSDNILLG---MDGSVKLTDFGFCAQ 411
Cdd:cd13990    81 CTVLEYCDGNDL-DFYLKQHksIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHsgnVSGEIKITDFGLSKI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 412 ITPEQSKRSTM------VGTPYWMAPEVVTRKAYGP----KVDIWSLGIMAIEMVEGEPPY-LNENPLRalylIATNGTP 480
Cdd:cd13990   160 MDDESYNSDGMeltsqgAGTYWYLPPECFVVGKTPPkissKVDVWSVGVIFYQMLYGRKPFgHNQSQEA----ILEENTI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1024249297 481 ----ELQNPER--LSAVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd13990   236 lkatEVEFPSKpvVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
274-467 4.46e-28

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: 112.87  E-value: 4.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATgqeVAIKQMNLQQQPKKELII--NEILVMRENKNPNIVNYLdSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQLQAfkNEVAVLRKTRHVNILLFM-GYMTKPQLAIVTQWCEGSSLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT----PEQSKRSTmvGT 425
Cdd:cd14062    77 KHlhVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTrwsgSQQFEQPT--GS 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 426 PYWMAPEVVTRK---AYGPKVDIWSLGIMAIEMVEGEPPYLNENP 467
Cdd:cd14062   155 ILWMAPEVIRMQdenPYSFQSDVYAFGIVLYELLTGQLPYSHINN 199
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
274-519 4.47e-28

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: 113.35  E-value: 4.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIAT-----GQEVAIKQM---NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd14076     9 LGEGEFGKVKLGWPLPKanhrsGVQVAIKLIrrdTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTETCMDEGQIAavCR---ECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK-RST 421
Cdd:cd14076    89 SGGELFDYILARRRLKDSVA--CRlfaQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNGDlMST 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPE-VVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLN--ENP----LRALYLIATNgTPeLQNPERLSAVFR 493
Cdd:cd14076   167 SCGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPFDDdpHNPngdnVPRLYRYICN-TP-LIFPEYVTPKAR 244
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14076   245 DLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
263-518 4.59e-28

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: 114.00  E-value: 4.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMnLQQQPKKELIIN---EILVMRENKNPNIVNYL---------- 329
Cdd:cd07865     9 DEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKV-LMENEKEGFPITalrEIKILQLLKHENVVNLIeicrtkatpy 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 330 -----DSYLVgdelwvvMEY----LAGGSLTDVVTetcMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS 400
Cdd:cd07865    88 nrykgSIYLV-------FEFcehdLAGLLSNKNVK---FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 401 VKLTDFG----FCAQITPEQSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI 474
Cdd:cd07865   158 LKLADFGlaraFSLAKNSQPNRYTNRVVTLWYRPPELLLgERDYGPPIDMWGAGcIMA-EMWTRSPIMQGNTEQHQLTLI 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 475 AT---NGTPEL----------------QN-----PERLSAVFR-----DFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07865   237 SQlcgSITPEVwpgvdklelfkkmelpQGqkrkvKERLKPYVKdpyalDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
272-519 6.73e-28

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: 113.33  E-value: 6.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQmnLQQQPKKELIINeiLVMRENKNPNIVNYLDSY-----LVGDE-----LWVV 341
Cdd:cd14171    12 QKLGTGISGPVRVCVKKSTGERFALKI--LLDRPKARTEVR--LHMMCSGHPNIVQIYDVYansvqFPGESsprarLLIV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVT-ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFcAQItpEQS 417
Cdd:cd14171    88 MELMEGGELFDRISqHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGF-AKV--DQG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 KRSTMVGTPYWMAPEVV-----------------TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAL-------YL 473
Cdd:cd14171   165 DLMTPQFTPYYVAPQVLeaqrrhrkersgiptspTPYTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTItkdmkrkIM 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 474 IATNGTPElQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14171   245 TGSYEFPE-EEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
274-520 8.33e-28

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: 112.62  E-value: 8.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKgetMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 ---TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItPEQSKRSTMVGTPY 427
Cdd:cd05577    81 kyhIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEF-KGGKKIKGRVGTHG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRK-AYGPKVDIWSLGIMAIEMVEGEPPY------LNENPLRALYLiatngTPELQNPERLSAVFRDFLNRCL 500
Cdd:cd05577   160 YMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFrqrkekVDKEELKRRTL-----EMAVEYPDSFSPEARSLCEGLL 234
                         250       260
                  ....*....|....*....|....*
gi 1024249297 501 EMDVDRR-----GSAKELLQHPFLK 520
Cdd:cd05577   235 QKDPERRlgcrgGSADEVKEHPFFR 259
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
269-520 9.73e-28

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: 113.49  E-value: 9.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 269 TRFEKI---GQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIIN---------EILVMRENKNPNIVNYLDSYLVGD 336
Cdd:cd05574     1 DHFKKIkllGKGDVGRVYLVRLKGTGKLFAMKVL------DKEEMIKrnkvkrvltEREILATLDHPFLPTLYASFQTST 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTDVVTET---CMDEGQI---AAvcrECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF--GF 408
Cdd:cd05574    75 HLCFVMDYCPGGELFRLLQKQpgkRLPEEVArfyAA---EVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlSK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 CAQITP--------------------------EQSKRS-TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPP 461
Cdd:cd05574   152 QSSVTPppvrkslrkgsrrssvksieketfvaEPSARSnSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTP 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 462 YLNENPLRALYLIaTNGTPELQNPERLSAVFRDFLNRCLEMDVDRR-GS---AKELLQHPFLK 520
Cdd:cd05574   232 FKGSNRDETFSNI-LKKELTFPESPPVSSEAKDLIRKLLVKDPSKRlGSkrgASEIKRHPFFR 293
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
260-519 1.19e-27

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: 113.61  E-value: 1.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 260 SVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNlqqQPKKELI-----INEILVMRENKNPNIVNYLDSYLV 334
Cdd:cd07878     9 TVWEVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLS---RPFQSLIharrtYRELRLLKHMKHENVIGLLDVFTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 335 G------DELWVVMEyLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF 408
Cdd:cd07878    86 AtsienfNEVYLVTN-LMGADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 CAQITPEQSKrstMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEP-----PYLNEnpLRALYLIATNGTPEL 482
Cdd:cd07878   165 ARQADDEMTG---YVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKAlfpgnDYIDQ--LKRIMEVVGTPSPEV 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 483 -----------------QNPER-LSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07878   240 lkkisseharkyiqslpHMPQQdLKKIFRganplaiDLLEKMLVLDSDKRISASEALAHPYF 301
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
272-519 1.43e-27

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: 111.59  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK------KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd14196    11 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGS-----VKLTDFGFCAQITpEQSKR 419
Cdd:cd14196    91 SGGELFDFLAQKeSLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML-LDKNipiphIKLIDFGLAHEIE-DGVEF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPERLSAVFRDFLNR 498
Cdd:cd14196   169 KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANItAVSYDFDEEFFSHTSELAKDFIRK 248
                         250       260
                  ....*....|....*....|.
gi 1024249297 499 CLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14196   249 LLVKETRKRLTIQEALRHPWI 269
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
282-519 1.66e-27

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: 111.66  E-value: 1.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 282 VYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD-VVTETCM 359
Cdd:cd14088    17 IFRAKDKTTGKLYTCKKFLKRDGRKvRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDwILDQGYY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 360 DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG---MDGSVKLTDFGFcAQItpEQSKRSTMVGTPYWMAPEVVTR 436
Cdd:cd14088    97 SERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHL-AKL--ENGLIKEPCGTPEYLAPEVVGR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 437 KAYGPKVDIWSLGIMAIEMVEGEPPYLN-------ENPLRALYLIATNGTPELQNP--ERLSAVFRDFLNRCLEMDVDRR 507
Cdd:cd14088   174 QRYGRPVDCWAIGVIMYILLSGNPPFYDeaeeddyENHDKNLFRKILAGDYEFDSPywDDISQAAKDLVTRLMEVEQDQR 253
                         250
                  ....*....|..
gi 1024249297 508 GSAKELLQHPFL 519
Cdd:cd14088   254 ITAEEAISHEWI 265
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
267-519 2.09e-27

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: 111.98  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI--INEILVMR---ENKNPNIVNYLD---SYLVGDEL 338
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLstVREVALLKrleAFDHPNIVRLMDvcaTSRTDRET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WV--VMEYLAGGSLT--DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITP 414
Cdd:cd07863    81 KVtlVFEHVDQDLRTylDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGL-ARIYS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEP--------------------PYLNENPlRALYLI 474
Cdd:cd07863   160 CQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPlfcgnseadqlgkifdliglPPEDDWP-RDVTLP 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 475 ATNGTPELQNP-----ERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07863   239 RGAFSPRGPRPvqsvvPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
268-520 2.33e-27

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: 110.71  E-value: 2.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQM--NLQQQ----PKKELIINEILVMRE----NKNPNIVNYLDSYLVGDE 337
Cdd:cd14101     2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQIsrNRVQQwsklPGVNPVPNEVALLQSvgggPGHRGVIRLLDWFEIPEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEY-LAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM-DGSVKLTDFGFCAqiTP 414
Cdd:cd14101    82 FLLVLERpQHCQDLFDYITERgALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLrTGDIKLIDFGSGA--TL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-LNENPLRAlyliatngtpELQNPERLSAVF 492
Cdd:cd14101   160 KDSMYTDFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFeRDTDILKA----------KPSFNKRVSNDC 229
                         250       260
                  ....*....|....*....|....*...
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd14101   230 RSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
274-466 2.76e-27

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: 112.10  E-value: 2.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIINEILV---MRE-------NKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKIL------KKDVIIQDDDVectMVEkrvlalsGKPPFLTQLHSCFQTMDRLYFVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ-ITPEQSKRsT 421
Cdd:cd05587    78 YVNGGDLMyHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEgIFGGKTTR-T 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 466
Cdd:cd05587   157 FCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGED 201
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
268-520 2.87e-27

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: 110.86  E-value: 2.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVA---IKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAakfIKKRRLSSSRRgvsREEIEREVNILREIQHPNIITLHDIFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGSV-----KLTDFGFCAQITPE 415
Cdd:cd14195    87 LELVSGGELFDFLAEKeSLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIML-LDKNVpnpriKLIDFGIAHKIEAG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRStMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPERLSAVFRD 494
Cdd:cd14195   166 NEFKN-IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNIsAVNYDFDEEYFSNTSELAKD 244
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd14195   245 FIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
274-466 3.03e-27

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: 112.36  E-value: 3.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQkkviLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 428
Cdd:cd05604    84 LFfHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGTPEY 163
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 466
Cdd:cd05604   164 LAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRD 201
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
274-520 4.13e-27

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: 112.47  E-value: 4.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd05596    34 IGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSdsaFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TMVGTPYWM 429
Cdd:cd05596   114 VNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDGLVRSdTAVGTPDYI 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 430 APEVVTRKA----YGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPE--RLSAVFRDFLNRCLEMD 503
Cdd:cd05596   194 SPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADS-LVGTYGKIMNHKNSLQFPDdvEISKDAKSLICAFLTDR 272
                         250
                  ....*....|....*....
gi 1024249297 504 VDR--RGSAKELLQHPFLK 520
Cdd:cd05596   273 EVRlgRNGIEEIKAHPFFK 291
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
267-519 4.89e-27

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: 110.59  E-value: 4.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd07861     1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LA---GGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd07861    81 LSmdlKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYTH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTP---------ELQN------ 484
Cdd:cd07861   161 EVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIfRILGTPtediwpgvtSLPDykntfp 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 485 ---PERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07861   241 kwkKGSLRTAVKnldedglDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
272-520 5.03e-27

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: 110.89  E-value: 5.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAGGS- 349
Cdd:cd14174     8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGSi 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDFGF---------CAQI-TPEQ 416
Cdd:cd14174    88 LAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPdkvSPVKICDFDLgsgvklnsaCTPItTPEL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 skrSTMVGTPYWMAPEVV---TRKA--YGPKVDIWSLGIMAIEMVEGEPPYLNE----------NPLRA----LYLIATN 477
Cdd:cd14174   168 ---TTPCGSAEYMAPEVVevfTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgEVCRVcqnkLFESIQE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 478 GTPELQNPE--RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd14174   245 GKYEFPDKDwsHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
266-520 5.04e-27

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: 111.88  E-value: 5.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQM--NLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLV--GDELWV 340
Cdd:cd07852     7 RRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdAFRNATDAQRTFREIMFLQElNDHPNIIKLLNVIRAenDKDIYL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLAggslTD---VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:cd07852    87 VFEYME----TDlhaVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 KRSTMVGTPY----WM-APEV-VTRKAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI-ATNGTP------ELQ 483
Cdd:cd07852   163 DDENPVLTDYvatrWYrAPEIlLGSTRYTKGVDMWSVGcILG-EMLLGKPLFPGTSTLNQLEKIiEVIGRPsaedieSIQ 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297 484 NPERLSAVFR---------------------DFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd07852   242 SPFAATMLESlppsrpksldelfpkaspdalDLLKKLLVFNPNKRLTAEEALRHPYVA 299
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
267-519 5.62e-27

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: 109.71  E-value: 5.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFE-KIGQGASGTVYTALDIATGQEVAIKQMNLQQ--QPKKELIINEILVMRENKNPNIVNYLDSY---LVGDELWV 340
Cdd:cd14033     1 RFLKFNiEIGRGSFKTVYRGLDTETTVEVAWCELQTRKlsKGERQRFSEEVEMLKGLQHPNIVRFYDSWkstVRGHKCII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 -VMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSN--QVIHRDIKSDNILL-GMDGSVKLTDFGFCAqiTPE 415
Cdd:cd14033    81 lVTELMTSGTLKTYLKRfREMKLKLLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFItGPTGSVKIGDLGLAT--LKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPYWMAPEVVTRKaYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTP-----ELQNPErlsa 490
Cdd:cd14033   159 ASFAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSGIKpdsfyKVKVPE---- 233
                         250       260
                  ....*....|....*....|....*....
gi 1024249297 491 vFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14033   234 -LKEIIEGCIRTDKDERFTIQDLLEHRFF 261
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
267-519 6.26e-27

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: 110.66  E-value: 6.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI--INEILVMRENKNPNIVNYLDsyLVGDE------- 337
Cdd:cd07864     8 KFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItaIREIKILRQLNHRSVVNLKE--IVTDKqdaldfk 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 -----LWVVMEY----LAGGSLTDVVTetcMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF 408
Cdd:cd07864    86 kdkgaFYLVFEYmdhdLMGLLESGLVH---FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 cAQITPEQSKR--STMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA-TNGTP---- 480
Cdd:cd07864   163 -ARLYNSEESRpyTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISrLCGSPcpav 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 481 ---------------ELQNPERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07864   242 wpdviklpyfntmkpKKQYRRRLREEFSfiptpalDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
267-462 8.68e-27

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: 109.29  E-value: 8.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQ------QQPKKELIIneilvMRENKNPNIVNYLDSYLVGDELWV 340
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPksssavEDSRKEAVL-----LAKMKHPNIVAFKESFEADGHLYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:cd08219    76 VMEYCDGGDLMQKIKLQrgkLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGA 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 418 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd08219   156 YACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPF 200
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
267-518 1.04e-26

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: 108.92  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd14665     1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIE-RGEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgmDGS----VKLTDFGFCAQITPEQSKRST 421
Cdd:cd14665    80 GGELFERICNAGrFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL--DGSpaprLKICDFGYSKSSVLHSQPKST 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 mVGTPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGTPELQNPE--RLSAVFRDFLN 497
Cdd:cd14665   158 -VGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDpEEPRNFRKTIQRILSVQYSIPDyvHISPECRHLIS 236
                         250       260
                  ....*....|....*....|.
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14665   237 RIFVADPATRITIPEIRNHEW 257
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
264-519 1.18e-26

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: 109.43  E-value: 1.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFE-KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSY---LVGDE 337
Cdd:cd14031     7 PGGRFLKFDiELGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQqrFKEEAEMLKGLQHPNIVRFYDSWesvLKGKK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWV-VMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILL-GMDGSVKLTDFGFCAQI 412
Cdd:cd14031    87 CIVlVTELMTSGTLKTYLKRfKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFItGPTGSVKIGDLGLATLM 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQSKrsTMVGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVF 492
Cdd:cd14031   167 RTSFAK--SVIGTPEFMAPEMY-EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTDPEV 243
                         250       260
                  ....*....|....*....|....*..
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14031   244 KEIIEGCIRQNKSERLSIKDLLNHAFF 270
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
274-520 1.29e-26

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: 110.51  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEliinEILVMRENKnpnivnylDSYLVGDELWV------------- 340
Cdd:cd05597     9 IGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRA----ETACFREER--------DVLVNGDRRWItklhyafqdenyl 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 --VMEYLAGGSL-------TDVVTETcMDEGQIAavcrECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ 411
Cdd:cd05597    77 ylVMDYYCGGDLltllskfEDRLPEE-MARFYLA----EMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 412 ITPEQSKRSTM-VGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNP 485
Cdd:cd05597   152 LREDGTVQSSVaVGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAES-LVETYGKIMNHKEHFSFP 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1024249297 486 ---ERLSAVFRDFLNRcLEMDVDRR---GSAKELLQHPFLK 520
Cdd:cd05597   231 ddeDDVSEEAKDLIRR-LICSRERRlgqNGIDDFKKHPFFE 270
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
268-520 1.46e-26

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: 110.53  E-value: 1.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQM----NLQQQPKKELiiNEILVMRENKNPNIVNYLD------SYLVGDE 337
Cdd:cd07855     7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIpnafDVVTTAKRTL--RELKILRHFKHDNIIAIRDilrpkvPYADFKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEyLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF--CAQITP 414
Cdd:cd07855    85 VYVVLD-LMESDLHHIIhSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMarGLCTSP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKR--STMVGTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN-GTPE--------- 481
Cdd:cd07855   164 EEHKYfmTEYVATRWYRAPELMlSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVlGTPSqavinaiga 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 482 ------LQN-----PERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd07855   244 drvrryIQNlpnkqPVPWETLYPkadqqalDLLSQMLRFDPSERITVAEALQHPFLA 300
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
274-516 1.96e-26

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: 107.96  E-value: 1.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKelIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRS--FLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 VTEtcMDE----GQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVK---LTDFGFCAQI------TPEQSKRS 420
Cdd:cd14065    79 LKS--MDEqlpwSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMpdektkKPDRKKRL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM---VEGEPPYLnenPLRALYLIATNGTPELQN---PERlsavFRD 494
Cdd:cd14065   157 TVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIigrVPADPDYL---PRTMDFGLDVRAFRTLYVpdcPPS----FLP 229
                         250       260
                  ....*....|....*....|..
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQH 516
Cdd:cd14065   230 LAIRCCQLDPEKRPSFVELEHH 251
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
281-523 2.17e-26

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 109.96  E-value: 2.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 281 TVYTALDIATGQEVAIKQMNLQQQPKKELII--NEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS----LTDVV 354
Cdd:cd08226    15 SVYLARHTPTGTLVTVKITNLDNCSEEHLKAlqNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSarglLKTYF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 355 TETcMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF-GFCAQITPEQSKR--------STMVgT 425
Cdd:cd08226    95 PEG-MNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLsHLYSMVTNGQRSKvvydfpqfSTSV-L 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PyWMAPEVVTRKAYG--PKVDIWSLGIMAIEMVEGEPPYLN-----------ENPLRALYLIA----------------- 475
Cdd:cd08226   173 P-WLSPELLRQDLHGynVKSDIYSVGITACELARGQVPFQDmrrtqmllqklKGPPYSPLDIFpfpelesrmknsqsgmd 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024249297 476 --------------TNGTPELQNP--ERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAK 523
Cdd:cd08226   252 sgigesvatssmtrTMTSERLQTPssKTFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFKQVK 315
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
338-520 2.33e-26

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: 109.41  E-value: 2.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ 416
Cdd:cd05582    72 LYLILDFLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHE 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI--ATNGTPELQNPER---LSAV 491
Cdd:cd05582   152 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMIlkAKLGMPQFLSPEAqslLRAL 231
                         170       180       190
                  ....*....|....*....|....*....|
gi 1024249297 492 F-RDFLNRcLEMDVDrrgSAKELLQHPFLK 520
Cdd:cd05582   232 FkRNPANR-LGAGPD---GVEEIKRHPFFA 257
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
267-518 3.00e-26

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: 107.55  E-value: 3.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd14662     1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYIE-RGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgmDGS----VKLTDFGFCAQITPEQSKRST 421
Cdd:cd14662    80 GGELFERICNAGrFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL--DGSpaprLKICDFGYSKSSVLHSQPKST 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 mVGTPYWMAPEVVTRKAYGPKV-DIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNGTPELQNPE--RLSAVFRDFLN 497
Cdd:cd14662   158 -VGTPAYIAPEVLSRKEYDGKVaDVWSCGVTLYVMLVGAYPFEDpDDPKNFRKTIQRIMSVQYKIPDyvRVSQDCRHLLS 236
                         250       260
                  ....*....|....*....|.
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14662   237 RIFVANPAKRITIPEIKNHPW 257
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
274-520 3.08e-26

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: 110.87  E-value: 3.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEliinEILVMRENKNPnIVN----YLDS--YLVGDE--LWVVMEYL 345
Cdd:cd05624    80 IGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRA----ETACFREERNV-LVNgdcqWITTlhYAFQDEnyLYLVMDYY 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVT--ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM- 422
Cdd:cd05624   155 VGGDLLTLLSkfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQSSVa 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRK-----AYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPERLSAV---FRD 494
Cdd:cd05624   235 VGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAES-LVETYGKIMNHEERFQFPSHVTDVseeAKD 313
                         250       260
                  ....*....|....*....|....*...
gi 1024249297 495 FLNRCLEMDVDRRGS--AKELLQHPFLK 520
Cdd:cd05624   314 LIQRLICSRERRLGQngIEDFKKHAFFE 341
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
268-519 3.57e-26

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: 110.10  E-value: 3.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIIN---EILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05626     3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHvkaERDILAEADNEWVVKLYYSFQDKDNLYFVMDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETCMDEGQIAAV-CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA------------- 410
Cdd:cd05626    83 IPGGDMMSLLIRMEVFPEVLARFyIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTgfrwthnskyyqk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 -------------------------------QITPEQSKR---STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 456
Cdd:cd05626   163 gshirqdsmepsdlwddvsncrcgdrlktleQRATKQHQRclaHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEML 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 457 EGEPPYLNENPLRA-LYLIATNGTPELQNPERLSAVFRDFLNR--CLEMDVDRRGSAKELLQHPFL 519
Cdd:cd05626   243 VGQPPFLAPTPTETqLKVINWENTLHIPPQVKLSPEAVDLITKlcCSAEERLGRNGADDIKAHPFF 308
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
274-464 3.93e-26

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: 108.08  E-value: 3.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLD-----SYLVGDELWVVMEYLAG 347
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKnKDRWCHEIQIMKKLNHPNVVKACDvpeemNFLVNDVPLLAMEYCSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVT--ETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSV---KLTDFGFcAQITPEQSKRS 420
Cdd:cd14039    81 GDLRKLLNkpENCcgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKivhKIIDLGY-AKDLDQGSLCT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1024249297 421 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN 464
Cdd:cd14039   160 SFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLH 203
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
242-520 4.08e-26

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: 110.48  E-value: 4.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 242 KKSKMTDEEILEKLRSIVSVGDPKKKYTRFEK---IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEIL 315
Cdd:cd05622    46 RKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVvkvIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsaFFWEERD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 316 VMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL 395
Cdd:cd05622   126 IMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 396 GMDGSVKLTDFGFCAQITPEQSKR-STMVGTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMVEGEPPYLNENpLRA 470
Cdd:cd05622   206 DKSGHLKLADFGTCMKMNKEGMVRcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADS-LVG 284
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1024249297 471 LYLIATNGTPELQNPERlSAVFRDFLNRCLEMDVDR-----RGSAKELLQHPFLK 520
Cdd:cd05622   285 TYSKIMNHKNSLTFPDD-NDISKEAKNLICAFLTDRevrlgRNGVEEIKRHLFFK 338
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
268-516 5.91e-26

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: 107.38  E-value: 5.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGD-----ELWVVM 342
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIVKEaggkkEVYLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVtETCMDEG------QIAAVCRECLQALDFLHSNQ---VIHRDIKSDNILLGMDGSVKLTDFGFC--AQ 411
Cdd:cd13986    82 PYYKRGSLQDEI-ERRLVKGtffpedRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLSEDDEPILMDLGSMnpAR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 412 ITPEQSKRSTMV-------GTPYWMAPEVVTRKAYG---PKVDIWSLGIMAIEMVEGEPPY-LNENPLRALYLIATNGTP 480
Cdd:cd13986   161 IEIEGRREALALqdwaaehCTMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPFeRIFQKGDSLALAVLSGNY 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1024249297 481 ELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQH 516
Cdd:cd13986   241 SFPDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
267-519 6.45e-26

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: 108.43  E-value: 6.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlqQQPKKELII-----NEILVMRENKNPNIVNYLDSYLVGDE-LWV 340
Cdd:cd07856    11 RYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKI---MKPFSTPVLakrtyRELKLLKHLRHENIISLSDIFISPLEdIYF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEyLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQItpEQSKRS 420
Cdd:cd07856    88 VTE-LLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGL-ARI--QDPQMT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMVEGEPPY---------------LNENPLRALYLIATNGTPELQN 484
Cdd:cd07856   164 GYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFpgkdhvnqfsiitelLGTPPDDVINTICSENTLRFVQ 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249297 485 --PER----LSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07856   244 slPKRervpFSEKFKnadpdaiDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
268-519 7.23e-26

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: 106.51  E-value: 7.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRAR-AFQERDILARLSHRRLTCLLDQFETRKTLILILELCSS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL--GMDGSVKLTDFGFCAQITPEQSKRSTMvG 424
Cdd:cd14107    83 EELLDrLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQFSKY-G 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQNPE--RLSAVFRDFLNRCLEM 502
Cdd:cd14107   162 SPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGEND-RATLLNVAEGVVSWDTPEitHLSEDAKDFIKRVLQP 240
                         250
                  ....*....|....*..
gi 1024249297 503 DVDRRGSAKELLQHPFL 519
Cdd:cd14107   241 DPEKRPSASECLSHEWF 257
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
264-467 8.03e-26

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 106.45  E-value: 8.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd14111     1 PQKPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAE-EKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGS-LTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR-ST 421
Cdd:cd14111    80 FCSGKElLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQlGR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENP 467
Cdd:cd14111   160 RTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDP 205
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
250-519 1.00e-25

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: 106.96  E-value: 1.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 250 EILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDiATGQEVAIKqmnlqqqpKKELIINEILVMRENKNPnivnyl 329
Cdd:cd14200    31 KVLSKKKLLKQYGFPRRPPPRGSKAAQGEQAKPLAPLE-RVYQEIAIL--------KKLDHVNIVKLIEVLDDP------ 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 330 dsylVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC 409
Cdd:cd14200    96 ----AEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 410 AQITPEQSKRSTMVGTPYWMAPEVV--TRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLrALYLIATNGTPELQNPE 486
Cdd:cd14200   172 NQFEGNDALLSSTAGTPAFMAPETLsdSGQSFsGKALDVWAMGVTLYCFVYGKCPFIDEFIL-ALHNKIKNKPVEFPEEP 250
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1024249297 487 RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14200   251 EISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
272-515 1.00e-25

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: 105.99  E-value: 1.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIK--QMNLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKtcRETLPPDLKRKFL-QEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVV--TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ-ITPEQSKRSTMVGTP 426
Cdd:cd05041    80 LLTFLrkKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREeEDGEYTVSDGLKQIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 427 Y-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGtpELQNPERLSAVFRDFLNRCLEMDV 504
Cdd:cd05041   160 IkWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQTREQIESGY--RMPAPELCPEAVYRLMLQCWAYDP 237
                         250
                  ....*....|.
gi 1024249297 505 DRRGSAKELLQ 515
Cdd:cd05041   238 ENRPSFSEIYN 248
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
274-466 1.15e-25

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: 107.78  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDS-YLVGDELWVVMEYLAGGS 349
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKILKkdvVIQDDDVECTMVEKRVLALSGKPPFLTQLHScFQTMDRLYFVMEYVNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 428
Cdd:cd05616    88 LMYHIQQVGrFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDY 167
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 466
Cdd:cd05616   168 IAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGED 205
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
274-456 1.54e-25

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: 106.18  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 V--TETCMDEgQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ--------------- 416
Cdd:cd14222    81 LraDDPFPWQ-QKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKkkpppdkpttkkrtl 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 417 -----SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 456
Cdd:cd14222   160 rkndrKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
263-521 1.96e-25

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 109.57  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE-------------------LIINEILVMRENKNP 323
Cdd:PTZ00283   29 EQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADknraqaevccllncdffsiVKCHEDFAKKDPRNP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 324 NIVNYLDsylvgdelwVVMEYLAGGSLTDVV-----TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD 398
Cdd:PTZ00283  109 ENVLMIA---------LVLDYANAGDLRQEIksrakTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSN 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 399 GSVKLTDFGF----CAQITPEQSKrsTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI 474
Cdd:PTZ00283  180 GLVKLGDFGFskmyAATVSDDVGR--TFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKT 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1024249297 475 ATNGTPELqnPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKL 521
Cdd:PTZ00283  258 LAGRYDPL--PPSISPEMQEIVTALLSSDPKRRPSSSKLLNMPICKL 302
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
249-520 2.08e-25

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: 108.16  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 249 EEILEKLRSIVSVGDpkkKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNI 325
Cdd:cd05621    38 EKIVNKIRELQMKAE---DYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSdsaFFWEERDIMAFANSPWV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 326 VNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTD 405
Cdd:cd05621   115 VQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLAD 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 406 FGFCAQITPEQSKR-STMVGTPYWMAPEVVTRKA----YGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTP 480
Cdd:cd05621   195 FGTCMKMDETGMVHcDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADS-LVGTYSKIMDHKN 273
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 481 ELQNPE--RLSAVFRDFLNRCL---EMDVDRRGsAKELLQHPFLK 520
Cdd:cd05621   274 SLNFPDdvEISKHAKNLICAFLtdrEVRLGRNG-VEEIKQHPFFR 317
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
215-544 2.10e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 109.34  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 215 VPNKEVTPPSAenanSSTLYRNTDRQRKKSKMTDEEILEK---------LRSIVSV---------GDPKKK-YTRFEKIG 275
Cdd:PTZ00267    1 MPNNEVEHGSA----SAELLNQYAKYFPHVLFTSEEAFEKycadldpeaYKKCVDLpegeevpesNNPREHmYVLTTLVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 276 QGASGTVYTALDIA-TGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVV 354
Cdd:PTZ00267   77 RNPTTAAFVATRGSdPKEKVVAKFVMLNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 355 TETCMD-----EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS--KRSTMVGTPY 427
Cdd:PTZ00267  157 KQRLKEhlpfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSldVASSFCGTPY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPerLSAVFRDFLNRCLEMDVDRR 507
Cdd:PTZ00267  237 YLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDPFPCP--VSSGMKALLDPLLSKNPALR 314
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1024249297 508 GSAKELLQHPFLKLakpLSSLTPLIIAAKEAIKNSSR 544
Cdd:PTZ00267  315 PTTQQLLHTEFLKY---VANLFQDIVRHSETISPHDR 348
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
265-519 2.18e-25

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: 108.56  E-value: 2.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEliinEILVMRENKNPnIVNYlDS-------YLVGDE 337
Cdd:cd05623    71 KEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRA----ETACFREERDV-LVNG-DSqwittlhYAFQDD 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 --LWVVMEYLAGGSLTDVVT--ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 413
Cdd:cd05623   145 nnLYLVMDYYVGGDLLTLLSkfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLM 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 414 PEQSKRSTM-VGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIATNGTPELQNPER 487
Cdd:cd05623   225 EDGTVQSSVaVGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAES-LVETYGKIMNHKERFQFPTQ 303
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1024249297 488 LSAV---FRDFLNRCLEMDVDRRGS--AKELLQHPFL 519
Cdd:cd05623   304 VTDVsenAKDLIRRLICSREHRLGQngIEDFKNHPFF 340
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
274-466 2.72e-25

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: 107.00  E-value: 2.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMN---LQQQPKKELIINEILVMRENKNPNIVNYLDS-YLVGDELWVVMEYLAGGS 349
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKkdvVIQDDDVECTMVEKRVLALQDKPPFLTQLHScFQTVDRLYFVMEYVNGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYW 428
Cdd:cd05615    98 LMYHIQQVGkFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTTRTFCGTPDY 177
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 466
Cdd:cd05615   178 IAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGED 215
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
69-126 2.92e-25

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 98.54  E-value: 2.92e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297  69 EISLPSDFEHTIHVGFDAVTGEFTGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFY 126
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFTGLPPEWAKLLDSSGITEDEQKENPKAVLDVLKFY 58
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
268-455 2.96e-25

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: 105.53  E-value: 2.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKI---GQGASGTVYTALDIATGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd14046     5 LTDFEELqvlGKGAFGQVVKVRNKLDGRYYAIKKIKLRsESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG-----FCAQITPEQS 417
Cdd:cd14046    85 YCEKSTLRDLIDSgLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGlatsnKLNVELATQD 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 418 KRST-------------MVGTPYWMAPEVV--TRKAYGPKVDIWSLGIMAIEM 455
Cdd:cd14046   165 INKStsaalgssgdltgNVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIFFEM 217
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
266-460 3.02e-25

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: 105.50  E-value: 3.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQE-VAIKQMNLQQQPKKELI--INEILVMRE---NKNPNIVNYLDSYLVG---- 335
Cdd:cd07862     1 QQYECVAEIGEGAYGKVFKARDLKNGGRfVALKRVRVQTGEEGMPLstIREVAVLRHletFEHPNVVRLFDVCTVSrtdr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 -DELWVVMEYLAGGSLT--DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQI 412
Cdd:cd07862    81 eTKLTLVFEHVDQDLTTylDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGL-ARI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249297 413 TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEP 460
Cdd:cd07862   160 YSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKP 207
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
273-513 3.04e-25

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: 104.90  E-value: 3.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILvmrenKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 352
Cdd:cd13991    13 RIGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACAGL-----TSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS-VKLTDFGFCAQITPEQSKRSTMV-----GT 425
Cdd:cd13991    88 LIKEQgCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSdAFLCDFGHAECLDPDGLGKSLFTgdyipGT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVD 505
Cdd:cd13991   168 ETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPPLREIPPSCAPLTAQAIQAGLRKEPV 247

                  ....*...
gi 1024249297 506 RRGSAKEL 513
Cdd:cd13991   248 HRASAAEL 255
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
266-519 3.21e-25

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: 106.62  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN-LQQQPKKELIINEILVMRENKNPNIVNYLD-----SYLVGDELW 339
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpFEHQTYCLRTLREIKILLRFKHENIIGILDiqrppTFESFKDVY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAggslTD---VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQ 416
Cdd:cd07849    85 IVQELME----TDlykLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGL-ARIADPE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTM----VGTPYWMAPEV-VTRKAYGPKVDIWSLG-IMAiEMVEGEPPYLNENPLRALYLI-ATNGTP---ELQNPE 486
Cdd:cd07849   160 HDHTGFlteyVATRWYRAPEImLNSKGYTKAIDIWSVGcILA-EMLSNRPLFPGKDYLHQLNLIlGILGTPsqeDLNCII 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 487 RLSA-----------------VFR-------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07849   239 SLKArnyikslpfkpkvpwnkLFPnadpkalDLLDKMLTFNPHKRITVEEALAHPYL 295
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
264-514 3.40e-25

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: 105.14  E-value: 3.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTAldiATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVV 341
Cdd:cd14151     6 PDGQITVGQRIGSGSFGTVYKG---KWHGDVAVKMLNVTAPTPQQLqaFKNEVGVLRKTRHVNILLFM-GYSTKPQLAIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQS-- 417
Cdd:cd14151    82 TQWCEGSSLYHHlhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL-ATVKSRWSgs 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 -KRSTMVGTPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQN-----PE 486
Cdd:cd14151   161 hQFEQLSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGylSPDLSKvrsncPK 240
                         250       260
                  ....*....|....*....|....*...
gi 1024249297 487 RLSAVFRDflnrCLEMDVDRRGSAKELL 514
Cdd:cd14151   241 AMKRLMAE----CLKKKRDERPLFPQIL 264
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-520 3.56e-25

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: 106.54  E-value: 3.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIA---TGQEVAIKQMN----LQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd05614     8 LGTGAYGKVFLVRKVSghdANKLYAMKVLRkaalVQKAKTVEHTRTERNVLEHvRQSPFLVTLHYAFQTDAKLHLILDYV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TMV 423
Cdd:cd05614    88 SGGELfTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEKERTySFC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNE---NPLRALYLIATNGTPELqnPERLSAVFRDFLNRC 499
Cdd:cd05614   168 GTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTLEgekNTQSEVSRRILKCDPPF--PSFIGPVARDLLQKL 245
                         250       260
                  ....*....|....*....|....*.
gi 1024249297 500 LEMDVDRR-GS----AKELLQHPFLK 520
Cdd:cd05614   246 LCKDPKKRlGAgpqgAQEIKEHPFFK 271
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
272-519 4.04e-25

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: 105.11  E-value: 4.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEYLAGGS- 349
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGGSi 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD---GSVKLTDF---------GFCAQI-TPEQ 416
Cdd:cd14173    88 LSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPnqvSPVKICDFdlgsgiklnSDCSPIsTPEL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 skrSTMVGTPYWMAPEVV-----TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE----------NPLRA----LYLIATN 477
Cdd:cd14173   168 ---LTPCGSAEYMAPEVVeafneEASIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgEACPAcqnmLFESIQE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 478 GTPELqnPER----LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14173   245 GKYEF--PEKdwahISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
274-519 4.60e-25

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: 104.69  E-value: 4.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQmnLQQQPKKELIINeiLVMRENKNPNIVNYLDSY---LVGDE-LWVVMEYLAGGS 349
Cdd:cd14172    12 LGLGVNGKVLECFHRRTGQKCALKL--LYDSPKARREVE--HHWRASGGPHIVHILDVYenmHHGKRcLLIIMECMEGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFcAQITPEQSKRSTMV 423
Cdd:cd14172    88 LFSRIQErgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSkekDAVLKLTDFGF-AKETTVQNALQTPC 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNeNPLRALYLIATN----GTPELQNPE--RLSAVFRDFLN 497
Cdd:cd14172   167 YTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYS-NTGQAISPGMKRrirmGQYGFPNPEwaEVSEEAKQLIR 245
                         250       260
                  ....*....|....*....|..
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14172   246 HLLKTDPTERMTITQFMNHPWI 267
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
272-507 5.23e-25

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: 105.11  E-value: 5.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQM---NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd08229    30 KKIGRGQFSEVYRATCLLDGVPVALKKVqifDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVV-----TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd08229   110 DLSRMIkhfkkQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLV 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE--NPLRALYLIATNGTPELQNpERLSAVFRDFLNRCLE 501
Cdd:cd08229   190 GTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDkmNLYSLCKKIEQCDYPPLPS-DHYSEELRQLVNMCIN 268

                  ....*.
gi 1024249297 502 MDVDRR 507
Cdd:cd08229   269 PDPEKR 274
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
267-518 5.43e-25

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: 104.82  E-value: 5.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQ----PKKELiiNEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDdegvPSSAL--REICLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYlaggslTDVVTETCMD--EGQI-AAVCR----ECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 415
Cdd:cd07839    79 EY------CDQDLKKYFDscNGDIdPEIVKsfmfQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLN----ENPLRALYLIAtnGTPELQN------ 484
Cdd:cd07839   153 VRCYSAEVVTLWYRPPDVLFgAKLYSTSIDMWSAGCIFAELANAGRPLFPgndvDDQLKRIFRLL--GTPTEESwpgvsk 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 485 -PE------------------RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07839   231 lPDykpypmypattslvnvvpKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
267-520 6.22e-25

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: 104.56  E-value: 6.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGA-DQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS--VKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd14104    80 GVDIFERITTARfeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGsyIKIIEFGQSRQLKPGDKFRLQY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VgTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT-NGTPELQNPERLSAVFRDFLNRCLE 501
Cdd:cd14104   160 T-SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNaEYAFDDEAFKNISIEALDFVDRLLV 238
                         250
                  ....*....|....*....
gi 1024249297 502 MDVDRRGSAKELLQHPFLK 520
Cdd:cd14104   239 KERKSRMTAQEALNHPWLK 257
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
242-520 6.63e-25

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: 104.75  E-value: 6.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 242 KKSKMTDEeiLEKLRSIVSVGDPKKKYTRFE-KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE--LIINEILVMR 318
Cdd:cd14030     2 ERNKQQDE--IEELETKAVG*SPDGRFLKFDiEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSErqRFKEEAGMLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 319 ENKNPNIVNYLDSY---LVGDELWV-VMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSD 391
Cdd:cd14030    80 GLQHPNIVRFYDSWestVKGKKCIVlVTELMTSGTLKTYLKRfKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 392 NILL-GMDGSVKLTDFGFCAqiTPEQSKRSTMVGTPYWMAPEVVTRKaYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRA 470
Cdd:cd14030   160 NIFItGPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSECQNAAQ 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 471 LYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd14030   237 IYRRVTSGVKPASFDKVAIPEVKEIIEGCIRQNKDERYAIKDLLNHAFFQ 286
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
266-519 7.79e-25

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: 105.75  E-value: 7.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLD---SYLVGDEL-- 338
Cdd:cd07879    15 ERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSrpFQSEIFAKRAYRELTLLKHMQHENVIGLLDvftSAVSGDEFqd 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 -WVVMEYLaggsLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 415
Cdd:cd07879    95 fYLVMPYM----QTDLqkIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKrstMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPERL----- 488
Cdd:cd07879   171 MTG---YVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQIlKVTGVPGPEFVQKLedkaa 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 489 ----------------------SAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07879   248 ksyikslpkyprkdfstlfpkaSPQAVDLLEKMLELDVDKRLTATEALEHPYF 300
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
265-520 7.87e-25

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: 105.80  E-value: 7.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDEL---- 338
Cdd:cd07880    14 PDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYrpFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfh 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 --WVVMEYLaGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQitpEQ 416
Cdd:cd07880    94 dfYLVMPFM-GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQ---TD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTPELQNPERLSAV--- 491
Cdd:cd07880   170 SEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMeIMKVTGTPSKEFVQKLQSEdak 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 492 ----------FRDF--------------LNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd07880   250 nyvkklprfrKKDFrsllpnanplavnvLEKMLVLDAESRITAAEALAHPYFE 302
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
274-515 9.63e-25

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: 104.13  E-value: 9.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDEL-------WVVMEYL 345
Cdd:cd14036     8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKlSGHPNIVQFCSAASIGKEEsdqgqaeYLLLTEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTE----TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFGFCAQI--TPEQS 417
Cdd:cd14036    88 CKGQLVDFVKKveapGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEahYPDYS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 ----KRS------TMVGTPYWMAPEVV---TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALyliatNGTPELQN 484
Cdd:cd14036   168 wsaqKRSlvedeiTRNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFEDGAKLRII-----NAKYTIPP 242
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 485 PERLSAVFRDFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd14036   243 NDTQYTVFHDLIRSTLKVNPEERLSITEIVE 273
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
273-463 1.08e-24

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: 103.89  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLD-----SYLVGDEL-WVVMEYL 345
Cdd:cd14038     1 RLGTGGFGNVLRWINQETGEQVAIKQCRQELSPKnRERWCLEIQIMKRLNHPNVVAARDvpeglQKLAPNDLpLLAMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVT--ETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL--GMDGSV-KLTDFGFCAQItpEQSK 418
Cdd:cd14038    81 QGGDLRKYLNqfENCcgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLqqGEQRLIhKIIDLGYAKEL--DQGS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 419 RST-MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL 463
Cdd:cd14038   159 LCTsFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
267-519 1.11e-24

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: 105.12  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNlqqQPKKELI-----INEILVMRENKNPNIVNYLDSYLVG------ 335
Cdd:cd07877    18 RYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLS---RPFQSIIhakrtYRELRLLKHMKHENVIGLLDVFTPArsleef 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 DELWVVMeYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 415
Cdd:cd07877    95 NDVYLVT-HLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKrstMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT-NGTPELQNPERLSA--- 490
Cdd:cd07877   174 MTG---YVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRlVGTPGAELLKKISSesa 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 491 -----------------VF-------RDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07877   251 rnyiqsltqmpkmnfanVFiganplaVDLLEKMLVLDSDKRITAAQALAHAYF 303
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
268-519 1.29e-24

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: 103.13  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14113     9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVN-KKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS---VKLTDFGFCAQI--TPEQSKrst 421
Cdd:cd14113    88 GRLLDyVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLntTYYIHQ--- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPER----LSAVFRDFLN 497
Cdd:cd14113   165 LLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNIC---RLDFSFPDDyfkgVSQKAKDFVC 241
                         250       260
                  ....*....|....*....|..
gi 1024249297 498 RCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14113   242 FLLQMDPAKRPSAALCLQEQWL 263
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
274-523 2.82e-24

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. 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. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 103.87  E-value: 2.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASG--TVYTALDIATGQEVAIKQMNLQQQPKK--ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd08227     6 IGRGFEDlmTVNLARYKPTGEYVTVRRINLEACTNEmvTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTETCMD---EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLT---------DFGFCAQITPEQS 417
Cdd:cd08227    86 AKDLICTHFMDgmsELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSglrsnlsmiNHGQRLRVVHDFP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 KRSTMVgTPyWMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPYlNENPLRALYLIATNGT---------------- 479
Cdd:cd08227   166 KYSVKV-LP-WLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPF-KDMPATQMLLEKLNGTvpclldtttipaeelt 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 480 --------------------PELQNPE--------RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAK 523
Cdd:cd08227   243 mkpsrsgansglgesttvstPRPSNGEssshpynrTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIK 314
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
272-516 3.31e-24

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: 102.03  E-value: 3.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTAldIATGQEVAIKQMnlQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd14147     9 EVIGIGGFGKVYRG--SWRGELVAVKAA--RQDPDEDISVTAESVRQEARlfamlaHPNIIALKAVCLEEPNLCLVMEYA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQ---VIHRDIKSDNILLGMDG--------SVKLTDFGFCAQItp 414
Cdd:cd14147    85 AGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIenddmehkTLKITDFGLAREW-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTpELQNPERLSAVFRD 494
Cdd:cd14147   163 HKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKL-TLPIPSTCPEPFAQ 241
                         250       260
                  ....*....|....*....|..
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQH 516
Cdd:cd14147   242 LMADCWAQDPHRRPDFASILQQ 263
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
262-518 3.73e-24

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: 103.01  E-value: 3.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 262 GDPKKkYTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlqqQP-KKELIINEILVMRE-NKNPNIVNYLDsyLVGDELW 339
Cdd:cd14132    15 GSQDD-YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL----KPvKKKKIKREIKILQNlRGGPNIVKLLD--VVKDPQS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 ----VVMEYLAG-------GSLTDvvtetcMDegqIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDG-SVKLTDFG 407
Cdd:cd14132    88 ktpsLIFEYVNNtdfktlyPTLTD------YD---IRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKrKLRLIDWG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 408 FCAQITPEQsKRSTMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATN-GTPELQN 484
Cdd:cd14132   159 LAEFYHPGQ-EYNVRVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPFFHgHDNYDQLVKIAKVlGTDDLYA 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 485 ---------PERLSAVFR------------------------DFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd14132   238 yldkygielPPRLNDILGrhskkpwerfvnsenqhlvtpealDLLDKLLRYDHQERITAKEAMQHPY 304
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
267-517 4.82e-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: 101.73  E-value: 4.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDI-ATGQEVAIKQM--NLQQQPKKELIINEILVMRENKN---PNIVNYLDSYLVGDELWV 340
Cdd:cd14052     1 RFANVELIGSGEFSQVYKVSERvPTGKVYAVKKLkpNYAGAKDRLRRLEEVSILRELTLdghDNIVQLIDSWEYHGHLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLAGGSLTDVVTE----TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQ 416
Cdd:cd14052    81 QTELCENGSLDVFLSElgllGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGM-ATVWPLI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRStMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM---VE----GEP------------PYLNENPLRALYLIATN 477
Cdd:cd14052   160 RGIE-REGDREYIAPEILSEHMYDKPADIFSLGLILLEAaanVVlpdnGDAwqklrsgdlsdaPRLSSTDLHSASSPSSN 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1024249297 478 GTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHP 517
Cdd:cd14052   239 PPPDPPNMPILSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
269-456 4.85e-24

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: 101.87  E-value: 4.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 269 TRFEKI---GQGASGTVYTALDIATGQEVAIKQMNLqqqPKKELIINEilVMRENK------NPNIVNYLDSYLVG---- 335
Cdd:cd14048     6 TDFEPIqclGRGGFGVVFEAKNKVDDCNYAVKRIRL---PNNELAREK--VLREVRalakldHPGIVRYFNAWLERppeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 -----DE--LWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQ----ALDFLHSNQVIHRDIKSDNILLGMDGSVKLT 404
Cdd:cd14048    81 wqekmDEvyLYIQMQLCRKENLKDWMNRRCTMESRELFVCLNIFKqiasAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024249297 405 DFGFCA---QITPEQSKRSTM---------VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 456
Cdd:cd14048   161 DFGLVTamdQGEPEQTVLTPMpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
272-451 5.31e-24

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: 101.59  E-value: 5.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGD-----ELWVVMEYL 345
Cdd:cd14037     9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRlSGHKNIVGYIDSSANRSgngvyEVLLLMEYC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFG-FCAQITPEQSKR 419
Cdd:cd14037    89 KGGGVIDLMNQrlqTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGsATTKILPPQTKQ 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1024249297 420 STMV--------GTPYWMAPEVV---TRKAYGPKVDIWSLGIM 451
Cdd:cd14037   169 GVTYveedikkyTTLQYRAPEMIdlyRGKPITEKSDIWALGCL 211
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
269-531 5.51e-24

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: 102.38  E-value: 5.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 269 TRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELiinEILVMRENkNPNIVNYLDSYlvGDEL--WVVMEYLA 346
Cdd:cd14092     9 LREEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSREV---QLLRLCQG-HPNIVKLHEVF--QDELhtYLVMELLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETCM-DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFcAQITPEQSKRSTM 422
Cdd:cd14092    83 GGELLERIRKKKRfTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGF-ARLKPENQPLKTP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVV----TRKAYGPKVDIWSLGIMAIEMVEGEPPY---LNENPLRALYLIATNGTPELQNPE--RLSAVFR 493
Cdd:cd14092   162 CFTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFqspSRNESAAEIMKRIKSGDFSFDGEEwkNVSSEAK 241
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSlTPL 531
Cdd:cd14092   242 SLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSS-TPL 278
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
274-515 6.25e-24

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: 101.22  E-value: 6.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALdiATGQEVAIKQMnlQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14148     2 IGVGGFGKVYKGL--WRGEEVAVKAA--RQDPDEDIAVTAENVRQEARlfwmlqHPNIIALRGVCLNPPHLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQ---VIHRDIKSDNILLG--------MDGSVKLTDFGFCAQItpEQ 416
Cdd:cd14148    78 GALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILepienddlSGKTLKITDFGLAREW--HK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTpELQNPERLSAVFRDFL 496
Cdd:cd14148   156 TTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKL-TLPIPSTCPEPFARLL 234
                         250
                  ....*....|....*....
gi 1024249297 497 NRCLEMDVDRRGSAKELLQ 515
Cdd:cd14148   235 EECWDPDPHGRPDFGSILK 253
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-520 6.44e-24

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: 102.00  E-value: 6.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIA---TGQEVAIKQMN----LQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd05613     8 LGTGAYGKVFLVRKVSghdAGKLYAMKVLKkatiVQKAKTAEHTRTERQVLEHiRQSPFLVTLHYAFQTDTKLHLILDYI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS-TMV 423
Cdd:cd05613    88 NGGELfTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDENERAySFC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVT--RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATN-GTPELQNPERLSAVFRDFLNRCL 500
Cdd:cd05613   168 GTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRiLKSEPPYPQEMSALAKDIIQRLL 247
                         250       260
                  ....*....|....*....|....*
gi 1024249297 501 EMDVDRR-----GSAKELLQHPFLK 520
Cdd:cd05613   248 MKDPKKRlgcgpNGADEIKKHPFFQ 272
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
268-462 7.43e-24

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: 100.70  E-value: 7.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGAsgtvYTALDIATGQE----VAIKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSY-LVGDELW 339
Cdd:cd14164     2 YTLGTTIGEGS----FSKVKLATSQKycckVAIKIVDRRRASPdfvQKFLPRELSILRRVNHPNIVQMFECIeVANGRLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGGSLTDV--VTETCMDEGQIAAVcrECLQALDFLHSNQVIHRDIKSDNILLGMDG-SVKLTDFGFCAQITPEQ 416
Cdd:cd14164    78 IVMEAAATDLLQKIqeVHHIPKDLARDMFA--QMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYP 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1024249297 417 SKRSTMVGTPYWMAPEVVTRKAYGP-KVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd14164   156 ELSTTFCGSRAYTPPEVILGTPYDPkKYDVWSLGVVLYVMVTGTMPF 202
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
267-524 9.41e-24

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 105.97  E-value: 9.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  267 KYTRFEKIGQGASGTVYTALDIATgQEV----AIKQMNLQQQPKKELIInEILVMRENKNPNIVNYLDSYL--VGDELWV 340
Cdd:PTZ00266    14 EYEVIKKIGNGRFGEVFLVKHKRT-QEFfcwkAISYRGLKEREKSQLVI-EVNVMRELKHKNIVRYIDRFLnkANQKLYI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  341 VMEYLAGGSLTDVVtETC------MDEGQIAAVCRECLQALDFLHS-------NQVIHRDIKSDNILLG----------- 396
Cdd:PTZ00266    92 LMEFCDAGDLSRNI-QKCykmfgkIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLStgirhigkita 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297  397 ----MDGS--VKLTDFGFCAQITPEQSKRSTmVGTPYWMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPL 468
Cdd:PTZ00266   171 qannLNGRpiAKIGDFGLSKNIGIESMAHSC-VGTPYYWSPELLLHetKSYDDKSDMWALGCIIYELCSGKTPFHKANNF 249
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1024249297  469 RALYLIATNGtPELQ---NPERLSAVFRDFLNrcleMDVDRRGSAKELLQHPFLKLAKP 524
Cdd:PTZ00266   250 SQLISELKRG-PDLPikgKSKELNILIKNLLN----LSAKERPSALQCLGYQIIKNVGP 303
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
318-498 1.26e-23

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: 102.41  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 318 RENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG 396
Cdd:cd05617    71 QASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMfHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLD 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 397 MDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY--LNENPLRAL--Y 472
Cdd:cd05617   151 ADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiITDNPDMNTedY 230
                         170       180       190
                  ....*....|....*....|....*....|
gi 1024249297 473 LIATNGTPELQNPERLS----AVFRDFLNR 498
Cdd:cd05617   231 LFQVILEKPIRIPRFLSvkasHVLKGFLNK 260
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
268-455 1.36e-23

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: 100.26  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQqpkkELIINEILVMRENKNPNIVNYLDSYLVGDE---------- 337
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNN----EKAEREVKALAKLDHPNIVRYNGCWDGFDYdpetsssnss 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 ------LWVVMEYLAGGSLTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF 408
Cdd:cd14047    84 rsktkcLFIQMEFCEKGTLESWIEKrngEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1024249297 409 CAQITpEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM 455
Cdd:cd14047   164 VTSLK-NDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFEL 209
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
274-516 1.44e-23

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: 100.50  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTAldIATGQEVAIKQMnlQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14146     2 IGVGGFGKVYRA--TWKGQEVAVKAA--RQDPDEDIKATAESVRQEAKlfsmlrHPNIIKLEGVCLEEPNLCLVMEFARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTETCMDEG-----------------QIAavcreclQALDFLHSNQV---IHRDIKSDNILLG--------MDG 399
Cdd:cd14146    78 GTLNRALAAANAAPGprrarripphilvnwavQIA-------RGMLYLHEEAVvpiLHRDLKSSNILLLekiehddiCNK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 400 SVKLTDFGFCAQItpEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT 479
Cdd:cd14146   151 TLKITDFGLAREW--HRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKL 228
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1024249297 480 pELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQH 516
Cdd:cd14146   229 -TLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQ 264
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
267-523 1.53e-23

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: 101.78  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGD-----ELW 339
Cdd:cd07859     1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINdvFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSrrefkDIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEyLAGGSLTDVVT---ETCMDEGQIaaVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQI---- 412
Cdd:cd07859    81 VVFE-LMESDLHQVIKandDLTPEHHQF--FLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGL-ARVafnd 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQSKRSTMVGTPYWMAPEVVTR--KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTN--GTP-------- 480
Cdd:cd07859   157 TPTAIFWTDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLI-TDllGTPspetisrv 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 481 ------------ELQNPERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFLK-LAK 523
Cdd:cd07859   236 rnekarrylssmRKKQPVPFSQKFPnadplalRLLERLLAFDPKDRPTAEEALADPYFKgLAK 298
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
273-523 1.57e-23

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: 100.49  E-value: 1.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTAldiATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVVMEYLAGGSL 350
Cdd:cd14149    19 RIGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQFqaFRNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCEGSSL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT----PEQSKRSTmvG 424
Cdd:cd14149    95 YKHlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgSQQVEQPT--G 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIATNG-TPELQNP-ERLSAVFRDFLNR 498
Cdd:cd14149   173 SILWMAPEVIRMQDNNPfsfQSDVYSYGIVLYELMTGELPYSHiNNRDQIIFMVGRGYaSPDLSKLyKNCPKAMKRLVAD 252
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 499 CLEMDVDRRG------SAKELLQHPFLKLAK 523
Cdd:cd14149   253 CIKKVKEERPlfpqilSSIELLQHSLPKINR 283
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
271-507 1.96e-23

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: 99.71  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEKIGQGASGTVYTAldiATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVVMEYLAGG 348
Cdd:cd14150     5 LKRIGTGSFGTVFRG---KWHGDVAVKILKVTEPTPEQLqaFKNEMQVLRKTRHVNILLFM-GFMTRPNFAIITQWCEGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT----PEQSKRSTm 422
Cdd:cd14150    81 SLYRHlhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTrwsgSQQVEQPS- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 vGTPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQN-PERLSAVFRDFL 496
Cdd:cd14150   160 -GSILWMAPEVIRMQDTNPysfQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGylSPDLSKlSSNCPKAMKRLL 238
                         250
                  ....*....|.
gi 1024249297 497 NRCLEMDVDRR 507
Cdd:cd14150   239 IDCLKFKREER 249
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
264-515 2.35e-23

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: 99.35  E-value: 2.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYtaLDIATGQEVAIKQMNLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05039     4 NKKDLKLGELIGKGEFGDVM--LGDYRGQKVAVKCLKDDSTAAQAFL-AEASVMTTLRHPNLVQLLGVVLEGNGLYIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTD--------VVTEtcmdEGQIAaVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGfcaqITPE 415
Cdd:cd05039    81 YMAKGSLVDylrsrgraVITR----KDQLG-FALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFG----LAKE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNEnPLRALYLIATNGTpELQNPERLSAVFR 493
Cdd:cd05039   152 ASSNQDGGKLPIkWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRI-PLKDVVPHVEKGY-RMEAPEGCPPEVY 229
                         250       260
                  ....*....|....*....|..
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd05039   230 KVMKNCWELDPAKRPTFKQLRE 251
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
273-461 2.54e-23

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: 99.88  E-value: 2.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYtaLDIATGQEVAIKQMN----LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd14158    22 KLGEGGFGVVF--KGYINDKNVAVKKLAamvdISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTetCMDEGQIAAVCREC------LQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKR--- 419
Cdd:cd14158   100 SLLDRLA--CLNDTPPLSWHMRCkiaqgtANGINYLHENNHIHRDIKSANILLDETFVPKISDFGL-ARASEKFSQTimt 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1024249297 420 STMVGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMVEGEPP 461
Cdd:cd14158   177 ERIVGTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIITGLPP 217
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
268-519 2.97e-23

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: 99.21  E-value: 2.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTS-ARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS--VKLTDFGFCAQITPEQSKRSTMvGT 425
Cdd:cd14108    83 ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQELTPNEPQYCKY-GT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT-NGTPELQNPERLSAVFRDFLNRCLEMDv 504
Cdd:cd14108   162 PEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNyNVAFEESMFKDLCREAKGFIIKVLVSD- 240
                         250
                  ....*....|....*
gi 1024249297 505 DRRGSAKELLQHPFL 519
Cdd:cd14108   241 RLRPDAEETLEHPWF 255
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
268-517 3.26e-23

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: 98.92  E-value: 3.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQmnlqqqpKKELIINEilVMRENK------------NPNIVNYLDSYLVG 335
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKR-------SRSRFRGE--KDRKRKleeverheklgeHPNCVRFIKAWEEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 DELWVVMEyLAGGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP 414
Cdd:cd14050    74 GILYIQTE-LCDTSLQQYCEEThSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMvGTPYWMAPEVVtRKAYGPKVDIWSLGIMA------IEMVEGEPPYlneNPLRALYLIA--TNGtpelqnpe 486
Cdd:cd14050   153 EDIHDAQE-GDPRYMAPELL-QGSFTKAADIFSLGITIlelacnLELPSGGDGW---HQLRQGYLPEefTAG-------- 219
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 487 rLSAVFRDFLNRCLEMDVDRRGSAKELLQHP 517
Cdd:cd14050   220 -LSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
268-520 3.57e-23

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: 99.71  E-value: 3.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05630     2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVV---TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItPEQSKRST 421
Cdd:cd05630    82 MNGGDLKFHIyhmGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHV-PEGQTIKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN---PLRALYLIATNGTPELQnpERLSAVFRDFLNR 498
Cdd:cd05630   161 RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKkkiKREEVERLVKEVPEEYS--EKFSPQARSLCSM 238
                         250       260
                  ....*....|....*....|....*..
gi 1024249297 499 CLEMDVDRR-----GSAKELLQHPFLK 520
Cdd:cd05630   239 LLCKDPAERlgcrgGGAREVKEHPLFK 265
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
268-519 3.83e-23

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: 99.65  E-value: 3.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd07870     2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTaIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 ggslTDVVTETCMDEG-----QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC-AQITPEQSKRS 420
Cdd:cd07870    82 ----TDLAQYMIQHPGglhpyNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLArAKSIPSQTYSS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVgTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLN-ENPLRALYLIAT-----------------NGTPE 481
Cdd:cd07870   158 EVV-TLWYRPPDVLLGATdYSSALDIWGAGCIFIEMLQGQPAFPGvSDVFEQLEKIWTvlgvptedtwpgvsklpNYKPE 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 482 LQNP----------ERLSAVFR--DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07870   237 WFLPckpqqlrvvwKRLSRPPKaeDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
274-519 5.79e-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: 100.59  E-value: 5.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQM-NLQQQpkkelIINEILVMRENK------NPNIVNYLDSYLVGD-----ELWVV 341
Cdd:cd07853     8 IGYGAFGVVWSVTDPRDGKRVALKKMpNVFQN-----LVSCKRVFRELKmlcffkHDNVLSALDILQPPHidpfeEIYVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd07853    83 TELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESKHMT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 M-VGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIaTN--GTPELQN------------- 484
Cdd:cd07853   163 QeVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLI-TDllGTPSLEAmrsacegarahil 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 485 -----PERLSAVFR----------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07853   242 rgphkPPSLPVLYTlssqatheavHLLCRMLVFDPDKRISAADALAHPYL 291
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
268-518 6.76e-23

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: 99.31  E-value: 6.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQpkKELI----INEILVMRENKNPNIVNYLD-SYLVGDE----- 337
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNE--KDGFpitaLREIKILKKLKHPNVVPLIDmAVERPDKskrkr 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 --LWVVMEY----LAGGSLTDVVTETcmdEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ 411
Cdd:cd07866    88 gsVYMVTPYmdhdLSGLLENPSVKLT---ESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 412 IT--PEQSKR---------STMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNG 478
Cdd:cd07866   165 YDgpPPNPKGgggggtrkyTNLVVTRWYRPPELLLgERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIfKLCG 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 479 TPELQN-------------------PERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07866   245 TPTEETwpgwrslpgcegvhsftnyPRTLEERFGklgpeglDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
268-520 6.83e-23

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: 100.51  E-value: 6.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlqqQPKKELIINEIL-------VMRENKNPNIVNYLDSYLVGDELWV 340
Cdd:cd05625     3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTL----RKKDVLLRNQVAhvkaerdILAEADNEWVVRLYYSFQDKDNLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLAGGSLTDVVTETCMDEGQIAAV-CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA--------- 410
Cdd:cd05625    79 VMDYIPGGDMMSLLIRMGVFPEDLARFyIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthdsk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 -----------------------------QITP------EQSKRS---TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMA 452
Cdd:cd05625   159 yyqsgdhlrqdsmdfsnewgdpencrcgdRLKPlerraaRQHQRClahSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVIL 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 453 IEMVEGEPPYLNENPLRA-LYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGS--AKELLQHPFLK 520
Cdd:cd05625   239 FEMLVGQPPFLAQTPLETqMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKngADEIKAHPFFK 309
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
68-113 8.02e-23

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


Pssm-ID: 238526  Cd Length: 46  Bit Score: 91.18  E-value: 8.02e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297  68 PEISLPSDFEHTIHVGFDAVTGEFTGIPEQWARLLQTSNITKLEQK 113
Cdd:cd01093     1 PEISSPTNFKHRVHVGFDPQTGEFTGLPEEWQRLLKSSGITKEEQK 46
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
267-518 8.74e-23

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: 98.75  E-value: 8.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQ----PKKELIINEILVMReNKNPNIVNYLDSYLVGDE----L 338
Cdd:cd07837     2 AYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEeegvPSTALREVSLLQML-SQSIYIVRLLDVEHVEENgkplL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGG-----SLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD-GSVKLTDFGFCAQI 412
Cdd:cd07837    81 YLVFEYLDTDlkkfiDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGLGRAF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQSKRSTMVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQ------- 483
Cdd:cd07837   161 TIPIKSYTHEIVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIfRLLGTPNEEvwpgvsk 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 484 ----------NPERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07837   241 lrdwheypqwKPQDLSRAVPdlepegvDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
271-520 8.77e-23

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: 98.42  E-value: 8.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd05608     6 FRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRkgyEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLT----DVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd05608    86 GDLRyhiyNVDEENpGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTKGY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL--------NENPLRALYLIATngtpelqNPERLSAVFRD 494
Cdd:cd05608   166 AGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRargekvenKELKQRILNDSVT-------YSEKFSPASKS 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 495 FLNRCLEMDVDRR-----GSAKELLQHPFLK 520
Cdd:cd05608   239 ICEALLAKDPEKRlgfrdGNCDGLRTHPFFR 269
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
259-519 9.08e-23

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: 99.72  E-value: 9.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 259 VSVGDPK----KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSY 332
Cdd:cd07876    10 VQVADSTftvlKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSrpFQNQTHAKRAYRELVLLKCVNHKNIISLLNVF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 333 LVG------DELWVVMEyLAGGSLTDVVtETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 406
Cdd:cd07876    90 TPQksleefQDVYLVME-LMDANLCQVI-HMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 407 GFcAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAL-YLIATNGTPELQNP 485
Cdd:cd07876   168 GL-ARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWnKVIEQLGTPSAEFM 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 486 ERL--------------------------------------SAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07876   247 NRLqptvrnyvenrpqypgisfeelfpdwifpseserdklkTSQARDLLSKMLVIDPDKRISVDEALRHPYI 318
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
274-482 1.16e-22

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: 97.52  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERkaLLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTETCMD-----EGQIAavcRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFGF--CAQITPEQSKRSTM 422
Cdd:cd13978    81 SLLEREIQDvpwslRFRII---HEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLskLGMKSISANRRRGT 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 423 ---VGTPYWMAPEVVTRKAYGP--KVDIWSLGIMAIEMVEGEPPYLNE-NPLRALYLIATNGTPEL 482
Cdd:cd13978   158 enlGGTPIYMAPEAFDDFNKKPtsKSDVYSFAIVIWAVLTRKEPFENAiNPLLIMQIVSKGDRPSL 223
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
274-474 1.22e-22

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


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 98.14  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLt 351
Cdd:cd07848     9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEevKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNML- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST-MVGTPYW 428
Cdd:cd07848    88 ELLEEmpNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTeYVATRWY 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 429 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI 474
Cdd:cd07848   168 RSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTI 213
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
267-520 1.38e-22

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 97.97  E-value: 1.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:PLN00009    3 QYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEgvPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LaggsltDVVTETCMDEGQ--------IAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM-DGSVKLTDFGFCAQITPE 415
Cdd:PLN00009   83 L------DLDLKKHMDSSPdfaknprlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARAFGIP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQN--------- 484
Cdd:PLN00009  157 VRTFTHEVVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIfRILGTPNEETwpgvtslpd 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 485 ---------PERLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:PLN00009  237 yksafpkwpPKDLATVVPtlepagvDLLSKMLRLDPSKRITARAALEHEYFK 288
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
265-515 1.42e-22

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 100.85  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALD--IATGQEVAIKQMNLQQQPKK------ELIINEILVMRE-NKNPNIVNYLDSYLVG 335
Cdd:COG5752    31 KERYRAIKPLGQGGFGRTFLAVDedIPSHPHCVIKQFYFPEQGPSsfqkavELFRQEAVRLDElGKHPQIPELLAYFEQD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 DELWVVMEYLAGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM-DGSVKLTDFGFCAQIT 413
Cdd:COG5752   111 QRLYLVQEFIEGQTLAQeLEKKGVFSESQIWQLLKDLLPVLQFIHSRNVIHRDIKPANIIRRRsDGKLVLIDFGVAKLLT 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 414 PEQ-SKRSTMVGTPYWMAPEVVTRKAYgPKVDIWSLGIMAIEMVEGEPPY-----LNENPLRALYLiatngTPELQNPER 487
Cdd:COG5752   191 ITAlLQTGTIIGTPEYMAPEQLRGKVF-PASDLYSLGVTCIYLLTGVSPFdlfdvSEDRWVWRDFL-----PPGTKVSDR 264
                         250       260
                  ....*....|....*....|....*....
gi 1024249297 488 LSAVfrdfLNRCLEMDV-DRRGSAKELLQ 515
Cdd:COG5752   265 LGQI----LDKLLQNALkQRYQSATEVLQ 289
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
267-519 1.59e-22

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 98.62  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIK----QMNLQQQPKKELIINEILVMRENKNP-NIVNYLDSYLVGDELWVV 341
Cdd:cd14225    44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIKiirnKKRFHHQALVEVKILDALRRKDRDNShNVIHMKEYFYFRNHLCIT 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEyLAGGSLTDVVTETCMDEGQIAAVCREC---LQALDFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFGF-CAqitpE 415
Cdd:cd14225   124 FE-LLGMNLYELIKKNNFQGFSLSLIRRFAislLQCLRLLYRERIIHCDLKPENILLRQRGqsSIKVIDFGSsCY----E 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA-------------------- 475
Cdd:cd14225   199 HQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMevlglpppelienaqrrrlf 278
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 476 ----------TN--GTPELQNPERLSAV-------FRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14225   279 fdskgnprciTNskGKKRRPNSKDLASAlktsdplFLDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
274-519 1.78e-22

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: 97.80  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQmnLQQQPKKELIINeiLVMRENKNPNIVNYLDSY--LVGDE--LWVVMEYLAGGS 349
Cdd:cd14170    10 LGLGINGKVLQIFNKRTQEKFALKM--LQDCPKARREVE--LHWRASQCPHIVRIVDVYenLYAGRkcLLIVMECLDGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFCAQITPEQSkRSTMV 423
Cdd:cd14170    86 LFSRIQDrgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNS-LTTPC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLR---ALYLIATNGTPELQNPE--RLSAVFRDFLNR 498
Cdd:cd14170   165 YTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAispGMKTRIRMGQYEFPNPEwsEVSEEVKMLIRN 244
                         250       260
                  ....*....|....*....|.
gi 1024249297 499 CLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14170   245 LLKTEPTQRMTITEFMNHPWI 265
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
267-519 2.00e-22

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: 97.07  E-value: 2.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFE-KIGQGASGTVYTALDIATGQEVAI------KQMNLQQQPKKEliinEILVMRENKNPNIVNYLDSYLVGDE-- 337
Cdd:cd14032     1 RFLKFDiELGRGSFKTVYKGLDTETWVEVAWcelqdrKLTKVERQRFKE----EAEMLKGLQHPNIVRFYDFWESCAKgk 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 --LWVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILL-GMDGSVKLTDFGFCAq 411
Cdd:cd14032    77 rcIVLVTELMTSGTLKTYLKRfKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFItGPTGSVKIGDLGLAT- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 412 iTPEQSKRSTMVGTPYWMAPEVVtRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTP-----ELQNPE 486
Cdd:cd14032   156 -LKRASFAKSVIGTPEFMAPEMY-EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKpasfeKVTDPE 233
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1024249297 487 rlsavFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14032   234 -----IKEIIGECICKNKEERYEIKDLLSHAFF 261
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
274-520 2.27e-22

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: 98.03  E-value: 2.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI---INE--ILVMRENKN-PNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVahtIGErnILVRTALDEsPFIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTP 426
Cdd:cd05586    81 GELFwHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGTT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 427 YWMAPEV-VTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPER-LSAVFRDF----LNRCL 500
Cdd:cd05586   161 EYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFG---KVRFPKDvLSDEGRSFvkglLNRNP 237
                         250       260
                  ....*....|....*....|
gi 1024249297 501 EMDVDRRGSAKELLQHPFLK 520
Cdd:cd05586   238 KHRLGAHDDAVELKEHPFFA 257
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
274-516 3.01e-22

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: 96.24  E-value: 3.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIiNEILVMRE-NKNPNIVNYLDSYLVGDELWV-VMEYLAGGSLT 351
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFL-REYNISLElSVHPHIIKTYDVAFETEDYYVfAQEYAPYGDLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVT-ETCMDEgqiaAVCRECLQ----ALDFLHSNQVIHRDIKSDNILLgMDGS---VKLTDFGFC-AQITPEQSKRSTm 422
Cdd:cd13987    80 SIIPpQVGLPE----ERVKRCAAqlasALDFMHSKNLVHRDIKPENVLL-FDKDcrrVKLCDFGLTrRVGSTVKRVSGT- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 vgTPYwMAPEVV-TRKAYG----PKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-------ATNGTPELQNP--ERL 488
Cdd:cd13987   154 --IPY-TAPEVCeAKKNEGfvvdPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEfvrwqkrKNTAVPSQWRRftPKA 230
                         250       260
                  ....*....|....*....|....*...
gi 1024249297 489 SAVFRdflnRCLEMDVDRRGSAKELLQH 516
Cdd:cd13987   231 LRMFK----KLLAPEPERRCSIKEVFKY 254
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
272-514 3.09e-22

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: 96.65  E-value: 3.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTAldIATGQEVAIKQMnlQQQPKKELIINEILVMRENK------NPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd14145    12 EIIGIGGFGKVYRA--IWIGDEVAVKAA--RHDPDEDISQTIENVRQEAKlfamlkHPNIIALRGVCLKEPNLCLVMEFA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQ---VIHRDIKSDNILLGM--------DGSVKLTDFGFCAQItp 414
Cdd:cd14145    88 RGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAivpVIHRDLKSSNILILEkvengdlsNKILKITDFGLAREW-- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTpELQNPERLSAVFRD 494
Cdd:cd14145   166 HRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKL-SLPIPSTCPEPFAR 244
                         250       260
                  ....*....|....*....|
gi 1024249297 495 FLNRCLEMDVDRRGSAKELL 514
Cdd:cd14145   245 LMEDCWNPDPHSRPPFTNIL 264
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
274-520 4.57e-22

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: 97.82  E-value: 4.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIIN---EILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd05627    10 IGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHiraERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 -TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ------------- 416
Cdd:cd05627    90 mTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHrtefyrnlthnpp 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 ---------SKRS-------------TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLI 474
Cdd:cd05627   170 sdfsfqnmnSKRKaetwkknrrqlaySTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETP-QETYRK 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 475 ATNGTPELQNPER--LSAVFRDFLNR-CLemDVDRR---GSAKELLQHPFLK 520
Cdd:cd05627   249 VMNWKETLVFPPEvpISEKAKDLILRfCT--DAENRigsNGVEEIKSHPFFE 298
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
265-514 5.00e-22

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: 95.59  E-value: 5.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYtaLDIATGQ-EVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05059     3 PSELTFLKELGSGQFGVVH--LGKWRGKiDVAIKMIK-EGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTET--CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRST 421
Cdd:cd05059    80 YMANGCLLNYLRERrgKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTSSV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 mvGTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEM-VEGEPPYLNENPLRALYLIATNgtPELQNPERLSAVFRDFLN 497
Cdd:cd05059   160 --GTKFpvkWSPPEVFMYSKFSSKSDVWSFGVLMWEVfSEGKMPYERFSNSEVVEHISQG--YRLYRPHLAPTEVYTIMY 235
                         250
                  ....*....|....*..
gi 1024249297 498 RCLEMDVDRRGSAKELL 514
Cdd:cd05059   236 SCWHEKPEERPTFKILL 252
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
274-515 5.34e-22

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: 95.28  E-value: 5.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV 353
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIY--KNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 VT--ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVK---LTDFGFCAQI----TPEQSKRSTMVG 424
Cdd:cd14156    79 LAreELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempANDPERKLSLVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQN--PERlsavFRDFLNRCLEM 502
Cdd:cd14156   159 SAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIPADPEVLPRTGDFGLDVQAFKEMVPgcPEP----FLDLAASCCRM 234
                         250
                  ....*....|...
gi 1024249297 503 DVDRRGSAKELLQ 515
Cdd:cd14156   235 DAFKRPSFAELLD 247
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
268-523 5.47e-22

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: 97.04  E-value: 5.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd06649     7 FERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAiRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETC-MDEGQIAAVCRECLQALDFL-HSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITpeQSKRSTMVG 424
Cdd:cd06649    87 GGSLDQVLKEAKrIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--DSMANSFVG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV--------------------------EGEPPYLNENP----------- 467
Cdd:cd06649   165 TRSYMSPERLQGTHYSVQSDIWSMGLSLVELAigrypipppdakeleaifgrpvvdgeEGEPHSISPRPrppgrpvsghg 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024249297 468 ---------LRALYLIATNGTPELQNPErLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAK 523
Cdd:cd06649   245 mdsrpamaiFELLDYIVNEPPPKLPNGV-FTPDFQEFVNKCLIKNPAERADLKMLMNHTFIKRSE 308
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
265-520 6.77e-22

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: 96.58  E-value: 6.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd05632     1 KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgesMALNEKQILEKVNSQFVVNLAYAYETKDALCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETC---MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItPEQSK 418
Cdd:cd05632    81 LTIMNGGDLKFHIYNMGnpgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKI-PEGES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 RSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYlnenplRALYLIATNGTPE---LQNPERLSAVF--- 492
Cdd:cd05632   160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPF------RGRKEKVKREEVDrrvLETEEVYSAKFsee 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024249297 493 -RDFLNRCLEMDVDRR-----GSAKELLQHPFLK 520
Cdd:cd05632   234 aKSICKMLLTKDPKQRlgcqeEGAGEVKRHPFFR 267
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
266-519 7.94e-22

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: 94.98  E-value: 7.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKqMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd14110     3 KTYAFQTEINRGRFSVVRQCEEKRSGQMLAAK-IIPYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ----SKRS 420
Cdd:cd14110    82 SGPELLYNLAErNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKvlmtDKKG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTpywMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCL 500
Cdd:cd14110   162 DYVET---MAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCYAGLSGGAVNFLKSTL 238
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd14110   239 CAKPWGRPTASECLQNPWL 257
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
274-520 8.57e-22

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: 95.58  E-value: 8.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINE----ILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetLALNErimlSLVSTGGDCPFIVCMTYAFQTPDKLCFILDLMN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRStmVGT 425
Cdd:cd05606    82 GGDLHYHLSQhGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHAS--VGT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDV 504
Cdd:cd05606   160 HGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDV 239
                         250       260
                  ....*....|....*....|.
gi 1024249297 505 DRR-----GSAKELLQHPFLK 520
Cdd:cd05606   240 SKRlgclgRGATEVKEHPFFK 260
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
268-519 1.29e-21

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: 94.29  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK---KELIINEILVMRENKNPNIVNYLDSYLVGD-ELWVVME 343
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEefiQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL-GMDgsVKLTDFGFcAQITPEQSKR-- 419
Cdd:cd14163    82 LAEDGDVFDCVLHGGpLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLqGFT--LKLTDFGF-AKQLPKGGREls 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYliatNGTPELQNPERL--SAVFRDFL 496
Cdd:cd14163   159 QTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLC----QQQKGVSLPGHLgvSRTCQDLL 234
                         250       260
                  ....*....|....*....|...
gi 1024249297 497 NRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14163   235 KRLLEPDMVLRPSIEEVSWHPWL 257
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
272-519 1.41e-21

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: 94.12  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMnlqqqPKKELIINEILVMRENKNPNIVNYLDSYLV-GDELWVVMEYLAGGSL 350
Cdd:cd14109    10 EDEKRAAQGAPFHVTERSTGRNFLAQLR-----YGDPFLMREVDIHNSLDHPNIVQMHDAYDDeKLAVTVIDNLASTIEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 --------TDVVTETCmdegqIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDgSVKLTDFGFCAQItpEQSKRSTM 422
Cdd:cd14109    85 vrdnllpgKDYYTERQ-----VAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQSRRL--LRGKLTTL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 V-GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP-ERLSAVFRDFLNRCL 500
Cdd:cd14109   157 IyGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPlGNISDDARDFIKKLL 236
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd14109   237 VYIPESRLTVDEALNHPWF 255
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
266-516 1.59e-21

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: 94.28  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVytALDIATGQEVAIKqmNLQQQPKKELIINEILVMRENKNPNIVNYLdSYLVGDE--LWVVME 343
Cdd:cd05082     6 KELKLLQTIGKGEFGDV--MLGDYRGNKVAVK--CIKNDATAQAFLAEASVMTQLRHSNLVQLL-GVIVEEKggLYIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVT---ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRS 420
Cdd:cd05082    81 YMAKGSLVDYLRsrgRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGtpyWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYlNENPLRALYLIATNGTpELQNPERLSAVFRDFLNRC 499
Cdd:cd05082   161 LPVK---WTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY-PRIPLKDVVPRVEKGY-KMDAPDGCPPAVYDVMKNC 235
                         250       260
                  ....*....|....*....|
gi 1024249297 500 LEMDVDRRGS---AKELLQH 516
Cdd:cd05082   236 WHLDAAMRPSflqLREQLEH 255
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
264-513 1.60e-21

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: 94.76  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTV----YTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLD-SYLVGD- 336
Cdd:cd05038     2 EERHLKFIKQLGEGHFGSVelcrYDPLGDNTGEQVAVKSLQPSGEEQhMSDFKREIEILRTLDHEYIVKYKGvCESPGRr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTDVVTET--CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITP 414
Cdd:cd05038    82 SLRLIMEYLPSGSLRDYLQRHrdQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGL-AKVLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EqSKRSTMVGTP-----YWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPpylNENPLRA-LYLIATNGTPE------ 481
Cdd:cd05038   161 E-DKEYYYVKEPgespiFWYAPECLRESRFSSASDVWSFGVTLYELFTyGDP---SQSPPALfLRMIGIAQGQMivtrll 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1024249297 482 --LQNPERLSA-------VFrDFLNRCLEMDVDRRGSAKEL 513
Cdd:cd05038   237 elLKSGERLPRppscpdeVY-DLMKECWEYEPQDRPSFSDL 276
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
264-514 2.47e-21

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: 93.95  E-value: 2.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVY--TALDIATGQ---EVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDE 337
Cdd:cd05032     4 PREKITLIRELGQGSFGMVYegLAKGVVKGEpetRVAIKTVNENASMRERIeFLNEASVMKEFNCHHVVRLLGVVSTGQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTETCMDE-----------GQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 406
Cdd:cd05032    84 TLVVMELMAKGDLKSYLRSRRPEAennpglgpptlQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 407 GFCAQITPEQSKRSTMVGT-PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYL---NENPLRalYLIATNgtp 480
Cdd:cd05032   164 GMTRDIYETDYYRKGGKGLlPVrWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQglsNEEVLK--FVIDGG--- 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024249297 481 ELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELL 514
Cdd:cd05032   239 HLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIV 272
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
313-520 3.19e-21

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 93.38  E-value: 3.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 313 EILV---MRenKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDI 388
Cdd:PHA03390   58 EPMVhqlMK--DNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLkKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 389 KSDNILL--GMDgSVKLTDFGFCAQI-TPeqskrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY--- 462
Cdd:PHA03390  136 KLENVLYdrAKD-RIYLCDYGLCKIIgTP-----SCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFked 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 463 ----LNENPLRALYliatngTPELQNPERLSAVFRDFLNRCLEMDVDRR-GSAKELLQHPFLK 520
Cdd:PHA03390  210 edeeLDLESLLKRQ------QKKLPFIKNVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFLK 266
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
257-530 6.30e-21

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: 94.34  E-value: 6.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 257 SIVSVGDPK----KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLD 330
Cdd:cd07875    11 YSVEIGDSTftvlKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSrpFQNQTHAKRAYRELVLMKCVNHKNIIGLLN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 331 SYLVG------DELWVVMEyLAGGSLTDVVtETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLT 404
Cdd:cd07875    91 VFTPQksleefQDVYIVME-LMDANLCQVI-QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKIL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 405 DFGFcAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEG-------------------------- 458
Cdd:cd07875   169 DFGL-ARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGgvlfpgtdhidqwnkvieqlgtpcpe 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 459 -----EP---PYLNENPLRALY----LIATNGTPELQNPERLSAV-FRDFLNRCLEMDVDRRGSAKELLQHPFLKL-AKP 524
Cdd:cd07875   248 fmkklQPtvrTYVENRPKYAGYsfekLFPDVLFPADSEHNKLKASqARDLLSKMLVIDASKRISVDEALQHPYINVwYDP 327

                  ....*.
gi 1024249297 525 LSSLTP 530
Cdd:cd07875   328 SEAEAP 333
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
274-462 7.35e-21

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 93.32  E-value: 7.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMN-LQQQPKKELIINEILVMRENKNPNIVNYL--DSYLVGDELWVVMEYLAGGSL 350
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNnLSFMRPLDVQMREFEVLKKLNHKNIVKLFaiEEELTTRHKVLVMELCPCGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TDVVTETC----MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNIL--LGMDGSV--KLTDFGFCAQITPEQSKRStM 422
Cdd:cd13988    81 YTVLEEPSnaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFGAARELEDDEQFVS-L 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249297 423 VGTPYWMAPEVVTR--------KAYGPKVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd13988   160 YGTEEYLHPDMYERavlrkdhqKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
267-520 8.67e-21

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: 93.69  E-value: 8.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIV---------NYLDSYLVG-- 335
Cdd:cd07854     6 RYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVkvyevlgpsGSDLTEDVGsl 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 ---DELWVVMEYLAgGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSV-KLTDFGFCAQ 411
Cdd:cd07854    86 telNSVYIVQEYME-TDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 412 ITPEQSKR---STMVGTPYWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI------------- 474
Cdd:cd07854   165 VDPHYSHKgylSEGLVTKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLIlesvpvvreedrn 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 475 ---------ATNGTPELQNPER-----LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 520
Cdd:cd07854   245 ellnvipsfVRNDGGEPRRPLRdllpgVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
268-519 9.82e-21

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: 92.76  E-value: 9.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLa 346
Cdd:cd07873     4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTaIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYL- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC-AQITPEQSKRSTMV 423
Cdd:cd07873    83 DKDLKQYLDDcgNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLArAKSIPTKTYSNEVV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 gTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPE-------LQNPE-------- 486
Cdd:cd07873   163 -TLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIfRILGTPTeetwpgiLSNEEfksynypk 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1024249297 487 -----------RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07873   242 yradalhnhapRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYF 285
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
267-457 1.04e-20

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: 93.00  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMR--ENKNPNIVNY---------------- 328
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVELALREFWALSsiQRQHPNVIQLeecvlqrdglaqrmsh 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 329 ----LDSYLVGDE----------------LWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDI 388
Cdd:cd13977    81 gsskSDLYLLLVEtslkgercfdprsacyLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQIVHRDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 389 KSDNILLGM---DGSVKLTDFGF---CAQITPE--------QSKRSTMVGTPYWMAPEvVTRKAYGPKVDIWSLGIMAIE 454
Cdd:cd13977   161 KPDNILISHkrgEPILKVADFGLskvCSGSGLNpeepanvnKHFLSSACGSDFYMAPE-VWEGHYTAKADIFALGIIIWA 239

                  ...
gi 1024249297 455 MVE 457
Cdd:cd13977   240 MVE 242
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
273-518 1.08e-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: 93.12  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTA--LDIATGQEVAIKQMnlqQQPKKELI------INEILVMRENKNPNIVNYLDSYLVGDE--LWVVM 342
Cdd:cd07842     7 CIGRGTYGRVYKAkrKNGKDGKEYAIKKF---KGDKEQYTgisqsaCREIALLRELKHENVVSLVEVFLEHADksVYLLF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYlAGGSLTDVV-----TETCM-DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFcAQI 412
Cdd:cd07842    84 DY-AEHDLWQIIkfhrqAKRVSiPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGL-ARL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQSKRST----MVGTPYWMAPEVVT-RKAYGPKVDIWSLG-IMAiEMVEGEPPYLNE-------NPLRALYLIA---T 476
Cdd:cd07842   162 FNAPLKPLAdldpVVVTIWYRAPELLLgARHYTKAIDIWAIGcIFA-ELLTLEPIFKGReakikksNPFQRDQLERifeV 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024249297 477 NGTPELQN-------PE--RLSAVF------------------------RDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd07842   241 LGTPTEKDwpdikkmPEydTLKSDTkastypnsllakwmhkhkkpdsqgFDLLRKLLEYDPTKRITAEEALEHPY 315
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
267-523 1.19e-20

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: 92.78  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKI---GQGASGTVYTALDIATGQE----VAIKQMNLQQQPK--KElIINEILVMRENKNPNIVNYLDSYLVgDE 337
Cdd:cd05108     5 KETEFKKIkvlGSGAFGTVYKGLWIPEGEKvkipVAIKELREATSPKanKE-ILDEAYVMASVDNPHVCRLLGICLT-ST 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTETCMDEGQ--IAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 415
Cdd:cd05108    83 VQLITQLMPFGCLLDYVREHKDNIGSqyLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVG-TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYlNENPLRALYLIATNGTPELQNPERLSAVF 492
Cdd:cd05108   163 EKEYHAEGGkVPIkWMALESILHRIYTHQSDVWSYGVTVWElMTFGSKPY-DGIPASEISSILEKGERLPQPPICTIDVY 241
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 493 RdFLNRCLEMDVDRRGSAKELLQHpFLKLAK 523
Cdd:cd05108   242 M-IMVKCWMIDADSRPKFRELIIE-FSKMAR 270
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
261-459 1.45e-20

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 93.91  E-value: 1.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 261 VGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQmnlqqqPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWV 340
Cdd:PHA03212   87 AGIEKAGFSILETFTPGAEGFAFACIDNKTCEHVVIKA------GQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCL 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VME--------YLAGGSLTDVvtetCmdegQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG-FCAQ 411
Cdd:PHA03212  161 ILPryktdlycYLAAKRNIAI----C----DILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGaACFP 232
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249297 412 ITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGE 459
Cdd:PHA03212  233 VDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
323-498 1.48e-20

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: 93.56  E-value: 1.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 323 PNIVNYLDSYLVGDELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSV 401
Cdd:cd05618    81 PFLVGLHSCFQTESRLFFVIEYVNGGDLMfHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHI 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 402 KLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY----LNENPLRAL--YLIA 475
Cdd:cd05618   161 KLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgSSDNPDQNTedYLFQ 240
                         170       180
                  ....*....|....*....|....*..
gi 1024249297 476 TNGTPELQNPERLS----AVFRDFLNR 498
Cdd:cd05618   241 VILEKQIRIPRSLSvkaaSVLKSFLNK 267
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
268-462 1.54e-20

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: 91.98  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05631     2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVV---TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItPEQSKRST 421
Cdd:cd05631    82 MNGGDLKFHIynmGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQI-PEGETVRG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd05631   161 RVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPF 201
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
338-520 1.58e-20

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: 92.87  E-value: 1.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ 416
Cdd:cd05588    71 LFFVIEFVNGGDLMfHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPG 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY----LNENPLRAL--YLIATNGTPELQNPERLS- 489
Cdd:cd05588   151 DTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgSSDNPDQNTedYLFQVILEKPIRIPRSLSv 230
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1024249297 490 ---AVFRDFLNRcleMDVDRRGSAKE-----LLQHPFLK 520
Cdd:cd05588   231 kaaSVLKGFLNK---NPAERLGCHPQtgfadIQSHPFFR 266
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
268-519 1.71e-20

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: 92.47  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQE--VAIKQM-NLQQqpKKELI---INEILVMRENKN-PNIVNYLDSYLVG----D 336
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEetVAIKKItNVFS--KKILAkraLRELKLLRHFRGhKNITCLYDMDIVFpgnfN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEyLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP- 414
Cdd:cd07857    80 ELYLYEE-LMEADLHQIIrSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSEn 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 ---EQSKRSTMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPE-------- 481
Cdd:cd07857   159 pgeNAGFMTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQIlQVLGTPDeetlsrig 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1024249297 482 ----------LQNPERLS-----------AVfrDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07857   239 spkaqnyirsLPNIPKKPfesifpnanplAL--DLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
267-462 1.96e-20

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: 91.17  E-value: 1.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQpkKELIINEILVMRENKN-PNIVNYLDSYLVGDELWVVMEyL 345
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQP--KQVLKMEVAVLKKLQGkPHFCRLIGCGRTERYNYIVMT-L 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS----VKLTDFGFCAQITP---- 414
Cdd:cd14017    78 LGPNLAELRRSQprgKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSdertVYILDFGLARQYTNkdge 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 415 -EQSKRST--MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd14017   158 vERPPRNAagFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPW 208
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
268-467 3.08e-20

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: 92.79  E-value: 3.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQvghIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ------- 416
Cdd:cd05628    83 LPGGDMmTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHrtefyrn 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024249297 417 ---------------SKRS-------------TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENP 467
Cdd:cd05628   163 lnhslpsdftfqnmnSKRKaetwkrnrrqlafSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETP 241
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
272-456 3.29e-20

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: 90.85  E-value: 3.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALdiATGQEVAIKQMNLQQ----QPKKELIINEILvmrenKNPNIVNYLDSYLVG----DELWVVME 343
Cdd:cd14053     1 EIKARGRFGAVWKAQ--YLNRLVAVKIFPLQEkqswLTEREIYSLPGM-----KHENILQFIGAEKHGesleAEYWLITE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSN----------QVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 413
Cdd:cd14053    74 FHERGSLCDYLKGNVISWNELCKIAESMARGLAYLHEDipatngghkpSIAHRDFKSKNVLLKSDLTACIADFGLALKFE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 414 PEQSKRST--MVGTPYWMAPEVV------TRKAYgPKVDIWSLGIMAIEMV 456
Cdd:cd14053   154 PGKSCGDThgQVGTRRYMAPEVLegainfTRDAF-LRIDMYAMGLVLWELL 203
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
266-455 4.30e-20

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: 90.64  E-value: 4.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYL--VGDELWVV 341
Cdd:cd14049     6 NEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCmkVLREVKVLAGLQHPNIVGYHTAWMehVQLMLYIQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEyLAGGSLTDVVTE---------------TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL-GMDGSVKLTD 405
Cdd:cd14049    86 MQ-LCELSLWDWIVErnkrpceeefksapyTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLhGSDIHVRIGD 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 406 FGF-CAQITPEQSKRSTM-----------VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM 455
Cdd:cd14049   165 FGLaCPDILQDGNDSTTMsrlnglthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLEL 226
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
259-519 4.74e-20

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: 91.10  E-value: 4.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 259 VSVGDP-KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKqmnLQQQPKK--ELIINEILVMRE--NKNP------NIVN 327
Cdd:cd14136     2 VKIGEVyNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALK---VVKSAQHytEAALDEIKLLKCvrEADPkdpgreHVVQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 328 YLDSYLV----GDELWVVMEYLaGGSLTDVVtETCMDEG-QIAAV---CRECLQALDFLHSN-QVIHRDIKSDNILLGMD 398
Cdd:cd14136    79 LLDDFKHtgpnGTHVCMVFEVL-GPNLLKLI-KRYNYRGiPLPLVkkiARQVLQGLDYLHTKcGIIHTDIKPENVLLCIS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 399 GS-VKLTDFG--------FCAQITPEQskrstmvgtpyWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEppYL------ 463
Cdd:cd14136   157 KIeVKIADLGnacwtdkhFTEDIQTRQ-----------YRSPEVILGAGYGTPADIWSTACMAFELATGD--YLfdphsg 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 464 -----NENPLrALYL---------IATNG--TPELQN--------------------------PERLSAVFRDFLNRCLE 501
Cdd:cd14136   224 edysrDEDHL-ALIIellgriprsIILSGkySREFFNrkgelrhisklkpwpledvlvekykwSKEEAKEFASFLLPMLE 302
                         330
                  ....*....|....*...
gi 1024249297 502 MDVDRRGSAKELLQHPFL 519
Cdd:cd14136   303 YDPEKRATAAQCLQHPWL 320
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
267-426 5.19e-20

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 89.82  E-value: 5.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIK-QMNLQQQPkkeLIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKiEKKDSKHP---QLEYEAKVYKLlQGGPGIPRLYWFGQEGDYNVMVMDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LaGGSLTDVVTE---------TCMdegqIAavcRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVK---LTDFGFCA-- 410
Cdd:cd14016    78 L-GPSLEDLFNKcgrkfslktVLM----LA---DQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAKky 149
                         170       180
                  ....*....|....*....|..
gi 1024249297 411 --QIT----PEQSKRStMVGTP 426
Cdd:cd14016   150 rdPRTgkhiPYREGKS-LTGTA 170
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
259-521 5.36e-20

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: 91.69  E-value: 5.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 259 VSVGDPK----KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDSY 332
Cdd:cd07874     6 VEVGDSTftvlKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSrpFQNQTHAKRAYRELVLMKCVNHKNIISLLNVF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 333 LVGDEL------WVVMEyLAGGSLTDVVtETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 406
Cdd:cd07874    86 TPQKSLeefqdvYLVME-LMDANLCQVI-QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 407 GFcAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAL-YLIATNGTP----- 480
Cdd:cd07874   164 GL-ARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWnKVIEQLGTPcpefm 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024249297 481 -ELQ---------NPERLSAVF-----------------------RDFLNRCLEMDVDRRGSAKELLQHPFLKL 521
Cdd:cd07874   243 kKLQptvrnyvenRPKYAGLTFpklfpdslfpadsehnklkasqaRDLLSKMLVIDPAKRISVDEALQHPYINV 316
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
268-519 5.59e-20

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: 90.13  E-value: 5.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTaIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 ggslTDVVT--ETC---MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC-AQITPEQSKRS 420
Cdd:cd07844    82 ----TDLKQymDDCgggLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLArAKSVPSKTYSN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVgTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYL-NENPLRALYLI-ATNGTPELQ-------NPERLSA 490
Cdd:cd07844   158 EVV-TLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFPgSTDVEDQLHKIfRVLGTPTEEtwpgvssNPEFKPY 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 491 VFR---------------------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07844   237 SFPfypprplinhaprldriphgeELALKFLQYEPKKRISAAEAMKHPYF 286
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
264-462 6.57e-20

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: 90.17  E-value: 6.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVY--TALDIATGQE----VAIKqMNLQQQPKKELI--INEILVMRE-NKNPNIVNYLDSYLV 334
Cdd:cd05053    10 PRDRLTLGKPLGEGAFGQVVkaEAVGLDNKPNevvtVAVK-MLKDDATEKDLSdlVSEMEMMKMiGKHKNIINLLGACTQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 335 GDELWVVMEYLAGGSLTD-----------------VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM 397
Cdd:cd05053    89 DGPLYVVVEYASKGNLREflrarrppgeeaspddpRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTE 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297 398 DGSVKLTDFGFCAQITPEQSKRSTMVG-TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05053   169 DNVMKIADFGLARDIHHIDYYRKTTNGrLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 236
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
269-514 7.32e-20

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: 89.24  E-value: 7.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 269 TRFEKIGQGASGTVYTALDIATgQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd05112     7 TFVQEIGSGQFGLVHLGYWLNK-DKVAIKTIR-EGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTEtcmDEGQIAA-----VCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTmv 423
Cdd:cd05112    85 CLSDYLRT---QRGLFSAetllgMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSST-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPYlnENPLRALYLIATNGTPELQNPERLSAVFRDFLNRC 499
Cdd:cd05112   160 GTKFpvkWSSPEVFSFSRYSSKSDVWSFGVLMWEVFsEGKIPY--ENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHC 237
                         250
                  ....*....|....*
gi 1024249297 500 LEMDVDRRGSAKELL 514
Cdd:cd05112   238 WKERPEDRPSFSLLL 252
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
252-519 1.02e-19

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 90.42  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 252 LEKLRSIVSVGDPKK----KYTRFEKI---GQGASGTVYTA-LDIATGQEVAIKQM---NLQQQPKKELIINEILVMREN 320
Cdd:PTZ00426    9 LHKKKDSDSTKEPKRknkmKYEDFNFIrtlGTGSFGRVILAtYKNEDFPPVAIKRFeksKIIKQKQVDHVFSERKILNYI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 321 KNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTET--------CMDEGQIAAVcreclqaLDFLHSNQVIHRDIKSDN 392
Cdd:PTZ00426   89 NHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNkrfpndvgCFYAAQIVLI-------FEYLQSLNIVYRDLKPEN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 393 ILLGMDGSVKLTDFGFCAQItpeQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLrALY 472
Cdd:PTZ00426  162 LLLDKDGFIKMTDFGFAKVV---DTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPL-LIY 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 473 LIATNGTpeLQNPERLSAVFRDFLNRCLEMDVDRR-----GSAKELLQHPFL 519
Cdd:PTZ00426  238 QKILEGI--IYFPKFLDNNCKHLMKKLLSHDLTKRygnlkKGAQNVKEHPWF 287
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
268-539 1.10e-19

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: 90.05  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLa 346
Cdd:cd07872     8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYL- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 ggsltDVVTETCMDE-GQIAAV------CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 419
Cdd:cd07872    87 -----DKDLKQYMDDcGNIMSMhnvkifLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPELQNPERLSAV--FRDF 495
Cdd:cd07872   162 SNEVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIfRLLGTPTEETWPGISSNdeFKNY 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297 496 ------------------------LNRCLEMDVDRRGSAKELLQHPFLKlakplsSLTPLIIAAKEAI 539
Cdd:cd07872   242 nfpkykpqplinhaprldtegielLTKFLQYESKKRISAEEAMKHAYFR------SLGTRIHSLPESI 303
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
274-463 1.38e-19

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: 88.30  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKqMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLtdv 353
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALK-MN-TLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 354 vtETCMDEGQIAAVCRECLQALD------FLHSNQVIHRDIKSDNILLGMDG---SVKLTDFGFCAQItPEQSKRS---T 421
Cdd:cd14155    76 --EQLLDSNEPLSWTVRVKLALDiarglsYLHSKGIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEKI-PDYSDGKeklA 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 422 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM---VEGEPPYL 463
Cdd:cd14155   153 VVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIiarIQADPDYL 197
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
274-519 1.52e-19

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: 88.49  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQ------QQPKKELIINEILVMRENKN--PNIVNYLDSYLVGDELWVVMEYL 345
Cdd:cd14100     8 LGSGGFGSVYSGIRVADGAPVAIKHVEKDrvsewgELPNGTRVPMEIVLLKKVGSgfRGVIRLLDWFERPDSFVLVLERP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AG-GSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD-GSVKLTDFGFCAQItpEQSKRSTM 422
Cdd:cd14100    88 EPvQDLFDFITERgALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNtGELKLIDFGSGALL--KDTVYTDF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-LNENPLRALYLIATNGTPELQNperlsavfrdFLNRCL 500
Cdd:cd14100   166 DGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFeHDEEIIRGQVFFRQRVSSECQH----------LIKWCL 235
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd14100   236 ALRPSDRPSFEDIQNHPWM 254
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
258-519 1.96e-19

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: 89.55  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 258 IVSVGDP-KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQM-NLQ---QQPKKELIINEILVMRENKN-PNIVNYLDS 331
Cdd:cd14134     3 IYKPGDLlTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrNVEkyrEAAKIEIDVLETLAEKDPNGkSHCVQLRDW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 332 YLVGDELWVVMEYLaGGSLTDVVTETC-----MDegQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGS------ 400
Cdd:cd14134    83 FDYRGHMCIVFELL-GPSLYDFLKKNNygpfpLE--HVQHIAKQLLEAVAFLHDLKLTHTDLKPENILL-VDSDyvkvyn 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 401 --------------VKLTDFGFCaqiTPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIE------------ 454
Cdd:cd14134   159 pkkkrqirvpkstdIKLIDFGSA---TFDDEYHSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVElytgellfqthd 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 455 ------MVE---GEPPY--LNENPLRALYLIATNGT---PELQ--------NPERLSAVFR----------DFLNRCLEM 502
Cdd:cd14134   236 nlehlaMMErilGPLPKrmIRRAKKGAKYFYFYHGRldwPEGSssgrsikrVCKPLKRLMLlvdpehrllfDLIRKMLEY 315
                         330
                  ....*....|....*..
gi 1024249297 503 DVDRRGSAKELLQHPFL 519
Cdd:cd14134   316 DPSKRITAKEALKHPFF 332
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-531 2.18e-19

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: 89.16  E-value: 2.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEliiNEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 352
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQ---REVAALRLcQSHPNIVALHEVLHDQYHTYLVMELLRGGELLD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTETCM-DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS---VKLTDFGFcAQITPEQSK-RSTMVGTPY 427
Cdd:cd14180    91 RIKKKARfSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGF-ARLRPQGSRpLQTPCFTLQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA------TNGTPELQNP--ERLSAVFRDFLNRC 499
Cdd:cd14180   170 YAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHAAdimhkiKEGDFSLEGEawKGVSEEAKDLVRGL 249
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024249297 500 LEMDVDRRGSAKELLQHPFLKLAKPLSSlTPL 531
Cdd:cd14180   250 LTVDPAKRLKLSELRESDWLQGGSALSS-TPL 280
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
268-519 2.76e-19

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: 88.14  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd07871     7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GG---SLTDVVTETCMDEGQIAAVcrECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFC-AQITPEQSKRSTM 422
Cdd:cd07871    87 SDlkqYLDNCGNLMSMHNVKIFMF--QLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLArAKSVPTKTYSNEV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VgTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPE------------------- 481
Cdd:cd07871   165 V-TLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIfRLLGTPTeetwpgvtsneefrsylfp 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 482 -------LQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07871   244 qyraqplINHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
274-520 3.22e-19

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: 88.18  E-value: 3.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 350
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 T---DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTmVGTPY 427
Cdd:cd05605    88 KfhiYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRGR-VGTVG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY--LNENPLRALYLIATNGTPELQNpERLSAVFRDFLNRCLEMDVD 505
Cdd:cd05605   167 YMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFraRKEKVKREEVDRRVKEDQEEYS-EKFSEEAKSICSQLLQKDPK 245
                         250       260
                  ....*....|....*....|
gi 1024249297 506 -----RRGSAKELLQHPFLK 520
Cdd:cd05605   246 trlgcRGEGAEDVKSHPFFK 265
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
275-519 3.60e-19

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: 87.76  E-value: 3.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 275 GQGASGTVYTALDIATGQEVAI-----KQMNLQQQPKKELIInEILV-----MRENKNPNIVNYLDSYLVGDE-LWVVME 343
Cdd:cd14011     5 GPGLPWKIYNGSKKSTKQEVSVfvfekKQLEEYSKRDREQIL-ELLKrgvkqLTRLRHPRILTVQHPLEESREsLAFATE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGgSLTDVVTET--------CMDEGQIAAV--CRECLQ---ALDFLHSNQ-VIHRDIKSDNILLGMDGSVKLTDFGFC 409
Cdd:cd14011    84 PVFA-SLANVLGERdnmpspppELQDYKLYDVeiKYGLLQiseALSFLHNDVkLVHGNICPESVVINSNGEWKLAGFDFC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 410 AQITP-----------EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPYLNENPLRALY-LIAT 476
Cdd:cd14011   163 ISSEQatdqfpyfreyDPNLPPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSYKkNSNQ 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1024249297 477 NGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14011   243 LRQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPFF 285
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
274-520 5.15e-19

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: 88.18  E-value: 5.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMR---ENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetLALNERIMLSlvsTGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRStmVGTP 426
Cdd:cd14223    88 GDLHYHLSQhGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHAS--VGTH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 427 YWMAPEVVTRK-AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVD 505
Cdd:cd14223   166 GYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVN 245
                         250       260
                  ....*....|....*....|
gi 1024249297 506 RR-----GSAKELLQHPFLK 520
Cdd:cd14223   246 RRlgcmgRGAQEVKEEPFFR 265
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
274-519 6.33e-19

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: 86.55  E-value: 6.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMnLQQQPKKELIINEILVMRE----NKNPN----IVNYLDSYLVGDELWVVMEYL 345
Cdd:cd14102     8 LGSGGFGTVYAGSRIADGLPVAVKHV-VKERVTEWGTLNGVMVPLEivllKKVGSgfrgVIKLLDWYERPDGFLIVMERP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 A-GGSLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM-DGSVKLTDFGFCAQItpEQSKRSTM 422
Cdd:cd14102    87 EpVKDLFDFITEKgALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLrTGELKLIDFGSGALL--KDTVYTDF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-LNENPLRALYLIATNGTPELQNperlsavfrdFLNRCL 500
Cdd:cd14102   165 DGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFeQDEEILRGRLYFRRRVSPECQQ----------LIKWCL 234
                         250
                  ....*....|....*....
gi 1024249297 501 EMDVDRRGSAKELLQHPFL 519
Cdd:cd14102   235 SLRPSDRPTLEQIFDHPWM 253
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
266-464 6.52e-19

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: 87.27  E-value: 6.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKK-----ELIINEILVMRENknPNIVNYLDSYLVGDELWV 340
Cdd:cd05607     2 KYFYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKsgekmALLEKEILEKVNS--PFIVSLAYAFETKTHLCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLAGGSLT---DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItPEQS 417
Cdd:cd05607    80 VMSLMNGGDLKyhiYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEV-KEGK 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1024249297 418 KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN 464
Cdd:cd05607   159 PITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRD 205
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
274-520 6.54e-19

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: 88.19  E-value: 6.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKE---LIINEILVMR---ENKNPNIVNYLDSYLVGDELWVVMEYLAG 347
Cdd:cd05633    13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgetLALNERIMLSlvsTGDCPFIVCMTYAFHTPDKLCFILDLMNG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRStmVGTP 426
Cdd:cd05633    93 GDLHYHLSQhGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHAS--VGTH 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 427 YWMAPEVVTR-KAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVD 505
Cdd:cd05633   171 GYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSPELKSLLEGLLQRDVS 250
                         250       260
                  ....*....|....*....|
gi 1024249297 506 RR-----GSAKELLQHPFLK 520
Cdd:cd05633   251 KRlgchgRGAQEVKEHSFFK 270
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
291-511 6.56e-19

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: 86.68  E-value: 6.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 291 GQEVAIKQMNLQQQPKKElIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDV--VTETCMDEGQIAAVC 368
Cdd:cd13992    25 GRTVAIKHITFSRTEKRT-ILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVllNREIKMDWMFKSSFI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 369 RECLQALDFLHSNQVI-HRDIKSDNILLGMDGSVKLTDFGfCAQITPEQSKRSTMVGTPY----WMAPEVVTRKAYG--- 440
Cdd:cd13992   104 KDIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFG-LRNLLEEQTNHQLDEDAQHkkllWTAPELLRGSLLEvrg 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 441 -PKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT----PEL-----QNPERLSAVFRDflnrCLEMDVDRRGSA 510
Cdd:cd13992   183 tQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNkpfrPELavlldEFPPRLVLLVKQ----CWAENPEKRPSF 258

                  .
gi 1024249297 511 K 511
Cdd:cd13992   259 K 259
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
272-518 8.76e-19

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 86.56  E-value: 8.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGT-VYTAldIATGQEVAIKQMNLQQQpkkELIINEILVMRENKN-PNIVNYLDSYLVGDELWVVMEyLAGGS 349
Cdd:cd13982     7 KVLGYGSEGTiVFRG--TFDGRPVAVKRLLPEFF---DFADREVQLLRESDEhPNVIRYFCTEKDRQFLYIALE-LCAAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVT--ETCMDEGQIAAVCRECLQ----ALDFLHSNQVIHRDIKSDNILLGMDGS-----VKLTDFGFCAQITPEQS- 417
Cdd:cd13982    81 LQDLVEspRESKLFLRPGLEPVRLLRqiasGLAHLHSLNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCKKLDVGRSs 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 --KRSTMVGTPYWMAPEV--------VTRkaygpKVDIWSLG-IMAIEMVEGEPPYlnENPLRALYLIATN--GTPELQN 484
Cdd:cd13982   161 fsRRSGVAGTSGWIAPEMlsgstkrrQTR-----AVDIFSLGcVFYYVLSGGSHPF--GDKLEREANILKGkySLDKLLS 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024249297 485 PERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPF 518
Cdd:cd13982   234 LGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHPF 267
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
264-477 9.05e-19

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: 86.33  E-value: 9.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALdIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05148     4 PREEFTLERKLGSGYFGEVWEGL-WKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTETcmdEGQIAAVCR------ECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQS 417
Cdd:cd05148    83 LMEKGSLLAFLRSP---EGQVLPVASlidmacQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGL-ARLIKEDV 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 418 KRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATN 477
Cdd:cd05148   159 YLSSDKKIPYkWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAG 220
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-462 9.77e-19

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: 87.02  E-value: 9.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEliiNEILVMRE-NKNPNIVNYLDSYlvGDEL--WVVMEYLAGGSL 350
Cdd:cd14179    15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQ---REIAALKLcEGHPNIVKLHEVY--HDQLhtFLVMELLKGGEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 351 TD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL---GMDGSVKLTDFGFCAQITPEQSKRSTMVGTP 426
Cdd:cd14179    90 LErIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQPLKTPCFTL 169
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1024249297 427 YWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd14179   170 HYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPF 205
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
226-543 1.21e-18

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 88.55  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 226 ENANSStlyrNTDRQRKKSKMTDEEILeklRSivsvgdPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQP 305
Cdd:PTZ00036   39 ERSHNN----NAGEDEDEEKMIDNDIN---RS------PNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 306 KKEliinEILVMRENKNPNIVnYLDSYLVGDE---------LWVVMEYLAGG--------SLTDVVTETCMDEGQIAAVC 368
Cdd:PTZ00036  106 KNR----ELLIMKNLNHINII-FLKDYYYTECfkkneknifLNVVMEFIPQTvhkymkhyARNNHALPLFLVKLYSYQLC 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 369 ReclqALDFLHSNQVIHRDIKSDNILLGMDG-SVKLTDFGFCAQITPEQsKRSTMVGTPYWMAPEVVTRKA-YGPKVDIW 446
Cdd:PTZ00036  181 R----ALAYIHSKFICHRDLKPQNLLIDPNThTLKLCDFGSAKNLLAGQ-RSVSYICSRFYRAPELMLGATnYTTHIDLW 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 447 SLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTP-----ELQNPERLSAVFRD--------------------FLNRCL 500
Cdd:PTZ00036  256 SLGCIIAEMILGYPIFSGQSSVDQLVrIIQVLGTPtedqlKEMNPNYADIKFPDvkpkdlkkvfpkgtpddainFISQFL 335
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 501 EMDVDRRGSAKELLQHPF--------LKLAKPLSSLTPLIIAAKEAIKNSS 543
Cdd:PTZ00036  336 KYEPLKRLNPIEALADPFfddlrdpcIKLPKYIDKLPDLFNFCDAEIKEMS 386
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
274-461 1.22e-18

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: 86.01  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTaLDIATGQEVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 352
Cdd:cd14664     1 IGRGGAGTVYK-GVMPNGTLVAVKRLKGEGTQGGDHgFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTETCMDEGQI--AAVCRECLQA---LDFLH---SNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV- 423
Cdd:cd14664    80 LLHSRPESQPPLdwETRQRIALGSargLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMSSVa 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1024249297 424 GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPP 461
Cdd:cd14664   160 GSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRP 197
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
267-523 1.56e-18

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: 85.93  E-value: 1.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKI---GQGASGTVYTALDIATGQ----EVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLvGDEL 338
Cdd:cd05057     5 KETELEKGkvlGSGAFGTVYKGVWIPEGEkvkiPVAIKVLREETGPKaNEEILDEAYVMASVDHPHLVRLLGICL-SSQV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGGSLTDVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ 416
Cdd:cd05057    84 QLITQLMPLGCLLDYVRNhrDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVG-TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLNEnPLRALYLIATNGTpELQNPERLSAVFR 493
Cdd:cd05057   164 KEYHAEGGkVPIkWMALESIQYRIYTHKSDVWSYGVTVWElMTFGAKPYEGI-PAVEIPDLLEKGE-RLPQPPICTIDVY 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQHpFLKLAK 523
Cdd:cd05057   242 MVLVKCWMIDAESRPTFKELANE-FSKMAR 270
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
271-455 1.79e-18

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: 85.84  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEKIGQGASGTV----YTALDIATGQEVAIKQmnLQQQPKKEL--IINEILVMRENKNPNIVNYLD-SYLVG-DELWVVM 342
Cdd:cd14205     9 LQQLGKGNFGSVemcrYDPLQDNTGEVVAVKK--LQHSTEEHLrdFEREIEILKSLQHDNIVKYKGvCYSAGrRNLRLIM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPeQSKRS 420
Cdd:cd14205    87 EYLPYGSLRDYLQKHKerIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGL-TKVLP-QDKEY 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTP-----YWMAPEVVTRKAYGPKVDIWSLGIMAIEM 455
Cdd:cd14205   165 YKVKEPgespiFWYAPESLTESKFSVASDVWSFGVVLYEL 204
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
266-513 3.05e-18

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: 84.54  E-value: 3.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALdiATGQEVAIKqmNLQQQPKKELIINEILVMRENKNPNIVNYLdSYLVGDELWVVMEYL 345
Cdd:cd05083     6 QKLTLGEIIGEGEFGAVLQGE--YMGQKVAVK--NIKCDVTAQAFLEETAVMTKLQHKNLVRLL-GVILHNGLYIVMELM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVT---ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRSTM 422
Cdd:cd05083    81 SKGNLVNFLRsrgRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGL-AKVGSMGVDNSRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 vgtPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYlnenPLRALYLI--ATNGTPELQNPERLSAVFRDFLNR 498
Cdd:cd05083   160 ---PVkWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY----PKMSVKEVkeAVEKGYRMEPPEGCPPDVYSIMTS 232
                         250
                  ....*....|....*
gi 1024249297 499 CLEMDVDRRGSAKEL 513
Cdd:cd05083   233 CWEAEPGKRPSFKKL 247
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
272-450 3.77e-18

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 85.11  E-value: 3.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALdiATGQEVAIK--QMNLQQQPKKELIINEILVMRenkNPNIVNYL--DSYLVGDELW---VVMEY 344
Cdd:cd14054     1 QLIGQGRYGTVWKGS--LDERPVAVKvfPARHRQNFQNEKDIYELPLME---HSNILRFIgaDERPTADGRMeylLVLEY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQ---------VIHRDIKSDNILLGMDGSVKLTDFGFCAQIT-- 413
Cdd:cd14054    76 APKGSLCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKADGSCVICDFGLAMVLRgs 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 414 --------PEQSKRSTMVGTPYWMAPEVV-------TRKAYGPKVDIWSLGI 450
Cdd:cd14054   156 slvrgrpgAAENASISEVGTLRYMAPEVLegavnlrDCESALKQVDVYALGL 207
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
263-462 3.99e-18

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: 84.16  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKkYTRFEKIGQGASGTVytALDIATGQ-EVAIKQMNLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd05113     2 DPKD-LTFLKELGTGQFGVV--KYGKWRGQyDVAIKMIKEGSMSEDEFI-EEAKVMMNLSHEKLVQLYGVCTKQRPIFII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 419
Cdd:cd05113    78 TEYMANGCLLNYLREMRkrFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTS 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1024249297 420 StmVGTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05113   158 S--VGSKFpvrWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPY 202
pknD PRK13184
serine/threonine-protein kinase PknD;
267-515 4.24e-18

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 88.29  E-value: 4.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMnlqqqpKKELIINEIL---VMRENK------NPNIVNYLDSYLVGDE 337
Cdd:PRK13184    3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKI------REDLSENPLLkkrFLREAKiaadliHPGIVPVYSICSDGDP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLT---------DVVTETCMDEGQIAA-------VCreclQALDFLHSNQVIHRDIKSDNILLGMDGSV 401
Cdd:PRK13184   77 VYYTMPYIEGYTLKsllksvwqkESLSKELAEKTSVGAflsifhkIC----ATIEYVHSKGVLHRDLKPDNILLGLFGEV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 402 KLTDFGFCAQITPEQ------------SKRSTM------VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL 463
Cdd:PRK13184  153 VILDWGAAIFKKLEEedlldidvdernICYSSMtipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297 464 NENpLRALYLIATNGTPELQNPER-----LSAVfrdfLNRCLEMD-VDRRGSAKELLQ 515
Cdd:PRK13184  233 RKK-GRKISYRDVILSPIEVAPYReippfLSQI----AMKALAVDpAERYSSVQELKQ 285
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
264-515 6.08e-18

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: 84.25  E-value: 6.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVY--TALDIATGQ---EVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDE 337
Cdd:cd05061     4 SREKITLLRELGQGSFGMVYegNARDIIKGEaetRVAVKTVNESASLRERIeFLNEASVMKGFTCHHVVRLLGVVSKGQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVV----TETCMDEGQIAAVCRECLQ-------ALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 406
Cdd:cd05061    84 TLVVMELMAHGDLKSYLrslrPEAENNPGRPPPTLQEMIQmaaeiadGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 407 GFCAQITPEQSKRSTMVG-TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGTpeLQ 483
Cdd:cd05061   164 GMTRDIYETDYYRKGGKGlLPVrWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVMDGGY--LD 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1024249297 484 NPERLSAVFRDFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd05061   242 QPDNCPERVTDLMRMCWQFNPKMRPTFLEIVN 273
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
272-462 9.47e-18

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 83.86  E-value: 9.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALdiATGQEVAIKQMNLQQQP--KKELIINEILVMRenkNPNIVNYLDSYLVGD----ELWVVMEYL 345
Cdd:cd14056     1 KTIGKGRYGEVWLGK--YRGEKVAVKIFSSRDEDswFRETEIYQTVMLR---HENILGFIAADIKSTgswtQLWLITEYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSN--------QVIHRDIKSDNILLGMDGSVKLTDFG----FCAQIT 413
Cdd:cd14056    76 EHGSLYDYLQRNTLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCIADLGlavrYDSDTN 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 414 PEQSKRSTMVGTPYWMAPEVVTrKAYGPK-------VDIWSLGIMAIEMV----------EGEPPY 462
Cdd:cd14056   156 TIDIPPNPRVGTKRYMAPEVLD-DSINPKsfesfkmADIYSFGLVLWEIArrceiggiaeEYQLPY 220
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
272-450 1.43e-17

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: 82.86  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQE---VAIKQMNLQQQP-KKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAG 347
Cdd:cd05056    12 RCIGEGQFGDVYQGVYMSPENEkiaVAVKTCKNCTSPsVREKFLQEAYIMRQFDHPHIVK-LIGVITENPVWIVMELAPL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVtETCMDEGQIAAVCRECLQ---ALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG 424
Cdd:cd05056    91 GELRSYL-QVNKYSLDLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKASKGK 169
                         170       180
                  ....*....|....*....|....*..
gi 1024249297 425 TPY-WMAPEVVTRKAYGPKVDIWSLGI 450
Cdd:cd05056   170 LPIkWMAPESINFRRFTSASDVWMFGV 196
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
274-514 1.46e-17

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: 82.85  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVY--TALDI---ATG-QEVAIKqmNLQQ----QPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05044     3 LGSGAFGEVFegTAKDIlgdGSGeTKVAVK--TLRKgatdQEKAEFL-KEAHLMSNFKHPNILKLLGVCLDNDPQYIILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGG-------------------SLTDVVtETCMDegqiaaVCREC--LQALDFlhsnqvIHRDIKSDNILLGMDGS-- 400
Cdd:cd05044    80 LMEGGdllsylraarptaftppllTLKDLL-SICVD------VAKGCvyLEDMHF------VHRDLAARNCLVSSKDYre 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 401 --VKLTDFGFCAQITPEQSKRSTMVGT-PY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLNENPLRALYLIA 475
Cdd:cd05044   147 rvVKIGDFGLARDIYKNDYYRKEGEGLlPVrWMAPESLVDGVFTTQSDVWAFGVLMWEiLTLGQQPYPARNNLEVLHFVR 226
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1024249297 476 TNGtpELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELL 514
Cdd:cd05044   227 AGG--RLDQPDNCPDDLYELMLRCWSTDPEERPSFARIL 263
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
271-515 1.59e-17

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: 82.78  E-value: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEKIGQGASGTVYTALdiaTGQEVAIK--QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd14063     5 KEVIGKGRFGRVHRGR---WHGDVAIKllNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCKGR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTE--TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGmDGSVKLTDFGF--CAQITPEQSKRSTMVG 424
Cdd:cd14063    82 TLYSLIHErkEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDFGLfsLSGLLQPGRREDTLVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPYW---MAPEVVT----------RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNpERLSAV 491
Cdd:cd14063   161 PNGWlcyLAPEIIRalspdldfeeSLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGKKQSLSQ-LDIGRE 239
                         250       260
                  ....*....|....*....|....
gi 1024249297 492 FRDFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd14063   240 VKDILMQCWAYDPEKRPTFSDLLR 263
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
267-519 2.28e-17

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: 83.57  E-value: 2.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMN--LQQQPKKELIINEILVMRENKNPNIVNYLDsylvgdelwvVMEY 344
Cdd:cd07858     6 KYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIAnaFDNRIDAKRTLREIKLLRHLDHENVIAIKD----------IMPP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDV--VTETcMDEG--QIAAV--------CR----ECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGF 408
Cdd:cd07858    76 PHREAFNDVyiVYEL-MDTDlhQIIRSsqtlsddhCQyflyQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 409 cAQITPEQSKRST-MVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPE---- 481
Cdd:cd07858   155 -ARTTSEKGDFMTeYVVTRWYRAPELLLNCSeYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLItELLGSPSeedl 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 482 --LQNPE--------------RLSAVFR-------DFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd07858   234 gfIRNEKarryirslpytprqSFARLFPhanplaiDLLEKMLVFDPSKRITVEEALAHPYL 294
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
282-519 2.85e-17

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 81.81  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 282 VYTALDIATGQEVA--------IKQMNLQQQPKKELIINEILVmrenKNPNIVNY----LDSYLVGDELWVVMEYLAGGS 349
Cdd:cd13984    10 AYLAMDTEEGVEVVwnevqfseRKIFKAQEEKIRAVFDNLIQL----DHPNIVKFhrywTDVQEEKARVIFITEYMSSGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTET-----CMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLtdfgfcAQITPEQSKRSTM 422
Cdd:cd13984    86 LKQFLKKTkknhkTMNEKSWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI------GSVAPDAIHNHVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 V-----GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV------EGEPPYLN-ENPLRALYLiatngtpeLQNPERlsa 490
Cdd:cd13984   160 TcreehRNLHFFAPEYGYLEDVTTAVDIYSFGMCALEMAaleiqsNGEKVSANeEAIIRAIFS--------LEDPLQ--- 228
                         250       260
                  ....*....|....*....|....*....
gi 1024249297 491 vfRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd13984   229 --KDFIRKCLSVAPQDRPSARDLLFHPVL 255
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
274-455 3.37e-17

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: 81.86  E-value: 3.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTV----YTALDIATGQEVAIKQmnLQQQPKKEL--IINEILVMRENKNPNIVNYLD-SYLVG-DELWVVMEYL 345
Cdd:cd05081    12 LGKGNFGSVelcrYDPLGDNTGALVAVKQ--LQHSGPDQQrdFQREIQILKALHSDFIVKYRGvSYGPGrRSLRLVMEYL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVV--TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPeQSKRSTMV 423
Cdd:cd05081    90 PSGCLRDFLqrHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGL-AKLLP-LDKDYYVV 167
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1024249297 424 GTP-----YWMAPEVVTRKAYGPKVDIWSLGIMAIEM 455
Cdd:cd05081   168 REPgqspiFWYAPESLSDNIFSRQSDVWSFGVVLYEL 204
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
272-468 8.08e-17

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 80.95  E-value: 8.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTA-LDiatGQEVAIKQMNLQ--QQPKKELIINEILVMrenKNPNIVNYLDS----YLVGDELWVVMEY 344
Cdd:cd13998     1 EVIGKGRFGEVWKAsLK---NEPVAVKIFSSRdkQSWFREKEIYRTPML---KHENILQFIAAderdTALRTELWLVTAF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVI---------HRDIKSDNILLGMDGSVKLTDFGFCAQITPE 415
Cdd:cd13998    75 HPNGSL*DYLSLHTIDWVSLCRLALSVARGLAHLHSEIPGctqgkpaiaHRDLKSKNILVKNDGTCCIADFGLAVRLSPS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024249297 416 QSK----RSTMVGTPYWMAPEV------VTRKAYGPKVDIWSLGIMAIEMV-----------EGEPPYLNENPL 468
Cdd:cd13998   155 TGEednaNNGQVGTKRYMAPEVlegainLRDFESFKRVDIYAMGLVLWEMAsrctdlfgiveEYKPPFYSEVPN 228
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
268-480 8.46e-17

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: 81.28  E-value: 8.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELI-INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYla 346
Cdd:cd07869     7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTaIREASLLKGLKHANIVLLHDIIHTKETLTLVFEY-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 ggsltdVVTETC--MDE-------GQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:cd07869    85 ------VHTDLCqyMDKhpgglhpENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSH 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297 418 KRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLN----ENPLRALYLIAtnGTP 480
Cdd:cd07869   159 TYSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmkdiQDQLERIFLVL--GTP 224
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
267-519 1.15e-16

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: 81.72  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIK----QMNLQQQPKKELIINEILVMRENKNP-NIVNYLDSYLVGDELWVV 341
Cdd:cd14224    66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKmvrnEKRFHRQAAEEIRILEHLKKQDKDNTmNVIHMLESFTFRNHICMT 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGgSLTDVVTETCMDEGQIAAV---CRECLQALDFLHSNQVIHRDIKSDNILLGMDG--SVKLTDFG-FCAqitpE 415
Cdd:cd14224   146 FELLSM-NLYELIKKNKFQGFSLQLVrkfAHSILQCLDALHRNKIIHCDLKPENILLKQQGrsGIKVIDFGsSCY----E 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEP----------------------PYLNENPLRALYL 473
Cdd:cd14224   221 HQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPlfpgedegdqlacmiellgmppQKLLETSKRAKNF 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 474 IATNGTPELQNPERLS----------------------------------AVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14224   301 ISSKGYPRYCTVTTLPdgsvvlnggrsrrgkmrgppgskdwvtalkgcddPLFLDFLKRCLEWDPAARMTPSQALRHPWL 380
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
271-507 1.44e-16

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: 79.85  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 271 FEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDsyLVGDELWVVMEYLAGG 348
Cdd:cd14025     1 WEKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERmeLLEEAKKMEMAKFRHILPVYG--ICSEPVGLVMEYMETG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVV-TETCMDEGQIAAVcRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFGFC---AQITPEQSKRSTM 422
Cdd:cd14025    79 SLEKLLaSEPLPWELRFRII-HETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAkwnGLSHSHDLSRDGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRK--AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGT-PEL-----QNPERLSAVFrD 494
Cdd:cd14025   158 RGTIAYLPPERFKEKnrCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKGHrPSLspiprQRPSECQQMI-C 236
                         250
                  ....*....|...
gi 1024249297 495 FLNRCLEMDVDRR 507
Cdd:cd14025   237 LMKRCWDQDPRKR 249
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
266-464 1.73e-16

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: 79.94  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEK-IGQGASGTV----YTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLD--SYLVGDE 337
Cdd:cd05080     3 KRYLKKIRdLGEGHFGKVslycYDPTNDGTGEMVAVKALKADCGPQhRSGWKQEIDILKTLYHENIVKYKGccSEQGGKS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI-TPEQ 416
Cdd:cd05080    83 LQLIMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVpEGHE 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 417 SKRSTMVG-TP-YWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN 464
Cdd:cd05080   163 YYRVREDGdSPvFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQS 212
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
267-523 2.33e-16

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: 79.30  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKI---GQGASGTVYTALDIATGQE----VAIKQMNLQQQPK--KElIINEILVMRENKNPNIVNYLDSYLVgDE 337
Cdd:cd05109     5 KETELKKVkvlGSGAFGTVYKGIWIPDGENvkipVAIKVLRENTSPKanKE-ILDEAYVMAGVGSPYVCRLLGICLT-ST 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTEtcmDEGQIAAV-----CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 412
Cdd:cd05109    83 VQLVTQLMPYGCLLDYVRE---NKDRIGSQdllnwCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQSKRSTMVG-TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYlNENPLRALYLIATNGTPELQNPERLS 489
Cdd:cd05109   160 DIDETEYHADGGkVPIkWMALESILHRRFTHQSDVWSYGVTVWElMTFGAKPY-DGIPAREIPDLLEKGERLPQPPICTI 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1024249297 490 AVFRdFLNRCLEMDVDRRGSAKELLqHPFLKLAK 523
Cdd:cd05109   239 DVYM-IMVKCWMIDSECRPRFRELV-DEFSRMAR 270
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
267-464 3.96e-16

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 78.57  E-value: 3.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEK-IGQGASGTVYTALDIATGQE---VAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd05033     4 SYVTIEKvIGGGEFGEVCSGSLKLPGKKeidVAIKTLKSGYSDKQRLdFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETcmDE----GQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:cd05033    84 TEYMENGSLDKFLREN--DGkftvTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEA 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 418 KRSTMVG-TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLN 464
Cdd:cd05033   162 TYTTKGGkIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEvMSYGERPYWD 211
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
372-451 4.72e-16

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: 78.30  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 372 LQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCaqiTPEQSKRSTMVGTPYWMAPEVVTRKaYGPKVDIWSLGIM 451
Cdd:cd13975   112 VEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFSGK-YDNSVDVYAFGIL 187
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
267-517 8.26e-16

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: 77.66  E-value: 8.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQmnlQQQPKKELIiNEILVMRE-------NKNPNIVNYLDSYLVGDELW 339
Cdd:cd14139     1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKR---SMRPFAGSS-NEQLALHEvyahavlGHHPHVVRYYSAWAEDDHMI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGGSLTDVVTETC-----MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNIL----LGMDGSV--------- 401
Cdd:cd14139    77 IQNEYCNGGSLQDAISENTksgnhFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFichkMQSSSGVgeevsneed 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 402 ---------KLTDFGFCAQITPEQSKRstmvGTPYWMAPEVVTRK-AYGPKVDIWSLGiMAIEMVEGEPPyLNENPlRAL 471
Cdd:cd14139   157 eflsanvvyKIGDLGHVTSINKPQVEE----GDSRFLANEILQEDyRHLPKADIFALG-LTVALAAGAEP-LPTNG-AAW 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 472 YLIATNGTPELqnPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHP 517
Cdd:cd14139   230 HHIRKGNFPDV--PQELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
272-515 9.22e-16

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: 77.28  E-value: 9.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS- 349
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDlKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDf 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQitpEQ----SKRSTMVG 424
Cdd:cd05084    82 LTFLRTEGPrLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSRE---EEdgvyAATGGMKQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 425 TPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLN-------ENPLRALYLIATNGTPElqnperlsAVFRdF 495
Cdd:cd05084   159 IPVkWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANlsnqqtrEAVEQGVRLPCPENCPD--------EVYR-L 229
                         250       260
                  ....*....|....*....|
gi 1024249297 496 LNRCLEMDVDRRGSAKELLQ 515
Cdd:cd05084   230 MEQCWEYDPRKRPSFSTVHQ 249
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
274-470 9.61e-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: 77.18  E-value: 9.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALdiATGQEVAIKQ---MNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVG-DELWVVMEYLAGGS 349
Cdd:cd14064     1 IGSGSFGKVYKGR--CRNKIVAIKRyraNTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDpSQFAIVTQYVSGGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTET--CMDEGQIAAVCRECLQALDFLH--SNQVIHRDIKSDNILLGMDGSVKLTDFG---FCAQItpEQSKRSTM 422
Cdd:cd14064    79 LFSLLHEQkrVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGesrFLQSL--DEDNMTKQ 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1024249297 423 VGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRA 470
Cdd:cd14064   157 PGNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPFAHLKPAAA 205
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
267-519 9.77e-16

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: 78.42  E-value: 9.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATG-QEVAIKQMN----LQQQPKKELiinEILVMRENKNPN----IVNYLDSYLVGDE 337
Cdd:cd14135     1 RYRVYGYLGKGVFSNVVRARDLARGnQEVAIKIIRnnelMHKAGLKEL---EILKKLNDADPDdkkhCIRLLRHFEHKNH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGgSLTDVVTETCMDEG-QIAAV---CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSV-KLTDFGFCA-- 410
Cdd:cd14135    78 LCLVFESLSM-NLREVLKKYGKNVGlNIKAVrsyAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTlKLCDFGSASdi 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 ---QITPEQSKRstmvgtpYWMAPEVVTRKAYGPKVDIWSLGIMAIEM---------------------VEGEPP----- 461
Cdd:cd14135   157 genEITPYLVSR-------FYRAPEIILGLPYDYPIDMWSVGCTLYELytgkilfpgktnnhmlklmmdLKGKFPkkmlr 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 462 -------YLNEN------------------------PLRALY--LIATNGTPELQNPERLSavFRDFLNRCLEMDVDRRG 508
Cdd:cd14135   230 kgqfkdqHFDENlnfiyrevdkvtkkevrrvmsdikPTKDLKtlLIGKQRLPDEDRKKLLQ--LKDLLDKCLMLDPEKRI 307
                         330
                  ....*....|.
gi 1024249297 509 SAKELLQHPFL 519
Cdd:cd14135   308 TPNEALQHPFI 318
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
272-517 1.16e-15

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: 77.44  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEVAIKQmnlQQQPKKELIiNEILVMRE-------NKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd14051     6 EKIGSGEFGSVYKCINRLDGCVYAIKK---SKKPVAGSV-DEQNALNEvyahavlGKHPHVVRYYSAWAEDDHMIIQNEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETC-----MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR 419
Cdd:cd14051    82 CNGGSLADAISENEkagerFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSSEEEEEDFEGEEDNPE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STMV--------------------GTPYWMAPEVVtRKAYG--PKVDIWSLGIMAIEMVEGEPpyLNENPlRALYLIATN 477
Cdd:cd14051   162 SNEVtykigdlghvtsisnpqveeGDCRFLANEIL-QENYShlPKADIFALALTVYEAAGGGP--LPKNG-DEWHEIRQG 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1024249297 478 GTPELQNperLSAVFRDFLNRCLEMDVDRRGSAKELLQHP 517
Cdd:cd14051   238 NLPPLPQ---CSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
272-464 1.19e-15

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: 77.44  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATGQEV----AIKQMNLQQQPKKELIINEIL-----VMRENKNPNIVNY--LDSYLVGDeLWV 340
Cdd:cd14001     5 KKLGYGTGVNVYLMKRSPRGGSSrspwAVKKINSKCDKGQRSLYQERLkeeakILKSLNHPNIVGFraFTKSEDGS-LCL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLaGGSLTDVVTETcMDEG-------QIAAVCRECLQALDFLHSN-QVIHRDIKSDNILLGMD-GSVKLTDFGFCAQ 411
Cdd:cd14001    84 AMEYG-GKSLNDLIEER-YEAGlgpfpaaTILKVALSIARALEYLHNEkKILHGDIKSGNVLIKGDfESVKLCDFGVSLP 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 412 ITPEQSKRST----MVGTPYWMAPE------VVTRKAygpkvDIWSLGIMAIEMVEGEPPYLN 464
Cdd:cd14001   162 LTENLEVDSDpkaqYVGTEPWKAKEaleeggVITDKA-----DIFAYGLVLWEMMTLSVPHLN 219
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
267-517 1.45e-15

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: 76.99  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQmnlqqqPKKELI--INEILVMRE-------NKNPNIVNYLDSYLVGDE 337
Cdd:cd14138     6 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKR------SKKPLAgsVDEQNALREvyahavlGQHSHVVRYYSAWAEDDH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTET-----CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM--------------- 397
Cdd:cd14138    80 MLIQNEYCNGGSLADAISENyrimsYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRtsipnaaseegdede 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 398 --DGSV--KLTDFGFCAQITPEQSKRstmvGTPYWMAPEVVTRK-AYGPKVDIWSLGIMAIEMVEGEPPYLNENplrALY 472
Cdd:cd14138   160 waSNKVifKIGDLGHVTRVSSPQVEE----GDSRFLANEVLQENyTHLPKADIFALALTVVCAAGAEPLPTNGD---QWH 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 473 LIATNGTPELqnPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHP 517
Cdd:cd14138   233 EIRQGKLPRI--PQVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
272-513 1.66e-15

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: 76.62  E-value: 1.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTAL-DIATGQE--VAIKQM--NLQQQPKKElIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLA 346
Cdd:cd05060     1 KELGHGNFGSVRKGVyLMKSGKEveVAVKTLkqEHEKAGKKE-FLREASVMAQLDHPCIVR-LIGVCKGEPLMLVMELAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcaqitpeqsKRSTMVGT 425
Cdd:cd05060    79 LGPLLKyLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGM---------SRALGAGS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PY------------WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGtpELQNPERLSAVF 492
Cdd:cd05060   150 DYyrattagrwplkWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLESGE--RLPRPEECPQEI 227
                         250       260
                  ....*....|....*....|.
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKEL 513
Cdd:cd05060   228 YSIMLSCWKYRPEDRPTFSEL 248
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
268-519 2.22e-15

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: 77.29  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQ----QQPKKELIINEILVM---RENKNpNIVNYLDSYLVGDELWV 340
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKpayfRQAMLEIAILTLLNTkydPEDKH-HIVRLLDHFMHHGHLCI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLA-------------GGSLTDVVTETcmdeGQIaavcrecLQALDFLHSNQVIHRDIKSDNILLGMDGS--VKLTD 405
Cdd:cd14212    80 VFELLGvnlyellkqnqfrGLSLQLIRKFL----QQL-------LDALSVLKDARIIHCDLKPENILLVNLDSpeIKLID 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 406 FG-FCAqitpEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIE-------------------MVE--GEPP-- 461
Cdd:cd14212   149 FGsACF----ENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAElflglplfpgnseynqlsrIIEmlGMPPdw 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 462 ---------------------------------------------YLNENPLRAL-----YLIATNGTPELQNPERLSav 491
Cdd:cd14212   225 mlekgkntnkffkkvaksggrstyrlktpeefeaenncklepgkrYFKYKTLEDIimnypMKKSKKEQIDKEMETRLA-- 302
                         330       340
                  ....*....|....*....|....*...
gi 1024249297 492 FRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14212   303 FIDFLKGLLEYDPKKRWTPDQALNHPFI 330
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
270-462 2.37e-15

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: 76.65  E-value: 2.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RF-EKIGQGASGTVYTALDIATGQE-----VAIKQMNLQQQPK-KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 342
Cdd:cd05048     8 RFlEELGEGAFGKVYKGELLGPSSEesaisVAIKTLKENASPKtQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSL----------TDVVTETCMDEGQIAAVCRECLQ-------ALDFLHSNQVIHRDIKSDNILLGMDGSVKLTD 405
Cdd:cd05048    88 EYMAHGDLheflvrhsphSDVGVSSDDDGTASSLDQSDFLHiaiqiaaGMEYLSSHHYVHRDLAARNCLVGDGLTVKISD 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 406 FGFCAQITPE-----QSKRSTMVgtpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05048   168 FGLSRDIYSSdyyrvQSKSLLPV---RWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPY 227
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
266-519 2.69e-15

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 76.63  E-value: 2.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIIN-------EILVMRENKNPNIVNYLDSY-LVGDE 337
Cdd:cd14040     6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILLgMDGS----VKLTDFGFcA 410
Cdd:cd14040    86 FCTVLEYCEGNDLDFYLKQhKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL-VDGTacgeIKITDFGL-S 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 411 QITPEQSK-------RSTMVGTPYWMAPEVVTRKAYGPK----VDIWSLGIMAIEMVEGEPPY---------LNENPLra 470
Cdd:cd14040   164 KIMDDDSYgvdgmdlTSQGAGTYWYLPPECFVVGKEPPKisnkVDVWSVGVIFFQCLYGRKPFghnqsqqdiLQENTI-- 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 471 lyLIATngtpELQNPER--LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14040   242 --LKAT----EVQFPVKpvVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
272-462 2.94e-15

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: 75.40  E-value: 2.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALDIATgQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGT-TKVAVKTLK-PGTMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTEtcmDEG-------------QIAavcreclQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQSK 418
Cdd:cd05034    79 DYLRT---GEGralrlpqlidmaaQIA-------SGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLI--EDDE 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1024249297 419 RSTMVGTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPY 462
Cdd:cd05034   147 YTAREGAKFpikWTAPEAALYGRFTIKSDVWSFGILLYEIVtYGRVPY 194
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
272-462 3.05e-15

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 76.32  E-value: 3.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTALdiATGQEVAIKQMNL--QQQPKKEL-IINEILVMRENknpnIVNYLDSYLVG----DELWVVMEY 344
Cdd:cd14142    11 ECIGKGRYGEVWRGQ--WQGESVAVKIFSSrdEKSWFRETeIYNTVLLRHEN----ILGFIASDMTSrnscTQLWLITHY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHS----NQ----VIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ 416
Cdd:cd14142    85 HENGSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTeifgTQgkpaIAHRDLKSKNILVKSNGQCCIADLGLAVTHSQET 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 417 SK----RSTMVGTPYWMAPEVVTR-------KAYgPKVDIWSLGIMAIE---------MVEG-EPPY 462
Cdd:cd14142   165 NQldvgNNPRVGTKRYMAPEVLDEtintdcfESY-KRVDIYAFGLVLWEvarrcvsggIVEEyKPPF 230
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
274-515 3.38e-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: 76.37  E-value: 3.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATGQE-----VAIKQMN-LQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd05055    43 LGAGAFGKVVEATAYGLSKSdavmkVAVKMLKpTAHSSEREALMSELKIMSHlGNHENIVNLLGACTIGGPILVITEYCC 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVV---TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ---SKRS 420
Cdd:cd05055   123 YGDLLNFLrrkRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSnyvVKGN 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPyWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY----LNENplraLYLIATNGTPELQnPERLSAVFRDF 495
Cdd:cd05055   203 ARLPVK-WMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYpgmpVDSK----FYKLIKEGYRMAQ-PEHAPAEIYDI 276
                         250       260
                  ....*....|....*....|
gi 1024249297 496 LNRCLEMDVDRRGSAKELLQ 515
Cdd:cd05055   277 MKTCWDADPLKRPTFKQIVQ 296
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
270-523 3.77e-15

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 76.26  E-value: 3.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RFEKIGQGASGTVYTALDIATGQEV----AIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLvGDELWVVMEY 344
Cdd:cd05110    11 RVKVLGSGAFGTVYKGIWVPEGETVkipvAIKILNETTGPKANVeFMDEALIMASMDHPHLVRLLGVCL-SPTIQLVTQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETCMDEGQ--IAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 422
Cdd:cd05110    90 MPHGCLLDYVHEHKDNIGSqlLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNAD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTP--YWMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYlNENPLRALYLIATNGTPELQNPERLSAVFRdFLNRC 499
Cdd:cd05110   170 GGKMpiKWMALECIHYRKFTHQSDVWSYGVTIWElMTFGGKPY-DGIPTREIPDLLEKGERLPQPPICTIDVYM-VMVKC 247
                         250       260
                  ....*....|....*....|....
gi 1024249297 500 LEMDVDRRGSAKELLQHpFLKLAK 523
Cdd:cd05110   248 WMIDADSRPKFKELAAE-FSRMAR 270
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
264-462 4.04e-15

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK 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: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 75.89  E-value: 4.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIA-TGQ----EVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDE 337
Cdd:cd05036     4 PRKNLTLIRALGQGAFGEVYEGTVSGmPGDpsplQVAVKTLPELCSEQDEMdFLMEALIMSKFNHPNIVRCIGVCFQRLP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 338 LWVVMEYLAGGSLTDVVTE-----------TCMDEGQIAavcRECLQALDFLHSNQVIHRDIKSDNILLGMDGS---VKL 403
Cdd:cd05036    84 RFILLELMAGGDLKSFLREnrprpeqpsslTMLDLLQLA---QDVAKGCRYLEENHFIHRDIAARNCLLTCKGPgrvAKI 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 404 TDFGFCAQITPEQSKRS---TMVGTPyWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05036   161 GDFGMARDIYRADYYRKggkAMLPVK-WMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPY 222
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
274-488 4.14e-15

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: 75.77  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTV-YTALdiATGQEVAIKQMNLQQQPKKELIIN---------------------EILVMRENKNPNIVnylds 331
Cdd:cd14067     1 LGQGGSGTViYRAR--YQGQPVAVKRFHIKKCKKRTDGSAdtmlkhlraadamknfsefrqEASMLHSLQHPCIV----- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 332 YLVG---DELWVVMEYLAGGSLTDVVTETCMDEGQIA-------AVCRECLQALDFLHSNQVIHRDIKSDNILL-GMDG- 399
Cdd:cd14067    74 YLIGisiHPLCFALELAPLGSLNTVLEENHKGSSFMPlghmltfKIAYQIAAGLAYLHKKNIIFCDLKSDNILVwSLDVq 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 400 ---SVKLTDFGFCAQITPEQSkrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT 476
Cdd:cd14067   154 ehiNIKLSDYGISRQSFHEGA--LGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSK 231
                         250
                  ....*....|..
gi 1024249297 477 NGTPELQNPERL 488
Cdd:cd14067   232 GIRPVLGQPEEV 243
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
264-462 5.50e-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: 75.82  E-value: 5.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIATGQE-------VAIKQMNlQQQPKKEL--IINEILVMRE-NKNPNIVNYLDSYL 333
Cdd:cd05098    11 PRDRLVLGKPLGEGCFGQVVLAEAIGLDKDkpnrvtkVAVKMLK-SDATEKDLsdLISEMEMMKMiGKHKNIINLLGACT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 334 VGDELWVVMEYLAGGSL-----------------TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG 396
Cdd:cd05098    90 QDGPLYVIVEYASKGNLreylqarrppgmeycynPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024249297 397 MDGSVKLTDFGFCAQITP-EQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05098   170 EDNVMKIADFGLARDIHHiDYYKKTTNGRLPVkWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPY 238
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
272-467 5.72e-15

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 75.49  E-value: 5.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTA-LDIATG---QEVAIKQMNLQQQP--KKEliiNEILVMRENKNPNIVNYLDSYLVGDEL----WVV 341
Cdd:cd14055     1 KLVGKGRFAEVWKAkLKQNASgqyETVAVKIFPYEEYAswKNE---KDIFTDASLKHENILQFLTAEERGVGLdrqyWLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQ---------VIHRDIKSDNILLGMDGSVKLTDFGFC--- 409
Cdd:cd14055    78 TAYHENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCVLADFGLAlrl 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297 410 -AQITPEQSKRSTMVGTPYWMAPEVVTRKA------YGPKVDIWSLGIMAIEMV----------EGEPPY---LNENP 467
Cdd:cd14055   158 dPSLSVDELANSGQVGTARYMAPEALESRVnledleSFKQIDVYSMALVLWEMAsrceasgevkPYELPFgskVRERP 235
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
274-510 6.71e-15

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: 74.96  E-value: 6.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALdiATGQEVAIKQMN---------------LQQQPKKELIIN------EILVMRENKNPNIVnyldsY 332
Cdd:cd14000     2 LGDGGFGSVYRAS--YKGEPVAVKIFNkhtssnfanvpadtmLRHLRATDAMKNfrllrqELTVLSHLHHPSIV-----Y 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 333 LVG---DELWVVMEYLAGGSLTDVVTEtcmDEGQIAAVCRECLQ--------ALDFLHSNQVIHRDIKSDNILL-GMDGS 400
Cdd:cd14000    75 LLGigiHPLMLVLELAPLGSLDHLLQQ---DSRSFASLGRTLQQrialqvadGLRYLHSAMIIYRDLKSHNVLVwTLYPN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 401 ----VKLTDFGFCAQITPEQSKrsTMVGTPYWMAPEVVTRKA-YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA 475
Cdd:cd14000   152 saiiIKIADYGISRQCCRMGAK--GSEGTPGFRAPEIARGNViYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIH 229
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1024249297 476 TNGTPELQNPErlSAVFR---DFLNRCLEMDVDRRGSA 510
Cdd:cd14000   230 GGLRPPLKQYE--CAPWPeveVLMKKCWKENPQQRPTA 265
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
269-515 7.26e-15

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: 74.51  E-value: 7.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 269 TRFEKIGQGASGTVYTALDIATGQeVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGG 348
Cdd:cd05114     7 TFMKELGSGLFGVVRLGKWRAQYK-VAIKAIR-EGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTEtcmDEGQIA-----AVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMV 423
Cdd:cd05114    85 CLLNYLRQ---RRGKLSrdmllSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 GTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEM-VEGEPPYLNENPLRALYLIaTNGTpELQNPERLSAVFRDFLNRCLE 501
Cdd:cd05114   162 KFPVkWSPPEVFNYSKFSSKSDVWSFGVLMWEVfTEGKMPFESKSNYEVVEMV-SRGH-RLYRPKLASKSVYEVMYSCWH 239
                         250
                  ....*....|....
gi 1024249297 502 MDVDRRGSAKELLQ 515
Cdd:cd05114   240 EKPEGRPTFADLLR 253
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
268-467 7.80e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 76.07  E-value: 7.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 268 YTRFEKIGQGASGTVYTALDIATGQEVAIKqmnLQQQPKKeLIinEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAg 347
Cdd:PHA03209   68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLK---IGQKGTT-LI--EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYS- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 gslTDVVTETCMDEGQIA---AVC--RECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGfCAQITPEQSKRSTM 422
Cdd:PHA03209  141 ---SDLYTYLTKRSRPLPidqALIieKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLG-AAQFPVVAPAFLGL 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 423 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVeGEPPYLNENP 467
Cdd:PHA03209  217 AGTVETNAPEVLARDKYNSKADIWSAGIVLFEML-AYPSTIFEDP 260
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
272-462 7.95e-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: 74.27  E-value: 7.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTAlDIATGQEVAIK--QMNLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd05085     2 ELLGKGNFGEVYKG-TLKDKTPVAVKtcKEDLPQELKIKFL-SEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVVTETcMDEGQIAAVCRECLQA---LDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTP 426
Cdd:cd05085    80 FLSFLRKK-KDELKTKQLVKFSLDAaagMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLKQIP 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1024249297 427 Y-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05085   159 IkWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPY 196
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
264-462 8.31e-15

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: 74.54  E-value: 8.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALdIATGQEVAIKQMNlQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVME 343
Cdd:cd05067     5 PRETLKLVERLGAGQFGEVWMGY-YNGHTKVAIKSLK-QGSMSPDAFLAEANLMKQLQHQRLVR-LYAVVTQEPIYIITE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTEtcmDEG------QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQS 417
Cdd:cd05067    82 YMENGSLVDFLKT---PSGikltinKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLI--EDN 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1024249297 418 KRSTMVGTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05067   157 EYTAREGAKFpikWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPY 205
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
264-462 8.82e-15

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: 74.37  E-value: 8.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIATgQEVAIKQMNLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVME 343
Cdd:cd05068     6 DRKSLKLLRKLGSGQFGEVWEGLWNNT-TPVAVKTLKPGTMDPEDFL-REAQIMKKLRHPKLIQLYAVCTLEEPIYIITE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVT--------ETCMD-EGQIAAvcreclqALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITP 414
Cdd:cd05068    84 LMKHGSLLEYLQgkgrslqlPQLIDmAAQVAS-------GMAYLESQNYIHRDLAARNVLVGENNICKVADFGL-ARVIK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 415 EQSKRSTMVGTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05068   156 VEDEYEAREGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPY 207
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
264-519 9.01e-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: 74.49  E-value: 9.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIA--TGQEVAIKQMNLQQQpkKELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd14112     1 PTGRFSFGSEIFRGRFSVIVKAVDSTteTDAHCAVKIFEVSDE--ASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGS--VKLTDFGFCAQITPEQSKR 419
Cdd:cd14112    79 MEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSwqVKLVDFGRAQKVSKLGKVP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 420 STmvGTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRalYLIATNGTPELQNPERL----SAVFRD 494
Cdd:cd14112   159 VD--GDTDWASPEFHnPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDE--EETKENVIFVKCRPNLIfveaTQEALR 234
                         250       260
                  ....*....|....*....|....*
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14112   235 FATWALKKSPTRRMRTDEALEHRWL 259
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
272-514 9.96e-15

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: 74.62  E-value: 9.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTAldiATGQEVAIK--QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd14152     6 ELIGQGRWGKVHRG---RWHGEVAIRllEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKGRT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVV--TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGmDGSVKLTDFG-FCAQITPEQSKRSTMVGTP 426
Cdd:cd14152    83 LYSFVrdPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGlFGISGVVQEGRRENELKLP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 427 ----YWMAPEVVTRKAYGPK---------VDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT-NGTPELQNPERLSAVF 492
Cdd:cd14152   162 hdwlCYLAPEIVREMTPGKDedclpfskaADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSgEGMKQVLTTISLGKEV 241
                         250       260
                  ....*....|....*....|..
gi 1024249297 493 RDFLNRCLEMDVDRRGSAKELL 514
Cdd:cd14152   242 TEILSACWAFDLEERPSFTLLM 263
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
265-456 1.01e-14

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: 74.58  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 265 KKKYTRFEKIGQGASGTV----YTALDIATGQEVAIKqmNLQQQPKKELIIN---EILVMRENKNPNIVNY--LDSYLVG 335
Cdd:cd05079     3 KRFLKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVK--SLKPESGGNHIADlkkEIEILRNLYHENIVKYkgICTEDGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 DELWVVMEYLAGGSLTDVV--TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 413
Cdd:cd05079    81 NGIKLIMEFLPSGSLKEYLprNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1024249297 414 PEQSKRSTM--VGTP-YWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 456
Cdd:cd05079   161 TDKEYYTVKddLDSPvFWYAPECLIQSKFYIASDVWSFGVTLYELL 206
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
274-473 1.16e-14

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: 74.86  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATgqEVAIKQM----NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd14159     1 IGEGGFGCVYQAVMRNT--EYAVKRLkedsELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTD----VVTETCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLTDFG---FCAQI-TPEQS-- 417
Cdd:cd14159    79 LEDrlhcQVSCPCLSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGlarFSRRPkQPGMSst 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1024249297 418 --KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYL 473
Cdd:cd14159   159 laRTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPTKYL 216
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
264-462 1.20e-14

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: 75.05  E-value: 1.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIATGQE-------VAIKQMNlQQQPKKEL--IINEILVMRE-NKNPNIVNYLDSYL 333
Cdd:cd05101    22 PRDKLTLGKPLGEGCFGQVVMAEAVGIDKDkpkeavtVAVKMLK-DDATEKDLsdLVSEMEMMKMiGKHKNIINLLGACT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 334 VGDELWVVMEYLAGGSLTDV-----------------VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG 396
Cdd:cd05101   101 QDGPLYVIVEYASKGNLREYlrarrppgmeysydinrVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVT 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024249297 397 MDGSVKLTDFGFCAQITP-EQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05101   181 ENNVMKIADFGLARDINNiDYYKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPY 249
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
266-520 1.42e-14

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 75.05  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 266 KKYTRFEKIGQGASGTVYTALDIATGQEVAIK----QMNLQQQPKKELIINEILVMR--ENKNpNIVNYLDSYLVGDELW 339
Cdd:cd14226    13 DRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKiiknKKAFLNQAQIEVRLLELMNKHdtENKY-YIVRLKRHFMFRNHLC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 340 VVMEYLAGgSLTDVVTETCMDEGQIAAVCR---ECLQALDFLHSN--QVIHRDIKSDNILL--GMDGSVKLTDFGFCAQI 412
Cdd:cd14226    92 LVFELLSY-NLYDLLRNTNFRGVSLNLTRKfaqQLCTALLFLSTPelSIIHCDLKPENILLcnPKRSAIKIIDFGSSCQL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPE-----QSKrstmvgtpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEP---------------------P----- 461
Cdd:cd14226   171 GQRiyqyiQSR--------FYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPlfsganevdqmnkivevlgmpPvhmld 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 462 -------YLNENPLRALYLIATNGTPELQNP--ERLSAV-------------------------FRDFLNRCLEMDVDRR 507
Cdd:cd14226   243 qapkarkFFEKLPDGTYYLKKTKDGKKYKPPgsRKLHEIlgvetggpggrragepghtvedylkFKDLILRMLDYDPKTR 322
                         330
                  ....*....|...
gi 1024249297 508 GSAKELLQHPFLK 520
Cdd:cd14226   323 ITPAEALQHSFFK 335
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
263-462 1.48e-14

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: 75.06  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 263 DPKKKYTRF-----EKIGQGASGTVYTALDIATGQE-------VAIKQMNlQQQPKKEL--IINEILVMRE-NKNPNIVN 327
Cdd:cd05100     4 DPKWELSRTrltlgKPLGEGCFGQVVMAEAIGIDKDkpnkpvtVAVKMLK-DDATDKDLsdLVSEMEMMKMiGKHKNIIN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 328 YLDSYLVGDELWVVMEYLAGGSL-----------TDVVTETC-MDEGQIA-----AVCRECLQALDFLHSNQVIHRDIKS 390
Cdd:cd05100    83 LLGACTQDGPLYVLVEYASKGNLreylrarrppgMDYSFDTCkLPEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAA 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024249297 391 DNILLGMDGSVKLTDFGFCAQI-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05100   163 RNVLVTEDNVMKIADFGLARDVhNIDYYKKTTNGRLPVkWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 237
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
308-512 1.53e-14

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: 73.69  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 308 ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRD 387
Cdd:cd14027    36 EALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 388 IKSDNILLGMDGSVKLTDFGFC-----AQITPEQSKRSTMV--------GTPYWMAPEVVTRKAYGP--KVDIWSLGIMA 452
Cdd:cd14027   116 LKPENILVDNDFHIKIADLGLAsfkmwSKLTKEEHNEQREVdgtakknaGTLYYMAPEHLNDVNAKPteKSDVYSFAIVL 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 453 IEMVEGEPPYLNENPLRALYLIATNGT-PELQN-PERLSAVFRDFLNRCLEMDVDRRGSAKE 512
Cdd:cd14027   196 WAIFANKEPYENAINEDQIIMCIKSGNrPDVDDiTEYCPREIIDLMKLCWEANPEARPTFPG 257
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
264-462 2.55e-14

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: 73.85  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALDIATGQE-------VAIKQMNlQQQPKKEL--IINEILVMR-ENKNPNIVNYLDSYL 333
Cdd:cd05099    10 PRDRLVLGKPLGEGCFGQVVRAEAYGIDKSrpdqtvtVAVKMLK-DNATDKDLadLISEMELMKlIGKHKNIINLLGVCT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 334 VGDELWVVMEYLAGGSLTDVVTE------------TCMDEGQIA-----AVCRECLQALDFLHSNQVIHRDIKSDNILLG 396
Cdd:cd05099    89 QEGPLYVIVEYAAKGNLREFLRArrppgpdytfdiTKVPEEQLSfkdlvSCAYQVARGMEYLESRRCIHRDLAARNVLVT 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024249297 397 MDGSVKLTDFGFCAQITP-EQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05099   169 EDNVMKIADFGLARGVHDiDYYKKTSNGRLPVkWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPY 237
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
273-462 2.58e-14

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: 73.22  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD 352
Cdd:cd05052    13 KLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFL-KEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTETcmDEGQIAAV-----CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 427
Cdd:cd05052    92 YLREC--NREELNAVvllymATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPI 169
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1024249297 428 -WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05052   170 kWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPY 206
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
267-519 3.04e-14

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: 73.56  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIIN-------EILVMRENKNPNIVNYLDSY-LVGDEL 338
Cdd:cd14041     7 RYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDSF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 WVVMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILL---GMDGSVKLTDFGFcAQI 412
Cdd:cd14041    87 CTVLEYCEGNDLDFYLKQhKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGL-SKI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQSK--------RSTMVGTPYWMAPEVVTRKAYGPK----VDIWSLGIMAIEMVEGEPPY---------LNENPLral 471
Cdd:cd14041   166 MDDDSYnsvdgmelTSQGAGTYWYLPPECFVVGKEPPKisnkVDVWSVGVIFYQCLYGRKPFghnqsqqdiLQENTI--- 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 472 yLIATngtpELQNPER--LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14041   243 -LKAT----EVQFPPKpvVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
273-513 3.20e-14

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: 73.46  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 351
Cdd:cd05045    12 EFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRdLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 352 DVVTET-------------------------CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 406
Cdd:cd05045    92 SFLRESrkvgpsylgsdgnrnssyldnpderALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRKMKISDF 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 407 GFCAQITPEQS--KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNgtPELQ 483
Cdd:cd05045   172 GLSRDVYEEDSyvKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPERLFNLLKTG--YRME 249
                         250       260       270
                  ....*....|....*....|....*....|
gi 1024249297 484 NPERLSAVFRDFLNRCLEMDVDRRGSAKEL 513
Cdd:cd05045   250 RPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
264-514 4.65e-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: 72.76  E-value: 4.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTAldIATG-------QEVAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVG 335
Cdd:cd05062     4 AREKITMSRELGQGSFGMVYEG--IAKGvvkdepeTRVAIKTVNEAASMRERIeFLNEASVMKEFNCHHVVRLLGVVSQG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 336 DELWVVMEYLAGGSLTDVV----TETCMDEGQIAAVCRECLQ-------ALDFLHSNQVIHRDIKSDNILLGMDGSVKLT 404
Cdd:cd05062    82 QPTLVIMELMTRGDLKSYLrslrPEMENNPVQAPPSLKKMIQmageiadGMAYLNANKFVHRDLAARNCMVAEDFTVKIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 405 DFGFCAQITPEQSKRSTMVG--TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGTpe 481
Cdd:cd05062   162 DFGMTRDIYETDYYRKGGKGllPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATlAEQPYQGMSNEQVLRFVMEGGL-- 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1024249297 482 LQNPERLSAVFRDFLNRCLEMDVDRRGSAKELL 514
Cdd:cd05062   240 LDKPDNCPDMLFELMRMCWQYNPKMRPSFLEII 272
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
70-105 5.91e-14

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 65.69  E-value: 5.91e-14
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1024249297   70 ISLPSDFEHTIHVGFDAVTGEFTGIPEQWARLLQTS 105
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTGGFTGLPTEWKSLLKTS 36
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
273-468 1.07e-13

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 71.74  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALdiATGQEVAIKQMNLQQQPK--KELIINEILVMRENknpNIVNYLDSYLVGD----ELWVVMEYLA 346
Cdd:cd14144     2 SVGKGRYGEVWKGK--WRGEKVAVKIFFTTEEASwfRETEIYQTVLMRHE---NILGFIAADIKGTgswtQLYLITDYHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSN--------QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 418
Cdd:cd14144    77 NGSLYDFLRGNTLDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAVKFISETNE 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 419 ----RSTMVGTPYWMAPEVVT----RKAYGP--KVDIWSLGIMAIEMV----------EGEPPYLNENPL 468
Cdd:cd14144   157 vdlpPNTRVGTKRYMAPEVLDeslnRNHFDAykMADMYSFGLVLWEIArrcisggiveEYQLPYYDAVPS 226
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
363-466 1.18e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 73.19  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 363 QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGfcaQITPEQSKRSTM----VGTPYWMAPEVVTRKA 438
Cdd:PHA03210  268 QTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFG---TAMPFEKEREAFdygwVGTVATNSPEILAGDG 344
                          90       100
                  ....*....|....*....|....*...
gi 1024249297 439 YGPKVDIWSLGIMAIEMVEGEPPYLNEN 466
Cdd:PHA03210  345 YCEITDIWSCGLILLDMLSHDFCPIGDG 372
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
273-507 1.33e-13

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: 71.26  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATgQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAGGSLTD 352
Cdd:cd05069    19 KLGQGCFGEVWMGTWNGT-TKVAIKTLKPGTM-MPEAFLQEAQIMKKLRHDKLVP-LYAVVSEEPIYIVTEFMGKGSLLD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQSKRSTMVGTPY-- 427
Cdd:cd05069    96 FLKEgdgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI--EDNEYTARQGAKFpi 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 428 -WMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPY---LNENPL----RALYLIATNGTPElqnperlsaVFRDFLNR 498
Cdd:cd05069   174 kWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPYpgmVNREVLeqveRGYRMPCPQGCPE---------SLHELMKL 244

                  ....*....
gi 1024249297 499 CLEMDVDRR 507
Cdd:cd05069   245 CWKKDPDER 253
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
359-454 1.50e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 73.00  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 359 MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpeQSKRST-----MVGTPYWMAPEV 433
Cdd:PHA03211  257 LGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFA---RGSWSTpfhygIAGTVDTNAPEV 333
                          90       100
                  ....*....|....*....|.
gi 1024249297 434 VTRKAYGPKVDIWSLGIMAIE 454
Cdd:PHA03211  334 LAGDPYTPSVDIWSAGLVIFE 354
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
273-507 1.72e-13

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: 70.76  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTV----YTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLdSYLVGDELWVVMEYLAGG 348
Cdd:cd05116     2 ELGSGNFGTVkkgyYQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMI-GICEAESWMLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVTET-CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS--KRSTMVGT 425
Cdd:cd05116    81 PLNKFLQKNrHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENyyKAQTHGKW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 426 PY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIaTNGTpELQNPERLSAVFRDFLNRCLEMD 503
Cdd:cd05116   161 PVkWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMI-EKGE-RMECPAGCPPEMYDLMKLCWTYD 238

                  ....
gi 1024249297 504 VDRR 507
Cdd:cd05116   239 VDER 242
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
259-519 1.88e-13

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. 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. 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: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 71.60  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 259 VSVGDP-KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQpKKELIINEILVMR--ENKNPN------IVNYL 329
Cdd:cd14216     2 VKIGDLfNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEH-YTETALDEIKLLKsvRNSDPNdpnremVVQLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 330 DSYLV----GDELWVVMEYLAGGSLTDVVTET-------CmdegqIAAVCRECLQALDFLHSN-QVIHRDIKSDNILLGM 397
Cdd:cd14216    81 DDFKIsgvnGTHICMVFEVLGHHLLKWIIKSNyqglplpC-----VKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 398 DG------------------------------SVKLTDFGFCAQItpeQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWS 447
Cdd:cd14216   156 NEqyirrlaaeatewqrnflvnplepknaeklKVKIADLGNACWV---HKHFTEDIQTRQYRSLEVLIGSGYNTPADIWS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 448 LGIMAIEMVEGE---PPYLNENPLR-----ALYLIATNGTP-------------------------------------EL 482
Cdd:cd14216   233 TACMAFELATGDylfEPHSGEDYSRdedhiALIIELLGKVPrklivagkyskefftkkgdlkhitklkpwglfevlveKY 312
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1024249297 483 QNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14216   313 EWSQEEAAGFTDFLLPMLELIPEKRATAAECLRHPWL 349
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
273-462 2.68e-13

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: 69.95  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATgQEVAIKQMnlqqQP---KKELIINEILVMRENKNPNIVNYldsYLVGDE--LWVVMEYLAG 347
Cdd:cd14203     2 KLGQGCFGEVWMGTWNGT-TKVAIKTL----KPgtmSPEAFLEEAQIMKKLRHDKLVQL---YAVVSEepIYIVTEFMSK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 348 GSLTDVVTEtcmDEG------QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQSKRST 421
Cdd:cd14203    74 GSLLDFLKD---GEGkylklpQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI--EDNEYTA 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 422 MVGTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPY 462
Cdd:cd14203   149 RQGAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPY 193
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
373-516 3.54e-13

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: 70.78  E-value: 3.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 373 QALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI--TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGI 450
Cdd:cd05103   190 KGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIykDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGV 269
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024249297 451 MAIEMVE-GEPPY----LNENPLRALYLIATNGTPELQNPErlsaVFRDFLNrCLEMDVDRRGSAKELLQH 516
Cdd:cd05103   270 LLWEIFSlGASPYpgvkIDEEFCRRLKEGTRMRAPDYTTPE----MYQTMLD-CWHGEPSQRPTFSELVEH 335
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
264-516 3.77e-13

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk 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: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 70.25  E-value: 3.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVY--TALDIATGQE---VAIKQM--NLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGD 336
Cdd:cd05050     3 PRNNIEYVRDIGQGAFGRVFqaRAPGLLPYEPftmVAVKMLkeEASADMQADFQ-REAALMAEFDHPNIVKLLGVCAVGK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTDVVTETC----MDEGQIAAVCRECLQ-------------------ALDFLHSNQVIHRDIKSDNI 393
Cdd:cd05050    82 PMCLLFEYMAYGDLNEFLRHRSpraqCSLSHSTSSARKCGLnplplscteqlciakqvaaGMAYLSERKFVHRDLATRNC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 394 LLGMDGSVKLTDFGFCAQI-TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRA 470
Cdd:cd05050   162 LVGENMVVKIADFGLSRNIySADYYKASENDAIPIrWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYYGMAHEEV 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1024249297 471 LYLIATNGTpeLQNPERLSAVFRDFLNRCLEMDVDRRGSAKEL---LQH 516
Cdd:cd05050   242 IYYVRDGNV--LSCPDNCPLELYNLMRLCWSKLPSDRPSFASInriLQR 288
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
274-462 4.83e-13

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: 69.30  E-value: 4.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTALDIATG--QEVAIKQMN-LQQQPKKELIINEILVM-RENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd05047     3 IGEGNFGQVLKARIKKDGlrMDAAIKRMKeYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVV-----------------TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAqi 412
Cdd:cd05047    83 LLDFLrksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSR-- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 413 TPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05047   161 GQEVYVKKTMGRLPVrWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 212
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
217-455 4.86e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 71.03  E-value: 4.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 217 NKEVTPPSAENANSSTLYRNTDRQrkkSKMTDEEilEKLRSIVSVGDP----KKKYTRFEKIGQGASGTVY--TALDIAT 290
Cdd:PHA03207   44 DCDELGDSDDVTHATDYDADEESL---SPQTDVC--QEPCETTSSSDPasvvRMQYNILSSLTPGSEGEVFvcTKHGDEQ 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 291 GQEVAIKQMNLQQQPKKEliineILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRE 370
Cdd:PHA03207  119 RKKVIVKAVTGGKTPGRE-----IDILKTISHRAIINLIHAYRWKSTVCMVMPKYKCDLFTYVDRSGPLPLEQAITIQRR 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 371 CLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT--PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSL 448
Cdd:PHA03207  194 LLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDahPDTPQCYGWSGTLETNSPELLALDPYCAKTDIWSA 273

                  ....*..
gi 1024249297 449 GIMAIEM 455
Cdd:PHA03207  274 GLVLFEM 280
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
270-523 6.52e-13

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: 69.21  E-value: 6.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RFEKIGQGASGTVYTALDIATGQE----VAIKQM-NLQQQPKKELIINEILVMRENKNPNIVNYLdSYLVGDELWVVMEY 344
Cdd:cd05111    11 KLKVLGSGVFGTVHKGIWIPEGDSikipVAIKVIqDRSGRQSFQAVTDHMLAIGSLDHAYIVRLL-GICPGASLQLVTQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTET--CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR-ST 421
Cdd:cd05111    90 LPLGSLLDHVRQHrgSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYPDDKKYfYS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 422 MVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNgtPELQNPERLSAVFRDFLNRC 499
Cdd:cd05111   170 EAKTPIkWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPYAGMRLAEVPDLLEKG--ERLAQPQICTIDVYMVMVKC 247
                         250       260
                  ....*....|....*....|....
gi 1024249297 500 LEMDVDRRGSAKELLQHpFLKLAK 523
Cdd:cd05111   248 WMIDENIRPTFKELANE-FTRMAR 270
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
373-515 6.62e-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. 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: 70.03  E-value: 6.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 373 QALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI--TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGI 450
Cdd:cd14207   191 RGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIykNPDYVRKGDARLPLKWMAPESIFDKIYSTKSDVWSYGV 270
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 451 MAIEMVE-GEPPY----LNENPLRALYLIATNGTPELQNPErlsaVFRDFLNrCLEMDVDRRGSAKELLQ 515
Cdd:cd14207   271 LLWEIFSlGASPYpgvqIDEDFCSKLKEGIRMRAPEFATSE----IYQIMLD-CWQGDPNERPRFSELVE 335
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
273-462 7.41e-13

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: 68.95  E-value: 7.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTALDIATGQeVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAGGSLTD 352
Cdd:cd05071    16 KLGQGCFGEVWMGTWNGTTR-VAIKTLKPGTM-SPEAFLQEAQVMKKLRHEKLVQ-LYAVVSEEPIYIVTEYMSKGSLLD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VV---TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQSKRSTMVGTPY-- 427
Cdd:cd05071    93 FLkgeMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLI--EDNEYTARQGAKFpi 170
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1024249297 428 -WMAPEVVTRKAYGPKVDIWSLGIMAIEM-VEGEPPY 462
Cdd:cd05071   171 kWTAPEAALYGRFTIKSDVWSFGILLTELtTKGRVPY 207
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
274-513 9.00e-13

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: 68.72  E-value: 9.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 274 IGQGASGTVYTA---LDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDEL------WVVM 342
Cdd:cd05035     7 LGEGEFGSVMEAqlkQDDGSQLKVAVKTMKVDIHTYSEIeeFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppspMVIL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTETCMDEGQIAAVCRECLQ-------ALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 415
Cdd:cd05035    87 PFMKHGDLHSYLLYSRLGGLPEKLPLQTLLKfmvdiakGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIYSG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 416 QSKRSTMVGT-PY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLN-ENPLRALYLIatNGTPELQNPERLSAV 491
Cdd:cd05035   167 DYYRQGRISKmPVkWIALESLADNVYTSKSDVWSFGVTMWEiATRGQTPYPGvENHEIYDYLR--NGNRLKQPEDCLDEV 244
                         250       260
                  ....*....|....*....|..
gi 1024249297 492 FrDFLNRCLEMDVDRRGSAKEL 513
Cdd:cd05035   245 Y-FLMYFCWTVDPKDRPTFTKL 265
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
272-489 9.47e-13

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: 68.52  E-value: 9.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTV----YTALDIATGQeVAIK---QMNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEY 344
Cdd:cd05040     1 EKLGDGSFGVVrrgeWTTPSGKVIQ-VAVKclkSDVLSQPNAMDDFLKEVNAMHSLDHPNLIR-LYGVVLSSPLMMVTEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETCmDEGQIAAVCRECLQ---ALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRST 421
Cdd:cd05040    79 APLGSLLDRLRKDQ-GHFLISTLCDYAVQianGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGL-MRALPQNEDHYV 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 422 M---VGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGtpelqnpERLS 489
Cdd:cd05040   157 MqehRKVPFaWCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKIDKEG-------ERLE 222
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
270-462 1.03e-12

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: 68.88  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RF-EKIGQGASGTVYTA------LDIAtgQEVAIKQMNLQQQPKK-ELIINEILVMRENKNPNIVNYLDSYLVGDELWVV 341
Cdd:cd05090     8 RFmEELGECAFGKIYKGhlylpgMDHA--QLVAIKTLKDYNNPQQwNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCML 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 342 MEYLAGGSL------------------TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKL 403
Cdd:cd05090    86 FEFMNQGDLheflimrsphsdvgcssdEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKI 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 404 TDFGFCAQITPEQSKR--STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05090   166 SDLGLSREIYSSDYYRvqNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPY 227
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
337-456 1.09e-12

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 68.90  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 337 ELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSN-----------QVIHRDIKSDNILLGMDGSVKLTD 405
Cdd:cd14140    67 ELWLITAFHDKGSLTDYLKGNIVSWNELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLTAVLAD 146
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1024249297 406 FGFCAQITPEQSKRST--MVGTPYWMAPEVV------TRKAYgPKVDIWSLGIMAIEMV 456
Cdd:cd14140   147 FGLAVRFEPGKPPGDThgQVGTRRYMAPEVLegainfQRDSF-LRIDMYAMGLVLWELV 204
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
373-515 1.13e-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: 69.24  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 373 QALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI--TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGI 450
Cdd:cd05102   183 RGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIykDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGV 262
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 451 MAIEMVE-GEPPY----LNENPLRALyliaTNGTpELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd05102   263 LLWEIFSlGASPYpgvqINEEFCQRL----KDGT-RMRAPEYATPEIYRIMLSCWHGDPKERPTFSDLVE 327
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
264-495 1.14e-12

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 68.53  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTALdIATGQEVAIKQMnlqqQPKK---ELIINEILVMRENKNPNIVNYLDSYLVGDELWV 340
Cdd:cd05072     5 PRESIKLVKKLGAGQFGEVWMGY-YNNSTKVAVKTL----KPGTmsvQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLAGGSLTDVVTEtcmDEG------QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItp 414
Cdd:cd05072    80 ITEYMAKGSLLDFLKS---DEGgkvllpKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVI-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 415 EQSKRSTMVGTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYlnenplralyliatngtPELQNPERLSA 490
Cdd:cd05072   155 EDNEYTAREGAKFpikWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPY-----------------PGMSNSDVMSA 217

                  ....*
gi 1024249297 491 VFRDF 495
Cdd:cd05072   218 LQRGY 222
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
270-462 1.40e-12

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: 68.49  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RFEK-IGQGASGTVYTALDIATGQEV--AIKQMN-LQQQPKKELIINEILVM-RENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05089     5 KFEDvIGEGNFGQVIKAMIKKDGLKMnaAIKMLKeFASENDHRDFAGELEVLcKLGHHPNIINLLGACENRGYLYIAIEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVV-----------------TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 407
Cdd:cd05089    85 APYGNLLDFLrksrvletdpafakehgTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFG 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024249297 408 FCAqiTPEQSKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05089   165 LSR--GEEVYVKKTMGRLPVrWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPY 219
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
273-513 1.49e-12

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: 68.07  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTA--LDIATGQE---VAIKQM-----NLQQQPKKELiinEILVMRENKNpnIVNYLDSYLVGDELWVVM 342
Cdd:cd05092    12 ELGEGAFGKVFLAecHNLLPEQDkmlVAVKALkeateSARQDFQREA---ELLTVLQHQH--IVRFYGVCTEGEPLIMVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 343 EYLAGGSLTDVVTE-----TCMDEG-----------QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDF 406
Cdd:cd05092    87 EYMRHGDLNRFLRShgpdaKILDGGegqapgqltlgQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 407 GFCAQITPEQSKR---STMVGTpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIaTNGTpEL 482
Cdd:cd05092   167 GMSRDIYSTDYYRvggRTMLPI-RWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECI-TQGR-EL 243
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1024249297 483 QNPERLSAVFRDFLNRCLEMDVDRRGSAKEL 513
Cdd:cd05092   244 ERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
272-467 2.74e-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: 67.11  E-value: 2.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVY--TALDiATGQEV--AIKQMN-LQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDEL-WVVMEYL 345
Cdd:cd05058     1 EVIGKGHFGCVYhgTLID-SDGQKIhcAVKSLNrITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSpLVVLPYM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTE-----TCMD-EGQIAAVCReclqALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ--- 416
Cdd:cd05058    80 KHGDLRNFIRSethnpTVKDlIGFGLQVAK----GMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEyys 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 417 SKRSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLNENP 467
Cdd:cd05058   156 VHNHTGAKLPVkWMALESLQTQKFTTKSDVWSFGVLLWElMTRGAPPYPDVDS 208
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
270-516 2.87e-12

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: 67.52  E-value: 2.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 270 RFEK-IGQGASGTVY--TALDI---ATGQEVAIKQMNLQQQP--KKELIINEILVMRENKNPNIVNYLDS-YLVGDELWV 340
Cdd:cd05054    10 KLGKpLGRGAFGKVIqaSAFGIdksATCRTVAVKMLKEGATAseHKALMTELKILIHIGHHLNVVNLLGAcTKPGGPLMV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 341 VMEYLAGGSLTDV--------------------VTETCMDEGQIAAVCRECL-------QALDFLHSNQVIHRDIKSDNI 393
Cdd:cd05054    90 IVEFCKFGNLSNYlrskreefvpyrdkgardveEEEDDDELYKEPLTLEDLIcysfqvaRGMEFLASRKCIHRDLAARNI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 394 LLGMDGSVKLTDFGFCAQITPEQSK-RSTMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY----LNEN 466
Cdd:cd05054   170 LLSENNVVKICDFGLARDIYKDPDYvRKGDARLPLkWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYpgvqMDEE 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 467 PLRALYLIATNGTPELQNPErlsaVFRDFLNrCLEMDVDRRGSAKELLQH 516
Cdd:cd05054   250 FCRRLKEGTRMRAPEYTTPE----IYQIMLD-CWHGEPKERPTFSELVEK 294
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
272-515 3.67e-12

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: 66.96  E-value: 3.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTAldiATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 349
Cdd:cd14153     6 ELIGKGRFGQVYHG---RWHGEVAIRLIDIERDNEEQLkaFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 350 LTDVV--TETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGmDGSVKLTDFGFCA-----QITPEQSKRSTM 422
Cdd:cd14153    83 LYSVVrdAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLFTisgvlQAGRREDKLRIQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 423 VGTPYWMAPEVVTRKA---------YGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPErLSAVFR 493
Cdd:cd14153   162 SGWLCHLAPEIIRQLSpeteedklpFSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGMKPNLSQIG-MGKEIS 240
                         250       260
                  ....*....|....*....|..
gi 1024249297 494 DFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd14153   241 DILLFCWAYEQEERPTFSKLME 262
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
267-462 6.48e-12

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; 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. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 65.84  E-value: 6.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 267 KYTRFEKIGQGASGTVYTALDIATGQEVAIKqMNLQQQPKKELIInEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 346
Cdd:cd14129     1 RWKVLRKIGGGGFGEIYDALDLLTRENVALK-VESAQQPKQVLKM-EVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQLQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETCMDEGQIAAVC---RECLQALDFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGF-------CAQI 412
Cdd:cd14129    79 GRNLADLRRSQSRGTFTISTTLrlgRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLarqftnsCGDV 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 413 TPEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd14129   159 RPPRAV-AGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 207
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
264-515 6.64e-12

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: 66.09  E-value: 6.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTA---LDIATGQEVAIKQM--NLQQQPKKELIINEILVMRENKNPNIVNyldsyLVGDEL 338
Cdd:cd05074     7 QEQQFTLGRMLGKGEFGSVREAqlkSEDGSFQKVAVKMLkaDIFSSSDIEEFLREAACMKEFDHPNVIK-----LIGVSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 339 -----------WVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQ-------ALDFLHSNQVIHRDIKSDNILLGMDGS 400
Cdd:cd05074    82 rsrakgrlpipMVILPFMKHGDLHTFLLMSRIGEEPFTLPLQTLVRfmidiasGMEYLSSKNFIHRDLAARNCMLNENMT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 401 VKLTDFGFCAQITPEQSKRSTMVGT-PY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLN-ENPLRALYLIAT 476
Cdd:cd05074   162 VCVADFGLSKKIYSGDYYRQGCASKlPVkWLALESLADNVYTTHSDVWAFGVTMWEiMTRGQTPYAGvENSEIYNYLIKG 241
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1024249297 477 NGTPelQNPERLSAVFrDFLNRCLEMDVDRRGSAKELLQ 515
Cdd:cd05074   242 NRLK--QPPDCLEDVY-ELMCQCWSPEPKCRPSFQHLRD 277
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
259-519 7.55e-12

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. 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. 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: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 66.97  E-value: 7.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 259 VSVGDP-KKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQpKKELIINEILVMR--------ENKNPNIVNYL 329
Cdd:cd14218     2 VKIGDLfNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVH-YTETAVDEIKLLKcvrdsdpsDPKRETIVQLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 330 DSYLV----GDELWVVMEYLAGGSLTDVVTETCMDEGQ--IAAVCRECLQALDFLHSN-QVIHRDIKSDNILLGM-DGSV 401
Cdd:cd14218    81 DDFKIsgvnGVHVCMVLEVLGHQLLKWIIKSNYQGLPLpcVKSILRQVLQGLDYLHTKcKIIHTDIKPENILMCVdEGYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 402 KL------------------TDFGFCAQ---ITPEQSKRSTMV-------GTPYWM--------------APEVVTRKAY 439
Cdd:cd14218   161 RRlaaeatiwqqagapppsgSSVSFGASdflVNPLEPQNADKIrvkiadlGNACWVhkhftediqtrqyrALEVLIGAEY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 440 GPKVDIWSLGIMAIEMVEGE----------------------------PP-----------YLN-ENPLRALYLIATNGT 479
Cdd:cd14218   241 GTPADIWSTACMAFELATGDylfephsgedytrdedhiahivellgdiPPhfalsgrysreYFNrRGELRHIKNLKHWGL 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1024249297 480 PEL-----QNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14218   321 YEVlvekyEWPLEQAAQFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
264-466 8.26e-12

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: 65.86  E-value: 8.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTAlDIATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVME 343
Cdd:cd05070     7 PRESLQLIKRLGNGQFGEVWMG-TWNGNTKVAIKTLKPGTM-SPESFLEEAQIMKKLKHDKLVQ-LYAVVSEEPIYIVTE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQSKRS 420
Cdd:cd05070    84 YMSKGSLLDFLKDgegRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLI--EDNEYT 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMV-EGEPPYLNEN 466
Cdd:cd05070   162 ARQGAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVtKGRVPYPGMN 211
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
269-507 8.54e-12

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: 65.77  E-value: 8.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 269 TRFEKIGQGASGTVYTALDIATGQE---VAIKQMNLQQQPKKEL-IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEY 344
Cdd:cd05063     8 TKQKVIGAGEFGEVFRGILKMPGRKevaVAIKTLKPGYTEKQRQdFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 345 LAGGSLTDVVTETCMDEG--QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT--PEQSKRS 420
Cdd:cd05063    88 MENGALDKYLRDHDGEFSsyQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEddPEGTYTT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 421 TMVGTPY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYL---NENPLRALyliatNGTPELQNPERLSAVFRDF 495
Cdd:cd05063   168 SGGKIPIrWTAPEAIAYRKFTSASDVWSFGIVMWEvMSFGERPYWdmsNHEVMKAI-----NDGFRLPAPMDCPSAVYQL 242
                         250
                  ....*....|..
gi 1024249297 496 LNRCLEMDVDRR 507
Cdd:cd05063   243 MLQCWQQDRARR 254
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
264-462 8.65e-12

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 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 (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 66.17  E-value: 8.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYT--------------ALDIATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIV 326
Cdd:cd05095     3 PRKLLTFKEKLGEGQFGEVHLceaegmekfmdkdfALEVSENQPVLVAVKMLRADANKNArndFLKEIKIMSRLKDPNII 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 327 NYLDSYLVGDELWVVMEYLAGGSLTDVV--------------------TETCMDEGQIAAvcreclqALDFLHSNQVIHR 386
Cdd:cd05095    83 RLLAVCITDDPLCMITEYMENGDLNQFLsrqqpegqlalpsnaltvsySDLRFMAAQIAS-------GMKYLSSLNFVHR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 387 DIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR--STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE--GEPPY 462
Cdd:cd05095   156 DLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTfcREQPY 235
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
373-514 1.15e-11

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 66.57  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 373 QALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQ---SKRSTMVGTPyWMAPEVVTRKAYGPKVDIWSLG 449
Cdd:cd05107   250 NGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSnyiSKGSTFLPLK-WMAPESIFNNLYTTLSDVWSFG 328
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024249297 450 IMAIEMVE-GEPPYlNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELL 514
Cdd:cd05107   329 ILLWEIFTlGGTPY-PELPMNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLV 393
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
264-462 1.20e-11

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: 65.05  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTAlDIATGQEVAIKQMNLQQQpKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVME 343
Cdd:cd05073     9 PRESLKLEKKLGAGQFGEVWMA-TYNKHTKVAVKTMKPGSM-SVEAFLAEANVMKTLQHDKLVK-LHAVVTKEPIYIITE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 344 YLAGGSLTDVVTEtcmDEG------QIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQS 417
Cdd:cd05073    86 FMAKGSLLDFLKS---DEGskqplpKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVI--EDN 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1024249297 418 KRSTMVGTPY---WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 462
Cdd:cd05073   161 EYTAREGAKFpikWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPY 209
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
273-462 1.24e-11

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: 65.85  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYTAL--DIATGQEVAIKQmnLQQQPKKELIINEILVMRENKNPNIVNYLDSYL--VGDELWVVMEYlAGG 348
Cdd:cd07868    24 KVGRGTYGHVYKAKrkDGKDDKDYALKQ--IEGTGISMSACREIALLRELKHPNVISLQKVFLshADRKVWLLFDY-AEH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 349 SLTDVVT----------ETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD----GSVKLTDFGFC----A 410
Cdd:cd07868   101 DLWHIIKfhraskankkPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFArlfnS 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1024249297 411 QITPeQSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPY 462
Cdd:cd07868   181 PLKP-LADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIF 232
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
281-519 1.44e-11

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 65.15  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 281 TVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMREN----KNPNIVNYLDSYLVGDE----LWVVMEYLAGGSLTD 352
Cdd:cd14034    24 SAYLAMDTEEGVEVVWNEVQFSERKNFKLQEEKVKAVFDNliqlEHLNIVKFHKYWADVKEnrarVIFITEYMSSGSLKQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 353 VVTET-----CMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILLGMDGSVKLtdfgfcAQITPEQSKRSTMV-- 423
Cdd:cd14034   104 FLKKTkknhkTMNEKAWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKI------GSVAPDTINNHVKTcr 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 424 ---GTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV------EGEPPYLNENPLralyliaTNGTPELQNPERlsavfRD 494
Cdd:cd14034   178 eeqKNLHFFAPEYGEVANVTTAVDIYSFGMCALEMAvleiqgNGESSYVPQEAI-------NSAIQLLEDPLQ-----RE 245
                         250       260
                  ....*....|....*....|....*
gi 1024249297 495 FLNRCLEMDVDRRGSAKELLQHPFL 519
Cdd:cd14034   246 FIQKCLEVDPSKRPTARELLFHQAL 270
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
272-455 1.61e-11

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 65.16  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 272 EKIGQGASGTVYTAldIATGQEVAIKQMNLQQQPK--KELIINEILVMRENknpNIVNYL--DSYLVG--DELWVVMEYL 345
Cdd:cd14143     1 ESIGKGRFGEVWRG--RWRGEDVAVKIFSSREERSwfREAEIYQTVMLRHE---NILGFIaaDNKDNGtwTQLWLVSDYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 346 AGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQV--------IHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQS 417
Cdd:cd14143    76 EHGSLFDYLNRYTVTVEGMIKLALSIASGLAHLHMEIVgtqgkpaiAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATD 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1024249297 418 K----RSTMVGTPYWMAPEVVTR-------KAYgPKVDIWSLGIMAIEM 455
Cdd:cd14143   156 TidiaPNHRVGTKRYMAPEVLDDtinmkhfESF-KRADIYALGLVFWEI 203
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
264-519 1.85e-11

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-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: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 65.00  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 264 PKKKYTRFEKIGQGASGTVYTA--------LDIATGQE------VAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNY 328
Cdd:cd05097     3 PRQQLRLKEKLGEGQFGEVHLCeaeglaefLGEGAPEFdgqpvlVAVKMLRADvTKTARNDFLKEIKIMSRLKNPNIIRL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 329 LDSYLVGDELWVVMEYLAGGSLTDVVTE-----TCMDEGQIAAVCRECL--------QALDFLHSNQVIHRDIKSDNILL 395
Cdd:cd05097    83 LGVCVSDDPLCMITEYMENGDLNQFLSQreiesTFTHANNIPSVSIANLlymavqiaSGMKYLASLNFVHRDLATRNCLV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 396 GMDGSVKLTDFGFCAQITPEQSKR--STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE--GEPPY--------- 462
Cdd:cd05097   163 GNHYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTlcKEQPYsllsdeqvi 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024249297 463 -----LNENPLRALYLIATNGTPelqnperlSAVFrDFLNRCLEMDVDRRGSAKELlqHPFL 519
Cdd:cd05097   243 entgeFFRNQGRQIYLSQTPLCP--------SPVF-KLMMRCWSRDIKDRPTFNKI--HHFL 293
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
273-467 3.36e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 64.29  E-value: 3.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 273 KIGQGASGTVYtaLDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENknpNIVNYLDSYLVGD----ELWVVMEYLA 346
Cdd:cd14220     2 QIGKGRYGEVW--MGKWRGEKVAVKVFFTTEEASwfRETEIYQTVLMRHE---NILGFIAADIKGTgswtQLYLITDYHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024249297 347 GGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSN--------QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 418
Cdd:cd14220    77 NGSLYDFLKCTTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNE 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024249297 419 ----RSTMVGTPYWMAPEV----VTRKAYGPKV--DIWSLGIMAIEMV----------EGEPPYLNENP 467
Cdd:cd14220   157 vdvpLNTRVGTKRYMAPEVldesLNKNHFQAYImaDIYSFGLIIWEMArrcvtggiveEYQLPYYDMVP 225
 
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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