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Conserved domains on  [gi|25143934|ref|NP_497696|]
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Serine/threonine-protein kinase prk-2 [Caenorhabditis elegans]

Protein Classification

PIM family serine/threonine-protein kinase( domain architecture ID 10195757)

PIM (Proviral Integration Moloney virus) family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
30-285 6.86e-148

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: 420.87  E-value: 6.86e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQ-VPMEICMLAKCSK--VRGVIRLLDWYSIPEG 106
Cdd:cd14005   1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINGPVpVPLEIALLLKASKpgVPGVIRLLDWYERPDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRR 186
Cdd:cd14005  81 FLLIMERPEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEVKLIDFGCGALLKD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAhllgpLPFFVP-VSAEVKDLISKC 265
Cdd:cd14005 161 SVYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFENDEQILRG-----NVLFRPrLSKECCDLISRC 235
                       250       260
                ....*....|....*....|
gi 25143934 266 LTFDPFQRCSLEAILNHPWV 285
Cdd:cd14005 236 LQFDPSKRPSLEQILSHPWF 255
 
Name Accession Description Interval E-value
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
30-285 6.86e-148

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: 420.87  E-value: 6.86e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQ-VPMEICMLAKCSK--VRGVIRLLDWYSIPEG 106
Cdd:cd14005   1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINGPVpVPLEIALLLKASKpgVPGVIRLLDWYERPDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRR 186
Cdd:cd14005  81 FLLIMERPEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEVKLIDFGCGALLKD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAhllgpLPFFVP-VSAEVKDLISKC 265
Cdd:cd14005 161 SVYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFENDEQILRG-----NVLFRPrLSKECCDLISRC 235
                       250       260
                ....*....|....*....|
gi 25143934 266 LTFDPFQRCSLEAILNHPWV 285
Cdd:cd14005 236 LQFDPSKRPSLEQILSHPWF 255
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
31-285 2.58e-70

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 222.79  E-value: 2.58e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934     31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWAringEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIV 110
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR----ERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    111 MErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQ- 188
Cdd:smart00220  76 ME--YcEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE-DGHVKLADFGLARQLDPGEk 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    189 YSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI-CTAHLLG-----PLPFFVPVSAEVKDLI 262
Cdd:smart00220 153 LTTFVGTPEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGkpkppFPPPEWDISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 25143934    263 SKCLTFDPFQRCSLEAILNHPWV 285
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
31-285 6.09e-51

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 171.27  E-value: 6.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWariNGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIV 110
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKK---KDKNILREIKILKKLNHPN-IVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   111 MERPyPCIDMFDFIKGQGKISEDMARFLFRQIAvtvhecvqnRVLHRDlkdenividlvtgstklidfgaatvlrrSQYS 190
Cdd:pfam00069  77 LEYV-EGGSLFDLLSEKGAFSEREAKFIMKQIL---------EGLESG----------------------------SSLT 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   191 DFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHL-----LGPLPFFVPVSAEVKDLISKC 265
Cdd:pfam00069 119 TFVGTPWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELiidqpYAFPELPSNLSEEAKDLLKKL 197
                         250       260
                  ....*....|....*....|
gi 25143934   266 LTFDPFQRCSLEAILNHPWV 285
Cdd:pfam00069 198 LKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
30-273 1.86e-39

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 147.85  E-value: 1.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARIngEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEAR--ERFRREARALARLNH-PNIVRVYDVGEEDGRPYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS-- 187
Cdd:COG0515  85 VMEY-VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT-PDGRVKLIDFGIARALGGAtl 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 -QYSDFQGTRLYCPPEwflhsLYLGREAA----VWSLGVLLYNSLNGRLPFR--NEKDICTAHLLGPLP----FFVPVSA 256
Cdd:COG0515 163 tQTGTVVGTPGYMAPE-----QARGEPVDprsdVYSLGVTLYELLTGRPPFDgdSPAELLRAHLREPPPppseLRPDLPP 237
                       250
                ....*....|....*..
gi 25143934 257 EVKDLISKCLTFDPFQR 273
Cdd:COG0515 238 ALDAIVLRALAKDPEER 254
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
31-333 9.90e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 97.39  E-value: 9.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   31 YKLKAELGRGGFGVVYRAVRTCDNA-LVAVKFIERSNVKE--WARingeqvpMEICMLAKCSKVrGVIRLLDWYSIPEGF 107
Cdd:PTZ00267  69 YVLTTLVGRNPTTAAFVATRGSDPKeKVVAKFVMLNDERQaaYAR-------SELHCLAACDHF-GIVKHFDDFKSDDKL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  108 LIVMERPYPCiDMFDFIKGQGK----ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIdLVTGSTKLIDFGAAtv 183
Cdd:PTZ00267 141 LLIMEYGSGG-DLNKQIKQRLKehlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFL-MPTGIIKLGDFGFS-- 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  184 lrrSQYSD---------FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFR--NEKDICTAHLLGPL-PFF 251
Cdd:PTZ00267 217 ---KQYSDsvsldvassFCGTPYYLAPELWERKRY-SKKADMWSLGVILYELLTLHRPFKgpSQREIMQQVLYGKYdPFP 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  252 VPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQTLSWDALTKNkvqkktSESSDDHHSETLGDHSETEEDRSPPTS 331
Cdd:PTZ00267 293 CPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFLKYVANLFQDIVRH------SETISPHDREEILRQLQESGERAPPPS 366

                 ..
gi 25143934  332 SV 333
Cdd:PTZ00267 367 SI 368
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
31-273 7.16e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 54.42  E-value: 7.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   31 YKLKAELGRGGFGVVYRAVRTCDNALVAVK-----------FIER-----SNVkewARIN----------GEQ--VPmei 82
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKvlrpdlardpeFVARfrreaQSA---ASLShpnivsvydvGEDggIP--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   83 cmlakcskvrgvirlldwYsipegflIVMErpY-PCIDMFDFIKGQGKISEDMA-RFLfRQI--AVTV-HecvQNRVLHR 157
Cdd:NF033483  83 ------------------Y-------IVME--YvDGRTLKDYIREHGPLSPEEAvEIM-IQIlsALEHaH---RNGIVHR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  158 DLKDENIVIDlVTGSTKLIDFG---AATVLRRSQYSDFQGTrlycppewfLHslYLGREAA----------VWSLGVLLY 224
Cdd:NF033483 132 DIKPQNILIT-KDGRVKVTDFGiarALSSTTMTQTNSVLGT---------VH--YLSPEQArggtvdarsdIYSLGIVLY 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143934  225 NSLNGRLPFRNEkdicTA------HLLGPLPffvPVSAEVKDL-------ISKCLTFDPFQR 273
Cdd:NF033483 200 EMLTGRPPFDGD----SPvsvaykHVQEDPP---PPSELNPGIpqsldavVLKATAKDPDDR 254
 
Name Accession Description Interval E-value
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
30-285 6.86e-148

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: 420.87  E-value: 6.86e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQ-VPMEICMLAKCSK--VRGVIRLLDWYSIPEG 106
Cdd:cd14005   1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINGPVpVPLEIALLLKASKpgVPGVIRLLDWYERPDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRR 186
Cdd:cd14005  81 FLLIMERPEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEVKLIDFGCGALLKD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAhllgpLPFFVP-VSAEVKDLISKC 265
Cdd:cd14005 161 SVYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFENDEQILRG-----NVLFRPrLSKECCDLISRC 235
                       250       260
                ....*....|....*....|
gi 25143934 266 LTFDPFQRCSLEAILNHPWV 285
Cdd:cd14005 236 LQFDPSKRPSLEQILSHPWF 255
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
31-285 2.46e-92

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: 279.53  E-value: 2.46e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKC-SKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14102   2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVLLKKVgSGFRGVIKLLDWYERPDGFLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRRSQY 189
Cdd:cd14102  82 VMERPEPVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTGELKLIDFGSGALLKDTVY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDIctahLLGPLPFFVPVSAEVKDLISKCLTFD 269
Cdd:cd14102 162 TDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEI----LRGRLYFRRRVSPECQQLIKWCLSLR 237
                       250
                ....*....|....*.
gi 25143934 270 PFQRCSLEAILNHPWV 285
Cdd:cd14102 238 PSDRPTLEQIFDHPWM 253
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
31-285 5.27e-92

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: 278.78  E-value: 5.27e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARI-NGEQVPMEICMLAKC-SKVRGVIRLLDWYSIPEGFL 108
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELpNGTRVPMEIVLLKKVgSGFRGVIRLLDWFERPDSFV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRRSQ 188
Cdd:cd14100  82 LVLERPEPVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGELKLIDFGSGALLKDTV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLgplpFFVPVSAEVKDLISKCLTF 268
Cdd:cd14100 162 YTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVF----FRQRVSSECQHLIKWCLAL 237
                       250
                ....*....|....*..
gi 25143934 269 DPFQRCSLEAILNHPWV 285
Cdd:cd14100 238 RPSDRPSFEDIQNHPWM 254
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
31-286 1.32e-90

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: 275.19  E-value: 1.32e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARI-NGEQVPMEICMLAKCSKV---RGVIRLLDWYSIPEG 106
Cdd:cd14101   2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLpGVNPVPNEVALLQSVGGGpghRGVIRLLDWFEIPEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRR 186
Cdd:cd14101  82 FLLVLERPQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGDIKLIDFGSGATLKD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHllgpLPFFVPVSAEVKDLISKCL 266
Cdd:cd14101 162 SMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFERDTDILKAK----PSFNKRVSNDCRSLIRSCL 237
                       250       260
                ....*....|....*....|
gi 25143934 267 TFDPFQRCSLEAILNHPWVK 286
Cdd:cd14101 238 AYNPSDRPSLEQILLHPWMM 257
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
31-285 2.58e-70

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 222.79  E-value: 2.58e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934     31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWAringEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIV 110
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR----ERILREIKILKKLKH-PNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    111 MErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQ- 188
Cdd:smart00220  76 ME--YcEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE-DGHVKLADFGLARQLDPGEk 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    189 YSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI-CTAHLLG-----PLPFFVPVSAEVKDLI 262
Cdd:smart00220 153 LTTFVGTPEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFPGDDQLlELFKKIGkpkppFPPPEWDISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 25143934    263 SKCLTFDPFQRCSLEAILNHPWV 285
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
30-284 2.54e-62

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: 201.98  E-value: 2.54e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarINGEQVPMEICMLakcSKVR--GVIRLLDWYSIPEGF 107
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKE---EIEEKIKREIEIM---KLLNhpNIIKLYEVIETENKI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR 186
Cdd:cd14003  75 YLVME--YaSGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLD-KNGNLKIIDFGLSNEFRG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQY-SDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL--GPLPFFVPVSAEVKDLIS 263
Cdd:cd14003 152 GSLlKTFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKIlkGKYPIPSHLSPDARDLIR 231
                       250       260
                ....*....|....*....|.
gi 25143934 264 KCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14003 232 RMLVVDPSKRITIEEILNHPW 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
30-284 8.84e-60

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: 195.77  E-value: 8.84e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDE---EMLRREIEILKRLDH-PNIVKLYEVFEDDKNLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST--KLIDFGAATVLRRS 187
Cdd:cd05117  77 VMEL-CTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSpiKIIDFGLAKIFEEG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 QY-SDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD------ICTAHLLGPLPFFVPVSAEVKD 260
Cdd:cd05117 156 EKlKTVCGTPYYVAPEVLKGKGY-GKKCDIWSLGVILYILLCGYPPFYGETEqelfekILKGKYSFDSPEWKNVSEEAKD 234
                       250       260
                ....*....|....*....|....
gi 25143934 261 LISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd05117 235 LIKRLLVVDPKKRLTAAEALNHPW 258
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
36-285 1.77e-57

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: 189.91  E-value: 1.77e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFI--ERSNVKEWARIN--GEqVPMEICMLAKCSKVR--GVIRLLDWYSIPEGFLI 109
Cdd:cd14004   7 EMGEGAYGQVNLAIYKSKGKEVVIKFIfkERILVDTWVRDRklGT-VPLEIHILDTLNKRShpNIVKLLDFFEDDEFYYL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQY 189
Cdd:cd14004  86 VMEKHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILD-GNGTIKLIDFGSAAYIKSGPF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDIctahLLGPLPFFVPVSAEVKDLISKCLTFD 269
Cdd:cd14004 165 DTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPFYNIEEI----LEADLRIPYAVSEDLIDLISRMLNRD 240
                       250
                ....*....|....*.
gi 25143934 270 PFQRCSLEAILNHPWV 285
Cdd:cd14004 241 VGDRPTIEELLTDPWL 256
Pkinase pfam00069
Protein kinase domain;
31-285 6.09e-51

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 171.27  E-value: 6.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWariNGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIV 110
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKK---KDKNILREIKILKKLNHPN-IVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   111 MERPyPCIDMFDFIKGQGKISEDMARFLFRQIAvtvhecvqnRVLHRDlkdenividlvtgstklidfgaatvlrrSQYS 190
Cdd:pfam00069  77 LEYV-EGGSLFDLLSEKGAFSEREAKFIMKQIL---------EGLESG----------------------------SSLT 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   191 DFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHL-----LGPLPFFVPVSAEVKDLISKC 265
Cdd:pfam00069 119 TFVGTPWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELiidqpYAFPELPSNLSEEAKDLLKKL 197
                         250       260
                  ....*....|....*....|
gi 25143934   266 LTFDPFQRCSLEAILNHPWV 285
Cdd:pfam00069 198 LKKDPSKRLTATQALQHPWF 217
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
37-283 6.23e-49

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: 165.91  E-value: 6.23e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwariNGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMERpYP 116
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKK----LLEELLREIEILKKLNH-PNIVKLYDVFETENFLYLVMEY-CE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIKGQ-GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQYSDFQ-- 193
Cdd:cd00180  75 GGSLKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDS-DGTVKLADFGLAKDLDSDDSLLKTtg 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 194 -GTRLYCPPEWFLHSLYLGREAAVWSLGVLLYnslngRLPfrnekdictahllgplpffvpvsaEVKDLISKCLTFDPFQ 272
Cdd:cd00180 154 gTTPPYYAPPELLGGRYYGPKVDIWSLGVILY-----ELE------------------------ELKDLIRRMLQYDPKK 204
                       250
                ....*....|.
gi 25143934 273 RCSLEAILNHP 283
Cdd:cd00180 205 RPSAKELLEHL 215
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
30-284 8.51e-45

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: 156.66  E-value: 8.51e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwARINgEQVPMEICMLaKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14079   3 NYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKS-LDME-EKIRREIQIL-KLFRHPHIIRLYEVIETPTDIFM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRsq 188
Cdd:cd14079  80 VME--YvSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLD-SNMNVKIADFGLSNIMRD-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 ySDFQ----GTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHllgplpFFVP--VSA 256
Cdd:cd14079 155 -GEFLktscGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPFDDEhipnlfKKIKSGI------YTIPshLSP 227
                       250       260
                ....*....|....*....|....*...
gi 25143934 257 EVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14079 228 GARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
30-273 5.63e-41

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: 146.58  E-value: 5.63e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFI---ERSNVKEWARINGEqvpMEIcmLAKCSKvRGVIRLLDWYSIPEG 106
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLrpeLAEDEEFRERFLRE---ARA--LARLSH-PNIVRVYDVGEDDGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIA---VTVHecvQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATV 183
Cdd:cd14014  75 PYIVMEY-VEGGSLADLLRERGPLPPREALRILAQIAdalAAAH---RAGIVHRDIKPANILLT-EDGRVKLTDFGIARA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQYSDFQ---GTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTA--HLLGPLPFFVP----V 254
Cdd:cd14014 150 LGDSGLTQTGsvlGTPAYMAPE-QARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLakHLQEAPPPPSPlnpdV 228
                       250
                ....*....|....*....
gi 25143934 255 SAEVKDLISKCLTFDPFQR 273
Cdd:cd14014 229 PPALDAIILRALAKDPEER 247
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
31-285 6.50e-41

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 146.40  E-value: 6.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEI-CMlaKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSK---AHLFQEVrCM--KLVQHPNVVRLYEVIDTQTKLYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPyPCIDMFDFI-KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRRSQ 188
Cdd:cd14074  80 ILELG-DGGDMYDYImKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSD-FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVP--VSAEVKDLISKC 265
Cdd:cd14074 159 KLEtSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPahVSPECKDLIRRM 238
                       250       260
                ....*....|....*....|
gi 25143934 266 LTFDPFQRCSLEAILNHPWV 285
Cdd:cd14074 239 LIRDPKKRASLEEIENHPWL 258
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
37-286 1.25e-40

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: 145.31  E-value: 1.25e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwariNG--EQVPMEICMLAKCsKVRGVIRLLDWYSIPEGFLIVMErp 114
Cdd:cd14007   8 LGKGKFGNVYLAREKKSGFIVALKVISKSQLQK----SGleHQLRREIEIQSHL-RHPNILRLYGYFEDKKRIYLILE-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 115 Y-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQYSDFQ 193
Cdd:cd14007  81 YaPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGS-NGELKLADFGWSVHAPSNRRKTFC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 194 GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPF 271
Cdd:cd14007 160 GTLDYLPPEMVEGKEY-DYKVDIWSLGVLCYELLVGKPPFesKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDPS 238
                       250
                ....*....|....*
gi 25143934 272 QRCSLEAILNHPWVK 286
Cdd:cd14007 239 KRLSLEQVLNHPWIK 253
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
37-285 2.85e-40

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: 145.00  E-value: 2.85e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVK---EWARINGEQ-VPM-----EICMLAKCSKvRGVIRLLDWYSIPEG- 106
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRkrrEGKNDRGKIkNALddvrrEIAIMKKLDH-PNIVRLYEVIDDPESd 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 -FLIVMER-PYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVTGST--KLIDFGAAT 182
Cdd:cd14008  80 kLYLVLEYcEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENL---LLTADGtvKISDFGVSE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRS--QYSDFQGTRLYCPPE--WFLHSLYLGREAAVWSLGVLLYNSLNGRLPFR--NEKDICTA--HLLGPLPFFVPV 254
Cdd:cd14008 157 MFEDGndTLQKTAGTPAFLAPElcDGDSKTYSGKAADIWALGVTLYCLVFGRLPFNgdNILELYEAiqNQNDEFPIPPEL 236
                       250       260       270
                ....*....|....*....|....*....|.
gi 25143934 255 SAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14008 237 SPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
30-273 1.86e-39

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 147.85  E-value: 1.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARIngEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:COG0515   8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEAR--ERFRREARALARLNH-PNIVRVYDVGEEDGRPYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS-- 187
Cdd:COG0515  85 VMEY-VEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT-PDGRVKLIDFGIARALGGAtl 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 -QYSDFQGTRLYCPPEwflhsLYLGREAA----VWSLGVLLYNSLNGRLPFR--NEKDICTAHLLGPLP----FFVPVSA 256
Cdd:COG0515 163 tQTGTVVGTPGYMAPE-----QARGEPVDprsdVYSLGVTLYELLTGRPPFDgdSPAELLRAHLREPPPppseLRPDLPP 237
                       250
                ....*....|....*..
gi 25143934 257 EVKDLISKCLTFDPFQR 273
Cdd:COG0515 238 ALDAIVLRALAKDPEER 254
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
31-285 1.66e-38

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: 139.83  E-value: 1.66e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVrgvIRLLDWYSIPEGFLIV 110
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHI---IRIYEVFENKDKIVIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MErpYPCI-DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQY 189
Cdd:cd14073  80 ME--YASGgELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLD-QNGNAKIADFGLSNLYSKDKL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 -SDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLLGPlpffvPVSAEVKDLI 262
Cdd:cd14073 157 lQTFCGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSdfkrlvKQISSGDYREP-----TQPSDASGLI 231
                       250       260
                ....*....|....*....|...
gi 25143934 263 SKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14073 232 RWMLTVNPKRRATIEDIANHWWV 254
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
30-285 3.97e-38

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: 139.12  E-value: 3.97e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEIcmlaKCSK--VRGVI-----------R 96
Cdd:cd14077   2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEI----SRDIrtIREAAlssllnhphicR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  97 LLDWYSIPEGFLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLI 176
Cdd:cd14077  78 LRDFLRTPNHYYMLFEY-VDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILIS-KSGNIKII 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAATVL-RRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEkDICTAH---LLGPLPFFV 252
Cdd:cd14077 156 DFGLSNLYdPRRLLRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGKVPFDDE-NMPALHakiKKGKVEYPS 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 25143934 253 PVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14077 235 YLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
31-285 1.30e-37

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: 137.70  E-value: 1.30e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRA--VRTCDNALVAVKFIERSNVKEwaringEQV----PMEICMLAKCSKvRGVIRLLDWYSIP 104
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPK------DFLekflPRELEILRKLRH-PNIIQVYSIFERG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATV 183
Cdd:cd14080  75 SKVFIFME--YaEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLD-SNNNVKLSDFGFARL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQYSD----FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPF---FVPV 254
Cdd:cd14080 152 CPDDDGDVlsktFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFddSNIKKMLKDQQNRKVRFpssVKKL 231
                       250       260       270
                ....*....|....*....|....*....|.
gi 25143934 255 SAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14080 232 SPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
30-285 2.13e-37

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: 137.00  E-value: 2.13e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringEQVPM----EICMLaKCSKVRGVIRLLDWYSIPE 105
Cdd:cd14081   2 PYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSK------ESVLMkverEIAIM-KLIEHPNVLKLYDVYENKK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVL 184
Cdd:cd14081  75 YLYLVLE--YvSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLD-EKNNIKIADFGMASLQ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQY-SDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVP--VSAEVKDL 261
Cdd:cd14081 152 PEGSLlETSCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPhfISPDAQDL 231
                       250       260
                ....*....|....*....|....
gi 25143934 262 ISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14081 232 LRRMLEVNPEKRITIEEIKKHPWF 255
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
30-277 3.16e-36

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: 134.01  E-value: 3.16e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPM--EICMLAKCSKVRGVIRLLDWYSIPEGF 107
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQKLPQlrEIDLHRRVSRHPNIITLHDVFETEVAI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERpYPCIDMFDFI--KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLR 185
Cdd:cd13993  81 YIVLEY-CPNGDLFEAIteNRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGTVKLCDFGLATTEK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSqySDFQ-GTRLYCPPEWF-----LHSLYLGREAAVWSLGVLLYNSLNGRLPFR--NEKDICTAHLLGPLP----FFVP 253
Cdd:cd13993 160 IS--MDFGvGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGIILLNLTFGRNPWKiaSESDPIFYDYYLNSPnlfdVILP 237
                       250       260
                ....*....|....*....|....
gi 25143934 254 VSAEVKDLISKCLTFDPFQRCSLE 277
Cdd:cd13993 238 MSDDFYNLLRQIFTVNPNNRILLP 261
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
31-285 1.24e-35

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: 131.94  E-value: 1.24e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWaringEQVPMEICMLAKCsKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKK-----ESILNEIAILKKC-KHPNIVKYYGSYLKKDELWIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFIKG-QGKISEDmarflfrQIAVTVHECVQ-------NRVLHRDLKDENIvidLVT--GSTKLIDFGA 180
Cdd:cd05122  76 MEF-CSGGSLKDLLKNtNKTLTEQ-------QIAYVCKEVLKgleylhsHGIIHRDIKAANI---LLTsdGEVKLIDFGL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRSQYSD-FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEkDICTAHLL---GPLPFF---VP 253
Cdd:cd05122 145 SAQLSDGKTRNtFVGTPYWMAPEVIQGKPY-GFKADIWSLGITAIEMAEGKPPYSEL-PPMKALFLiatNGPPGLrnpKK 222
                       250       260       270
                ....*....|....*....|....*....|..
gi 25143934 254 VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd05122 223 WSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
37-284 2.47e-35

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: 131.10  E-value: 2.47e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARIngEQVPMEICMLAKCsKVRGVIRLldWYSI--PEGFLIVMErp 114
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEV--EHTLNERNILERV-NHPFIVKL--HYAFqtEEKLYLVLD-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 115 Y-PCIDMFDFIKGQGKISEDMARFLFRQIAVTV---HecvQNRVLHRDLKDENIVIDLvTGSTKLIDFG-AATVLRRSQY 189
Cdd:cd05123  74 YvPGGELFSHLSKEGRFPEERARFYAAEIVLALeylH---SLGIIYRDLKPENILLDS-DGHIKLTDFGlAKELSSDGDR 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SD-FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL--GPLPFFVPVSAEVKDLISKCL 266
Cdd:cd05123 150 TYtFCGTPEYLAPEVLLGKGY-GKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKIlkSPLKFPEYVSPEAKSLISGLL 228
                       250       260
                ....*....|....*....|.
gi 25143934 267 TFDPFQR---CSLEAILNHPW 284
Cdd:cd05123 229 QKDPTKRlgsGGAEEIKAHPF 249
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
27-284 6.10e-35

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: 130.94  E-value: 6.10e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVK----EWARINgEQVPMEICMLAKCSKVRGVIRLLDWYS 102
Cdd:cd14093   1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKssenEAEELR-EATRREIEILRQVSGHPNIIELHDVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 103 IPEGFLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT 182
Cdd:cd14093  80 SPTFIFLVFEL-CRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLD-DNLNVKISDFGFAT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRSQY-SDFQGTRLYCPPEWFLHSLYL-----GREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL--GPLPFFVP- 253
Cdd:cd14093 158 RLDEGEKlRELCGTPGYLAPEVLKCSMYDnapgyGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNImeGKYEFGSPe 237
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 254 ---VSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14093 238 wddISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31-284 6.63e-35

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 130.27  E-value: 6.63e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGV--VYRAVRTcdNALVAVKFIERSNvkewaRINgEQVPMEIcMLAKCSKVRGVIRLLDWYSIPEGFL 108
Cdd:cd14662   2 YELVKDIGSGNFGVarLMRNKET--KELVAVKYIERGL-----KID-ENVQREI-INHRSLRHPNIIRFKEVVLTPTHLA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMErpYPCI-DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlvtGST----KLIDFG-AAT 182
Cdd:cd14662  73 IVME--YAAGgELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLD---GSPaprlKICDFGySKS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKD----------ICTAHLlgPLPFFV 252
Cdd:cd14662 148 SVLHSQPKSTVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDpknfrktiqrIMSVQY--KIPDYV 225
                       250       260       270
                ....*....|....*....|....*....|..
gi 25143934 253 PVSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14662 226 RVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
31-284 1.25e-34

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: 129.28  E-value: 1.25e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIerSNVKEWARINGEqvpmEICMLAKCSKVRG---VIRLLDWYSIPEG- 106
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI--KNDFRHPKAALR----EIKLLKHLNDVEGhpnIVKLLDVFEHRGGn 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 -FLIVMERPYPciDMFDFIKGQGK-ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVL 184
Cdd:cd05118  75 hLCLVFELMGM--NLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLKLADFGLARSF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR--LPFRNEKD--ICTAHLLGPLPFfvpvsaevKD 260
Cdd:cd05118 153 TSPPYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRplFPGDSEVDqlAKIVRLLGTPEA--------LD 224
                       250       260
                ....*....|....*....|....
gi 25143934 261 LISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd05118 225 LLSKMLKYDPAKRITASQALAHPY 248
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
31-284 2.91e-34

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: 128.28  E-value: 2.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarINGEQVPMEICMLaKCSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDE---ENLKKIYREVQIM-KMLNHPHIIKLYQVMETKDMLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQY 189
Cdd:cd14071  78 TE--YaSNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDA-NMNIKIADFGFSNFFKPGEL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 -SDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFR-NEKDICTAHLLG---PLPFFvpVSAEVKDLISK 264
Cdd:cd14071 155 lKTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDgSTLQTLRDRVLSgrfRIPFF--MSTDCEHLIRR 232
                       250       260
                ....*....|....*....|
gi 25143934 265 CLTFDPFQRCSLEAILNHPW 284
Cdd:cd14071 233 MLVLDPSKRLTIEQIKKHKW 252
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
28-285 5.35e-34

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: 127.88  E-value: 5.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVkewarinGEQVP---MEICMLAKCSKvRGVIRLLDWYSIP 104
Cdd:cd14078   2 LKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAL-------GDDLPrvkTEIEALKNLSH-QHICRLYHVIETD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATV 183
Cdd:cd14078  74 NKIFMVLE--YcPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLD-EDQNLKLIDFGLCAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 ---LRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVP--VSAEV 258
Cdd:cd14078 151 pkgGMDHHLETCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPewLSPSS 230
                       250       260
                ....*....|....*....|....*..
gi 25143934 259 KDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14078 231 KLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
31-285 5.71e-34

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: 127.84  E-value: 5.71e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWAR--INGEQVPMEicmlakcsKVR--GVIRLLDWYSIPEG 106
Cdd:cd14075   4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQrlLSREISSME--------KLHhpNIIRLYEVVETLSK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMErpYPCI-DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIdLVTGSTKLIDFGAATVLR 185
Cdd:cd14075  76 LHLVME--YASGgELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFY-ASNNCVKVGDFGFSTHAK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSD-FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHllgplpFFVP--VSA 256
Cdd:cd14075 153 RGETLNtFCGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAEtvaklkKCILEGT------YTIPsyVSE 226
                       250       260
                ....*....|....*....|....*....
gi 25143934 257 EVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14075 227 PCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31-284 6.38e-34

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: 127.52  E-value: 6.38e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVkewARIN-GEQVPMEICMLaKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQV---AREGmVEQIKREIAIM-KLLRHPNIVELHEVMATKTKIFF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVlrRSQY 189
Cdd:cd14663  78 VMELVTGG-ELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLD-EDGNLKISDFGLSAL--SEQF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SD------FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLLGPlPFFvpvSAE 257
Cdd:cd14663 154 RQdgllhtTCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDEnlmalyRKIMKGEFEYP-RWF---SPG 229
                       250       260
                ....*....|....*....|....*..
gi 25143934 258 VKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14663 230 AKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
30-285 7.08e-34

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: 127.25  E-value: 7.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwariNGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14072   1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNP----SSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpYPCI-DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQ 188
Cdd:cd14072  77 VME--YASGgEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLD-ADMNIKIADFGFSNEFTPGN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSD-FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGP--LPFFvpVSAEVKDLIS 263
Cdd:cd14072 154 KLDtFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFdgQNLKELRERVLRGKyrIPFY--MSTDCENLLK 231
                       250       260
                ....*....|....*....|..
gi 25143934 264 KCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14072 232 KFLVLNPSKRGTLEQIMKDRWM 253
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
31-284 7.59e-34

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: 127.41  E-value: 7.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewaRINgEQVPMEIcMLAKCSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGE-----KID-ENVQREI-INHRSLRHPNIVRFKEVILTPTHLAIV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlvtGST----KLIDFG-AATVLR 185
Cdd:cd14665  75 MEYAAGG-ELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLD---GSPaprlKICDFGySKSSVL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKD-----ICTAHLLG---PLPFFVPVSAE 257
Cdd:cd14665 151 HSQPKSTVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEprnfrKTIQRILSvqySIPDYVHISPE 230
                       250       260
                ....*....|....*....|....*..
gi 25143934 258 VKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14665 231 CRHLISRIFVADPATRITIPEIRNHEW 257
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
37-284 2.31e-33

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: 125.80  E-value: 2.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERsnvkewARING---EQVPMEICMLaKCSKVRGVIRLLDWYSIPEGFLIVMEr 113
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISR------KKLNKklqENLESEIAIL-KSIKHPNIVRLYDVQKTEDFIYLVLE- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 pYpCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVTGST-----KLIDFGAATVLRR 186
Cdd:cd14009  73 -Y-CAggDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNL---LLSTSGddpvlKIADFGFARSLQP 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSD-FQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRN------EKDICTAHLLGPLPFFVPVSAEVK 259
Cdd:cd14009 148 ASMAEtLCGSPLYMAPE-ILQFQKYDAKADLWSVGAILFEMLVGKPPFRGsnhvqlLRNIERSDAVIPFPIAAQLSPDCK 226
                       250       260
                ....*....|....*....|....*
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14009 227 DLLRRLLRRDPAERISFEEFFAHPF 251
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
32-283 2.82e-33

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 126.17  E-value: 2.82e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAeLGRGGFGVVYRaVRTCDNALVAVKFIERSNVKEWAR---INgeqvpmEICMLAKCSKVRGVIRLLDW-YSIPEGF 107
Cdd:cd14131   5 ILKQ-LGKGGSSKVYK-VLNPKKKIYALKRVDLEGADEQTLqsyKN------EIELLKKLKGSDRIIQLYDYeVTDEDDY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 L-IVMErpYPCIDMFDFIKGQ--GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVidLVTGSTKLIDFGAAT-- 182
Cdd:cd14131  77 LyMVME--CGEIDLATILKKKrpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFL--LVKGRLKLIDFGIAKai 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 ------VLRRSQYsdfqGTRLYCPPEWFL---------HSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKD-------IC 240
Cdd:cd14131 153 qndttsIVRDSQV----GTLNYMSPEAIKdtsasgegkPKSKIGRPSDVWSLGCILYQMVYGKTPFQHITNpiaklqaII 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 25143934 241 TAHLLGPLPFFVPVSAevKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd14131 229 DPNHEIEFPDIPNPDL--IDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
37-285 4.47e-33

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: 125.33  E-value: 4.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIVMErpY- 115
Cdd:cd06606   8 LGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEEL---EALEREIRILSSLKHPN-IVRYLGTERTENTLNIFLE--Yv 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKISEDMARFLFRQIA---VTVHEcvqNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSD- 191
Cdd:cd06606  82 PGGSLASLLKKFGKLPEPVVRKYTRQILeglEYLHS---NGIVHRDIKGANILVD-SDGVVKLADFGCAKRLAEIATGEg 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 ---FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD-------ICTAHLLGPLPFFVpvSAEVKDL 261
Cdd:cd06606 158 tksLRGTPYWMAPEVIRGEGY-GRAADIWSLGCTVIEMATGKPPWSELGNpvaalfkIGSSGEPPPIPEHL--SEEAKDF 234
                       250       260
                ....*....|....*....|....
gi 25143934 262 ISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06606 235 LRKCLQRDPKKRPTADELLQHPFL 258
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
27-285 4.97e-33

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: 125.07  E-value: 4.97e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGVVYRAvRTCDNALVAVKFIERSNVKEWARINGEQVPMEIcMLAKCSKvrGVIRLLDWYSIPEG 106
Cdd:cd14161   1 LKHRYEFLETLGKGTYGRVKKA-RDSSGRLVAIKSIRKDRIKDEQDLLHIRREIEI-MSSLNHP--HIISVYEVFENSSK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR 186
Cdd:cd14161  77 IVIVMEYASRG-DLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLD-ANGNIKIADFGLSNLYNQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQY-SDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLLGPlpffvPVSAEVK 259
Cdd:cd14161 155 DKFlQTYCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHdykilvKQISSGAYREP-----TKPSDAC 229
                       250       260
                ....*....|....*....|....*.
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14161 230 GLIRWLLMVNPERRATLEDVASHWWV 255
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
29-285 6.52e-33

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: 125.14  E-value: 6.52e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersNVKEWARINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFL 108
Cdd:cd14069   1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFV---DMKRAPGDCPENIKKEVCIQKMLSH-KNVVRFYGHRREGEFQY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERpypCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLR- 185
Cdd:cd14069  77 LFLEY---ASggELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLD-ENDNLKISDFGLATVFRy 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 --RSQYSDFQ-GTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL---GPLPFFVP---VSA 256
Cdd:cd14069 153 kgKERLLNKMcGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDwkeNKKTYLTPwkkIDT 232
                       250       260
                ....*....|....*....|....*....
gi 25143934 257 EVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14069 233 AALSLLRKILTENPNKRITIEDIKKHPWY 261
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
36-287 5.59e-32

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: 122.32  E-value: 5.59e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIersNVKEwARINGEQVPMEICMLAKCsKVRGVIRLLDWYSIPEGFLIVMErpy 115
Cdd:cd06623   8 VLGQGSSGVVYKVRHKPTGKIYALKKI---HVDG-DEEFRKQLLRELKTLRSC-ESPYVVKCYGAFYKEGEISIVLE--- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pCID---MFDFIKGQGKISEDMARFLFRQIA---VTVHEcvQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQY 189
Cdd:cd06623  80 -YMDggsLADLLKKVGKIPEPVLAYIARQILkglDYLHT--KRHIIHRDIKPSNLLINS-KGEVKIADFGISKVLENTLD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 --SDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL-----GPLPFFVP--VSAEVKD 260
Cdd:cd06623 156 qcNTFVGTVTYMSPERIQGESY-SYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMqaicdGPPPSLPAeeFSPEFRD 234
                       250       260
                ....*....|....*....|....*..
gi 25143934 261 LISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06623 235 FISACLQKDPKKRPSAAELLQHPFIKK 261
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
30-283 1.25e-31

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: 121.42  E-value: 1.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQvpmEICMLAKCsKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALN---EVKLLSKL-KHPNIVKYYESFEENGKLCI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpY-PCIDMFDFIKGQGK----ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVL 184
Cdd:cd08215  77 VME--YaDGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLT-KDGVVKLGDFGISKVL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSqySDFQ----GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLG---PLPFFvpVS 255
Cdd:cd08215 154 EST--TDLAktvvGTPYYLSPELCENKPY-NYKSDIWALGCVLYELCTLKHPFeaNNLPALVYKIVKGqypPIPSQ--YS 228
                       250       260
                ....*....|....*....|....*...
gi 25143934 256 AEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd08215 229 SELRDLVNSMLQKDPEKRPSANEILSSP 256
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
37-284 1.54e-31

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: 120.84  E-value: 1.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMERpyp 116
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKK------EAVLREISILNQLQH-PRIIQLHEAYESPTELVLILEL--- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 C--IDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST-KLIDFGAATVLRRSQYSDFQ 193
Cdd:cd14006  71 CsgGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQiKIIDFGLARKLNPGEELKEI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 194 -GTRLYCPPEWFLHSlYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTahLLGPL--------PFFVPVSAEVKDLISK 264
Cdd:cd14006 151 fGTPEFVAPEIVNGE-PVSLATDMWSIGVLTYVLLSGLSPFLGEDDQET--LANISacrvdfseEYFSSVSQEAKDFIRK 227
                       250       260
                ....*....|....*....|
gi 25143934 265 CLTFDPFQRCSLEAILNHPW 284
Cdd:cd14006 228 LLVKEPRKRPTAQEALQHPW 247
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
31-298 2.90e-31

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: 121.20  E-value: 2.90e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERS--NVKEwaringeqvpmEICMLAKCSKVRGVIRLLDWYSIPEGFL 108
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSkrDPSE-----------EIEILLRYGQHPNIITLRDVYDDGNSVY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERpypCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTG---STKLIDFGAATV 183
Cdd:cd14091  71 LVTEL---LRggELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpeSLRICDFGFAKQ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQ-------YsdfqgTRLYCPPEwflhslYL---GREAA--VWSLGVLLYNSLNGRLPFRNEKDICTAHLL-----G 246
Cdd:cd14091 148 LRAENgllmtpcY-----TANFVAPE------VLkkqGYDAAcdIWSLGVLLYTMLAGYTPFASGPNDTPEVILarigsG 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 247 PLPFFVP----VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ-QTLSWDALTKN 298
Cdd:cd14091 217 KIDLSGGnwdhVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNrDSLPQRQLTDP 273
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
31-284 4.37e-31

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: 120.27  E-value: 4.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARiNGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIV 110
Cdd:cd14098   2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDK-NLQLFQREINILKSLEH-PGIVRLIDWYEDDQHIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI---DLVTgsTKLIDFGAATVLRR- 186
Cdd:cd14098  80 MEY-VEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqdDPVI--VKISDFGLAKVIHTg 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLH---SLYLGREAAV--WSLGVLLYNSLNGRLPF-RNEKDICT------AHLLGPLPFFvPV 254
Cdd:cd14098 157 TFLVTFCGTMAYLAPEILMSkeqNLQGGYSNLVdmWSVGCLVYVMLTGALPFdGSSQLPVEkrirkgRYTQPPLVDF-NI 235
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 255 SAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14098 236 SEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
30-285 5.56e-31

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: 119.66  E-value: 5.56e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQvpmEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:cd14002   2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQ---EIEILRKLNH-PNIIEMLDSFETKKEFVV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA------TV 183
Cdd:cd14002  78 VTE--YAQGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIG-KGGVVKLCDFGFAramscnTL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSqysdFQGTRLYCPPEwflhslyLGRE------AAVWSLGVLLYNSLNGRLPFrnekdiCTAHLL--------GPLP 249
Cdd:cd14002 155 VLTS----IKGTPLYMAPE-------LVQEqpydhtADLWSLGCILYELFVGQPPF------YTNSIYqlvqmivkDPVK 217
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 25143934 250 FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14002 218 WPSNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
39-286 1.37e-30

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: 118.86  E-value: 1.37e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  39 RGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVrgvIRLldWYSI--PEGFLIVMErpY- 115
Cdd:cd05579   3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFV---VKL--YYSFqgKKNLYLVME--Yl 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG--AATVLRRSQYSDFQ 193
Cdd:cd05579  76 PGGDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILID-ANGHLKLTDFGlsKVGLVRRQIKLSIQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 194 ---------------GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLlgPLPFFV 252
Cdd:cd05579 155 kksngapekedrrivGTPDYLAPEILLGQGH-GKTVDWWSLGVILYEFLVGIPPFHAEtpeeifQNILNGKI--EWPEDP 231
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 25143934 253 PVSAEVKDLISKCLTFDPFQR---CSLEAILNHPWVK 286
Cdd:cd05579 232 EVSDEAKDLISKLLTPDPEKRlgaKGIEEIKNHPFFK 268
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
31-285 1.43e-30

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: 118.55  E-value: 1.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARIngEQVPMEICMLaKCSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQ--KFLPREIEVI-KGLKHPNLICFYEAIETTSRVYII 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERPYPcIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA-----TVLR 185
Cdd:cd14162  79 MELAEN-GDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLD-KNNNLKITDFGFArgvmkTKDG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSD-FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFF---VPVSAEVKDL 261
Cdd:cd14162 157 KPKLSEtYCGSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRVVFpknPTVSEECKDL 236
                       250       260
                ....*....|....*....|....
gi 25143934 262 ISKCLTFDPfQRCSLEAILNHPWV 285
Cdd:cd14162 237 ILRMLSPVK-KRITIEEIKRDPWF 259
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
37-285 1.50e-30

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: 118.56  E-value: 1.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVV--YRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVRgVIRLLDW-YSIPEGFLIVMER 113
Cdd:cd13994   1 IGKGATSVVriVTKKNPRSGVLYAVKEYRRRDDESKRKDYVKRLTSEYIISSKLHHPN-IVKVLDLcQDLHGKWCLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 pYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLR-----RSQ 188
Cdd:cd13994  80 -CPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLD-EDGVLKLTDFGTAEVFGmpaekESP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSD-FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK----------DICTAHLLGPLPFFVPVSAE 257
Cdd:cd13994 158 MSAgLCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRSAKksdsaykayeKSGDFTNGPYEPIENLLPSE 237
                       250       260
                ....*....|....*....|....*...
gi 25143934 258 VKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd13994 238 CRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
27-285 8.16e-30

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: 116.72  E-value: 8.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQ---VPMEICMLAKCSKVrGVIRLLDWYSI 103
Cdd:cd14084   4 LRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREINKprnIETEIEILKKLSHP-CIIKIEDFFDA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 PEGFLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST--KLIDFGAA 181
Cdd:cd14084  83 EDDYYIVLEL-MEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECliKITDFGLS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVL-RRSQYSDFQGTRLYCPPEWFLHSLYLG--REAAVWSLGVLLYNSLNGRLPFRNE-KDICTAH--LLGPLPFFVP-- 253
Cdd:cd14084 162 KILgETSLMKTLCGTPTYLAPEVLRSFGTEGytRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEqiLSGKYTFIPKaw 241
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 254 --VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14084 242 knVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
31-284 8.32e-30

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: 116.27  E-value: 8.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewarinGEQ--VPMEICMLAKCSKVRgVIRLLDWYSIPEGFL 108
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCK------GKEhmIENEVAILRRVKHPN-IVQLIEEYDTDTELY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMErpypCI---DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENI-VIDLVTGST--KLIDFGAAT 182
Cdd:cd14095  75 LVME----LVkggDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLlVVEHEDGSKslKLADFGLAT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRSQYSdFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFR----NEKDICTAHLLG----PLPFFVPV 254
Cdd:cd14095 151 EVKEPLFT-VCGTPTYVAPEILAETGY-GLKVDIWAAGVITYILLCGFPPFRspdrDQEELFDLILAGefefLSPYWDNI 228
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 255 SAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14095 229 SDSAKDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
29-287 2.00e-29

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: 116.37  E-value: 2.00e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersNVKEWARINGEQVPME--ICMLAKCSKVrgvIRLLDWYSiPEG 106
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKII---NTKKLSARDHQKLEREarICRLLKHPNI---VRLHDSIS-EEG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMerpypcidmFDFIKGqGKISEDM----------ARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVT--GSTK 174
Cdd:cd14086  74 FHYLV---------FDLVTG-GELFEDIvarefyseadASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSkgAAVK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 175 LIDFGAATVLRRSQ--YSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD------ICTAHLLG 246
Cdd:cd14086 144 LADFGLAIEVQGDQqaWFGFAGTPGYLSPEVLRKDPY-GKPVDIWACGVILYILLVGYPPFWDEDQhrlyaqIKAGAYDY 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25143934 247 PLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd14086 223 PSPEWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPWICQ 263
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
30-285 9.60e-29

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: 114.46  E-value: 9.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAV-RTCDNALVAVKFIERSNVKEWARINGE--QVPMEICMLAKCSkVRGVIRLLDWYSIPEG 106
Cdd:cd14096   2 NYRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRKADLSSDNLKGSSraNILKEVQIMKRLS-HPNIVKLLDFQESDEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLV----------------- 169
Cdd:cd14096  81 YYIVLEL-ADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPIpfipsivklrkadddet 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 170 ---------------TGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFR 234
Cdd:cd14096 160 kvdegefipgvggggIGIVKLADFGLSKQVWDSNTKTPCGTVGYTAPEVVKDERY-SKKVDMWALGCVLYTLLCGFPPFY 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 235 NEK-DICTAHLL-GPLPFFVP----VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14096 239 DESiETLTEKISrGDYTFLSPwwdeISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
29-284 3.34e-28

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: 112.69  E-value: 3.34e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSnvkewaRINGE----QVPMEICMLAKCSKVrGVIRLLDWYSIP 104
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKR------HIIKEkkvkYVTIEKEVLSRLAHP-GIVKLYYTFQDE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATV 183
Cdd:cd05581  74 SKLYFVLE--YaPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLD-EDMHIKITDFGTAKV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQYSD-------------------FQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFR--NEKDICTA 242
Cdd:cd05581 151 LGPDSSPEstkgdadsqiaynqaraasFVGTAEYVSPE-LLNEKPAGKSSDLWALGCIIYQMLTGKPPFRgsNEYLTFQK 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 25143934 243 HLLGPLPFFVPVSAEVKDLISKCLTFDPFQR------CSLEAILNHPW 284
Cdd:cd05581 230 IVKLEYEFPENFPPDAKDLIQKLLVLDPSKRlgvnenGGYDELKAHPF 277
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
29-301 1.16e-27

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: 111.13  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARIngEQVPMEICMLakcSKVRG--VIRLLDWYSIPEG 106
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQV--EHVLNEKRIL---SEVRHpfIVNLLGSFQDDRN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLR 185
Cdd:cd05580  76 LYMVME--YvPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLD-SDGHIKITDFGFAKRVK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSdFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEK--DICTAHLLGPLPFFVPVSAEVKDLIS 263
Cdd:cd05580 153 DRTYT-LCGTPEYLAPEIILSKGH-GKAVDWWALGILIYEMLAGYPPFFDENpmKIYEKILEGKIRFPSFFDPDAKDLIK 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 25143934 264 KCLTFDPFQRCSL-----EAILNHPWVKqqTLSWDALTKNKVQ 301
Cdd:cd05580 231 RLLVVDLTKRLGNlkngvEDIKNHPWFA--GIDWDALLQRKIP 271
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
27-285 1.32e-27

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: 110.45  E-value: 1.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringEQVPMEICMLAKCSKVRgVIRLLDWYSIPEG 106
Cdd:cd14113   5 FDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKR------DQVTHELGVLQSLQHPQ-LVGLLDTFETPTS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPypciD---MFDFIKGQGKISEDMARFLFRQIAVTV---HECvqnRVLHRDLKDENIVID--LVTGSTKLIDF 178
Cdd:cd14113  78 YILVLEMA----DqgrLLDYVVRWGNLTEEKIRFYLREILEALqylHNC---RIAHLDLKPENILVDqsLSKPTIKLADF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 GAATVLRRSQYSDfqgtRLYCPPEWFLHSLYLGREAA----VWSLGVLLYNSLNGRLPFRNEK------DICTAHLLGPL 248
Cdd:cd14113 151 GDAVQLNTTYYIH----QLLGSPEFAAPEIILGNPVSltsdLWSIGVLTYVLLSGVSPFLDESveetclNICRLDFSFPD 226
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 25143934 249 PFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14113 227 DYFKGVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
29-284 1.65e-27

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: 110.26  E-value: 1.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewARINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFL 108
Cdd:cd14165   1 RGYILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAP--DDFVEKFLPRELEILARLNH-KSIIKTYEIFETSDGKV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 -IVMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS 187
Cdd:cd14165  78 yIVMELGVQG-DLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLD-KDFNIKLTDFGFSKRCLRD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 Q------YSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFF--VPVSAE 257
Cdd:cd14165 156 EngrivlSKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYddSNVKKMLKIQKEHRVRFPrsKNLTSE 235
                       250       260
                ....*....|....*....|....*..
gi 25143934 258 VKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14165 236 CKDLIYRLLQPDVSQRLCIDEVLSHPW 262
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
27-286 2.94e-27

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: 110.85  E-value: 2.94e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKL---KAELGRGGFGVVYRAVRTCDNALVAVKFIERsnvkewaRINGEQvpmEICMLAKCSKVRGVIRLLDWYSI 103
Cdd:cd14092   1 FFQNYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVSR-------RLDTSR---EVQLLRLCQGHPNIVKLHEVFQD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 PEGFLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI--DLVTGSTKLIDFGAA 181
Cdd:cd14092  71 ELHTYLVMEL-LRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdEDDDAEIKIVDFGFA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQYSD---FqgTRLYCPPEWFLHSLYLG--REAA-VWSLGVLLYNSLNGRLPF----RNE------KDICTAHLL 245
Cdd:cd14092 150 RLKPENQPLKtpcF--TLPYAAPEVLKQALSTQgyDESCdLWSLGVILYTMLSGQVPFqspsRNEsaaeimKRIKSGDFS 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25143934 246 GPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd14092 228 FDGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQ 268
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
30-283 3.18e-27

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: 109.55  E-value: 3.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCsKVRGVIRLLDWYSIPEGFL- 108
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEK---QQLVSEVNILREL-KHPNIVRYYDRIVDRANTTl 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 -IVMErpYpCI--DMFDFIKG----QGKISEDMARFLFRQIAVTVHEC-----VQNRVLHRDLKDENIVIDlVTGSTKLI 176
Cdd:cd08217  77 yIVME--Y-CEggDLAQLIKKckkeNQYIPEEFIWKIFTQLLLALYEChnrsvGGGKILHRDLKPANIFLD-SDNNVKLG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAATVLRRSQY--SDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKD----ICTAHLLgPL 248
Cdd:cd08217 153 DFGLARVLSHDSSfaKTYVGTPYYMSPELLNEQSY-DEKSDIWSLGCLIYELCALHPPFqaANQLElakkIKEGKFP-RI 230
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 249 PFFvpVSAEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd08217 231 PSR--YSSELNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
31-284 1.13e-26

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: 108.34  E-value: 1.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarinGeqVPM----EICMLAKCSKvRGVIRLLDWYSIPEG 106
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEE-----G--IPStalrEISLLKELKH-PNIVKLLDVIHTENK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMErpYPCIDMFDFIKG-QGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGaatvLR 185
Cdd:cd07829  73 LYLVFE--YCDQDLKKYLDKrPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLIN-RDGVLKLADFG----LA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RS------QYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH----LLG--------- 246
Cdd:cd07829 146 RAfgiplrTYTHEVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFkifqILGtpteeswpg 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 247 ---------PLPFFVPVS---------AEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07829 226 vtklpdykpTFPKWPKNDlekvlprldPEGIDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
37-284 1.53e-26

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: 107.37  E-value: 1.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDN-ALVAVKFIERSNVKEWARingEQVPMEICMLaKCSKVRGVIRLLDWYSIPEGFLIVMErpY 115
Cdd:cd14121   3 LGSGTYATVYKAYRKSGArEVVAVKCVSKSSLNKAST---ENLLTEIELL-KKLKHPHIVELKDFQWDEEHIYLIME--Y 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVidLVTGST---KLIDFGAATVLR-RSQY 189
Cdd:cd14121  77 -CSggDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLL--LSSRYNpvlKLADFGFAQHLKpNDEA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SDFQGTRLYCPPEWFLHSLYLGReAAVWSLGVLLYNSLNGRLPF------------RNEKDIctahllgPLPFFVPVSAE 257
Cdd:cd14121 154 HSLRGSPLYMAPEMILKKKYDAR-VDLWSVGVILYECLFGRAPFasrsfeeleekiRSSKPI-------EIPTRPELSAD 225
                       250       260
                ....*....|....*....|....*..
gi 25143934 258 VKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14121 226 CRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
30-283 2.11e-26

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: 107.11  E-value: 2.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVkewARINGEQVPMEICMLAKCSKvRGVIRLLDwySIPEGFL- 108
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRM---SRKMREEAIDEARVLSKLNS-PYVIKYYD--SFVDKGKl 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 -IVMERPyPCIDMFDFIKGQGK--ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLr 185
Cdd:cd08529  75 nIVMEYA-ENGDLHSLIKSQRGrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLD-KGDNVKIGDLGVAKIL- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 rSQYSDFQ----GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLG---PLPffVPVSA 256
Cdd:cd08529 152 -SDTTNFAqtivGTPYYLSPELCEDKPY-NEKSDVWALGCVLYELCTGKHPFeaQNQGALILKIVRGkypPIS--ASYSQ 227
                       250       260
                ....*....|....*....|....*..
gi 25143934 257 EVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd08529 228 DLSQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
30-284 4.22e-26

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: 107.03  E-value: 4.22e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWArinGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGI---PNQALREIKALQACQGHPYVVKLRDVFPHGTGFVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpYPCIDMFDFIKGQGK-ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVL---R 185
Cdd:cd07832  78 VFE--YMLSSLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS-STGVLKIADFGLARLFseeD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDI----CTAHLLG--------------- 246
Cdd:cd07832 155 PRLYSHQVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIeqlaIVLRTLGtpnektwpeltslpd 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 25143934 247 ------------PLPFFVP-VSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07832 235 ynkitfpeskgiRLEEIFPdCSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
37-284 5.70e-26

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: 105.96  E-value: 5.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSnvkEWARINGEQVPMEICMLAKCSKVrGVIRLLDWYSIPEGFLIVMERPYP 116
Cdd:cd14082  11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKL---RFPTKQESQLRNEVAILQQLSHP-GVVNLECMFETPERVFVVMEKLHG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 ciDMFDFIKGQ--GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTG--STKLIDFGAATVL-----RRS 187
Cdd:cd14082  87 --DMLEMILSSekGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpQVKLCDFGFARIIgeksfRRS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 qysdFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDIC----TAHLLGPLPFFVPVSAEVKDLIS 263
Cdd:cd14082 165 ----VVGTPAYLAPEVLRNKGY-NRSLDMWSVGVIIYVSLSGTFPFNEDEDINdqiqNAAFMYPPNPWKEISPDAIDLIN 239
                       250       260
                ....*....|....*....|.
gi 25143934 264 KCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14082 240 NLLQVKMRKRYSVDKSLSHPW 260
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
29-284 7.82e-26

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: 105.33  E-value: 7.82e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNV-KEWARingEQVPMEIcMLAKCSKVRGVIRLLDWYSIPEGF 107
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLtKPKQR---EKLKSEI-KIHRSLKHPNIVKFHDCFEDEENV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERpypCID--MFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLR 185
Cdd:cd14099  77 YILLEL---CSNgsLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLD-ENMNVKIGDFGLAARLE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 rsqySDFQ------GTRLYCPPEWFL----HSLylgrEAAVWSLGVLLYNSLNGRLPF--RNEKDI--CTAHLLGPLPFF 251
Cdd:cd14099 153 ----YDGErkktlcGTPNYIAPEVLEkkkgHSF----EVDIWSLGVILYTLLVGKPPFetSDVKETykRIKKNEYSFPSH 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 25143934 252 VPVSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14099 225 LSISDEAKDLIRSMLQPDPTKRPSLDEILSHPF 257
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
30-285 1.99e-25

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: 104.23  E-value: 1.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCsKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDL---KSVMGEIDLLKKL-NHPNIVKYIGSVKTKDSLYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpypcidmF-------DFIKGQGKISEDMARFLFRQIA---VTVHEcvqNRVLHRDLKDENIvidLVT--GSTKLID 177
Cdd:cd06627  77 ILE--------YvengslaSIIKKFGKFPESLVAVYIYQVLeglAYLHE---QGVIHRDIKGANI---LTTkdGLVKLAD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 178 FGAATVLRRSQYSDF--QGTRLYCPPEWFLHSlylGREAA--VWSLGVLLYNSLNGRLP----------FRNEKDICTah 243
Cdd:cd06627 143 FGVATKLNEVEKDENsvVGTPYWMAPEVIEMS---GVTTAsdIWSVGCTVIELLTGNPPyydlqpmaalFRIVQDDHP-- 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 25143934 244 llgPLPffVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06627 218 ---PLP--ENISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
31-285 4.70e-25

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: 103.15  E-value: 4.70e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaRINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEG-FLI 109
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPE--EFIQRFLPRELQIVERLDH-KNIIHVYEMLESADGkIYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVTGST-KLIDFGAATVL---R 185
Cdd:cd14163  79 VMELAEDG-DVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENA---LLQGFTlKLTDFGFAKQLpkgG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE---KDICTAHLLGPLPFFVPVSAEVKDLI 262
Cdd:cd14163 155 RELSQTFCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTdipKMLCQQQKGVSLPGHLGVSRTCQDLL 234
                       250       260
                ....*....|....*....|...
gi 25143934 263 SKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14163 235 KRLLEPDMVLRPSIEEVSWHPWL 257
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
31-286 6.57e-25

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: 102.67  E-value: 6.57e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINgeqvpmEICMLAKCsKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIIN------EILIMKEC-KHPNIVDYYDSYLVGDELWVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MErpypcidmfdFIKGqGKISEDMARFLFR----QIAVTVHECVQ-------NRVLHRDLKDENIVIDLvTGSTKLIDFG 179
Cdd:cd06614  75 ME----------YMDG-GSLTDIITQNPVRmnesQIAYVCREVLQgleylhsQNVIHRDIKSDNILLSK-DGSVKLADFG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVL--RRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL---GPLPFFVP- 253
Cdd:cd06614 143 FAAQLtkEKSKRNSVVGTPYWMAPEVIKRKDY-GPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLIttkGIPPLKNPe 221
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 254 -VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06614 222 kWSPEFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
29-285 7.75e-25

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: 102.73  E-value: 7.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICmlakcSKVR--GVIRLLDWYSIPEG 106
Cdd:cd14116   5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQ-----SHLRhpNILRLYGYFHDATR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPyPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR 186
Cdd:cd14116  80 VYLILEYA-PLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLG-SAGELKIADFGWSVHAPS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVP--VSAEVKDLISK 264
Cdd:cd14116 158 SRRTTLCGTLDYLPPEMIEGRMH-DEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPdfVTEGARDLISR 236
                       250       260
                ....*....|....*....|.
gi 25143934 265 CLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14116 237 LLKHNPSQRPMLREVLEHPWI 257
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
31-284 9.01e-25

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 103.00  E-value: 9.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIER--SNVKEWARINgeqvpmEICMLAKCSKVRGVIRLLDWYSIPEGFL 108
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKkfYSWEECMNLR------EVKSLRKLNEHPNIVKLKEVFRENDELY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMErpypCID--MFDFIKGQ--GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVTGST--KLIDFGAAT 182
Cdd:cd07830  75 FVFE----YMEgnLYQLMKDRkgKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENL---LVSGPEvvKIADFGLAR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLR-RSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR--LPFRNEKD----ICT-------------- 241
Cdd:cd07830 148 EIRsRPPYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRplFPGSSEIDqlykICSvlgtptkqdwpegy 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 242 --AHLLG---------PLPFFVP-VSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07830 228 klASKLGfrfpqfaptSLHQLIPnASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
37-284 1.45e-24

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: 101.58  E-value: 1.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIVMErpyp 116
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKK------EQAAHEAALLQHLQHPQ-YITLHDTYESPTSYILVLE---- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CID---MFDFIKGQGKISEDMARFLFRQIAVTV---HECvqnRVLHRDLKDENIVIDLV--TGSTKLIDFGAA---TVLR 185
Cdd:cd14115  70 LMDdgrLLDYLMNHDELMEEKVAFYIRDIMEALqylHNC---RVAHLDIKPENLLIDLRipVPRVKLIDLEDAvqiSGHR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYsdFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK------DICTAHLLGPLPFFVPVSAEVK 259
Cdd:cd14115 147 HVHH--LLGNPEFAAPE-VIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESkeetciNVCRVDFSFPDEYFGDVSQAAR 223
                       250       260
                ....*....|....*....|....*
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14115 224 DFINVILQEDPRRRPTAATCLQHPW 248
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
27-287 2.05e-24

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: 101.92  E-value: 2.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGVVYRAV--RTCDNalVAVKFIE-----RSNVKEWARINgEQVPMEICMLAKCSKVRGVIRLLD 99
Cdd:cd14182   1 FYEKYEPKEILGRGVSSVVRRCIhkPTRQE--YAVKIIDitgggSFSPEEVQELR-EATLKEIDILRKVSGHPNIIQLKD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 100 WYSIPEGFLIV---MERPypciDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLI 176
Cdd:cd14182  78 TYETNTFFFLVfdlMKKG----ELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLD-DDMNIKLT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAATVLRRSQ-YSDFQGTRLYCPPEWFL------HSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL--GP 247
Cdd:cd14182 153 DFGFSCQLDPGEkLREVCGTPGYLAPEIIEcsmddnHPGY-GKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMImsGN 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 25143934 248 LPFFVP----VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd14182 232 YQFGSPewddRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
29-284 3.07e-24

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: 101.26  E-value: 3.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERsnvkewARINGEQ--VPMEICMLAKCsKVRGVIRLLDWYSIPEG 106
Cdd:cd14184   1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDK------AKCCGKEhlIENEVSILRRV-KHPNIIMLIEEMDTPAE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLV---TGSTKLIDFGAATV 183
Cdd:cd14184  74 LYLVMEL-VKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYpdgTKSLKLGDFGLATV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQYSdFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD--------ICTAHLLGPLPFFVPVS 255
Cdd:cd14184 153 VEGPLYT-VCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRSENNlqedlfdqILLGKLEFPSPYWDNIT 230
                       250       260
                ....*....|....*....|....*....
gi 25143934 256 AEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14184 231 DSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
37-284 3.53e-24

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


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 100.76  E-value: 3.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWaringEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIVMErpyp 116
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDR-----EDVRNEIEIMNQLRHPR-LLQLYDAFETPREMVLVME---- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CID---MFD-FIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIV-IDLVTGSTKLIDFGAAtvlRRSQYSD 191
Cdd:cd14103  71 YVAggeLFErVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNQIKIIDFGLA---RKYDPDK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 ----FQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPL------PFFVPVSAEVKDL 261
Cdd:cd14103 148 klkvLFGTPEFVAPE-VVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAkwdfddEAFDDISDEAKDF 226
                       250       260
                ....*....|....*....|...
gi 25143934 262 ISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14103 227 ISKLLVKDPRKRMSAAQCLQHPW 249
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
31-284 6.38e-24

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: 100.47  E-value: 6.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKfIERSNvKEW---ARINGEQVPMEICMLAKCSKVRGVIRLLDWYSI-PEG 106
Cdd:cd13990   2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACK-IHQLN-KDWseeKKQNYIKHALREYEIHKSLDHPRIVKLYDVFEIdTDS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMErpY-PCIDMFDFIKGQGKISEDMARFLFRQI--AVTVHECVQNRVLHRDLKDENIVID--LVTGSTKLIDFGAA 181
Cdd:cd13990  80 FCTVLE--YcDGNDLDFYLKQHKSIPEREARSIIMQVvsALKYLNEIKPPIIHYDLKPGNILLHsgNVSGEIKITDFGLS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQYSD--------FQGTRLYCPPEWFLhslyLGREAA-------VWSLGVLLYNSLNGRLPF-RNEKDICTAHLL 245
Cdd:cd13990 158 KIMDDESYNSdgmeltsqGAGTYWYLPPECFV----VGKTPPkisskvdVWSVGVIFYQMLYGRKPFgHNQSQEAILEEN 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 25143934 246 GPL-------PFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd13990 234 TILkatevefPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
31-285 7.47e-24

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: 100.09  E-value: 7.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWAR-INGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:cd14194   7 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRgVSREDIEREVSILKEIQH-PNVITLHEVYENKTDVIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI---DLVTGSTKLIDFGAATVLRR 186
Cdd:cd14194  86 ILEL-VAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLldrNVPKPRIKIIDFGLAHKIDF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 -SQYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPL------PFFVPVSAEVK 259
Cdd:cd14194 165 gNEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVnyefedEYFSNTSALAK 243
                       250       260
                ....*....|....*....|....*.
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14194 244 DFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
37-284 9.21e-24

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: 99.61  E-value: 9.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEW---ARINGEQVPMEICmlakCSKVrgVIRLLDWYSIPEGFLIVMEr 113
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTrqqEHIFSEKEILEEC----NSPF--IVKLYRTFKDKKYLYMLME- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 pyPCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQ--Y 189
Cdd:cd05572  74 --YCLggELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDS-NGYVKLVDFGFAKKLGSGRktW 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SdFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD----ICTAHLLGPLPFFVP--VSAEVKDLIS 263
Cdd:cd05572 151 T-FCGTPEYVAPEIILNKGY-DFSVDYWSLGILLYELLTGRPPFGGDDEdpmkIYNIILKGIDKIEFPkyIDKNAKNLIK 228
                       250       260
                ....*....|....*....|....*.
gi 25143934 264 KCLTFDPFQRC-----SLEAILNHPW 284
Cdd:cd05572 229 QLLRRNPEERLgylkgGIRDIKKHKW 254
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-298 9.51e-24

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: 99.96  E-value: 9.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewarinGEQ--VPMEICMLAKCSKvRGVIRLLDWYSIPEGFL 108
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALR------GKEamVENEIAVLRRINH-ENIVSLEDIYESPTHLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLI--DFGAATVLRR 186
Cdd:cd14169  78 LAMEL-VTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMisDFGLSKIEAQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD------ICTAHLLGPLPFFVPVSAEVKD 260
Cdd:cd14169 157 GMLSTACGTPGYVAPELLEQKPY-GKAVDVWAIGVISYILLCGYPPFYDENDselfnqILKAEYEFDSPYWDDISESAKD 235
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 25143934 261 LISKCLTFDPFQRCSLEAILNHPWVKQQTlswdALTKN 298
Cdd:cd14169 236 FIRHLLERDPEKRFTCEQALQHPWISGDT----ALDRD 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
31-286 1.21e-23

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: 99.69  E-value: 1.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWAR-INGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:cd14195   7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRgVSREEIEREVNILREIQH-PNIITLHDIFENKTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI---DLVTGSTKLIDFGAATVLRR 186
Cdd:cd14195  86 ILEL-VSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldkNVPNPRIKLIDFGIAHKIEA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 -SQYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLLGPLPFFVPVSAEVK 259
Cdd:cd14195 165 gNEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGEtkqetlTNISAVNYDFDEEYFSNTSELAK 243
                       250       260
                ....*....|....*....|....*..
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd14195 244 DFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
31-285 1.58e-23

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 99.48  E-value: 1.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWAR-INGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:cd14105   7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRgVSREDIEREVSILRQVLH-PNIITLHDVFENKTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI---DLVTGSTKLIDFGAATVLRR 186
Cdd:cd14105  86 ILEL-VAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldkNVPIPRIKLIDFGLAHKIED 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQ-YSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPL------PFFVPVSAEVK 259
Cdd:cd14105 165 GNeFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVnydfddEYFSNTSELAK 243
                       250       260
                ....*....|....*....|....*.
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14105 244 DFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
37-299 1.85e-23

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: 100.82  E-value: 1.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIersnvKEWARINGEQ---VPMEICMLAKCSKvRGVIRLLdwYSI--PEGFLIVM 111
Cdd:cd05573   9 IGRGAFGEVWLVRDKDTGQVYAMKIL-----RKSDMLKREQiahVRAERDILADADS-PWIVRLH--YAFqdEDHLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 ERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSD 191
Cdd:cd05573  81 EY-MPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLD-ADGHIKLADFGLCTKMNKSGDRE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQ-------------------------------GTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDIC 240
Cdd:cd05573 159 SYlndsvntlfqdnvlarrrphkqrrvraysavGTPDYIAPE-VLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVE 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 241 TA--------HLLgpLPFFVPVSAEVKDLISKCLTfDPFQR-CSLEAILNHPWVKqqTLSWDALTKNK 299
Cdd:cd05573 238 TYskimnwkeSLV--FPDDPDVSPEAIDLIRRLLC-DPEDRlGSAEEIKAHPFFK--GIDWENLRESP 300
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
36-287 2.18e-23

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: 98.96  E-value: 2.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEWARingEQVPMEICMLAKCSKVRgvirLLDWYsipeGFLIVMERPY 115
Cdd:cd06605   8 ELGEGNGGVVSKVRHRPSGQIMAVKVI-RLEIDEALQ---KQILRELDVLHKCNSPY----IVGFY----GAFYSEGDIS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFD------FIKGQGKISEDMARFLFRQI--AVT-VHEcvQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR 186
Cdd:cd06605  76 ICMEYMDggsldkILKEVGRIPERILGKIAVAVvkGLIyLHE--KHKIIHRDVKPSNILVN-SRGQVKLCDFGVSGQLVD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEK--------DICTAHLLGPLPFFV--PVSA 256
Cdd:cd06605 153 SLAKTFVGTRSYMAPERISGGKY-TVKSDIWSLGLSLVELATGRFPYPPPNakpsmmifELLSYIVDEPPPLLPsgKFSP 231
                       250       260       270
                ....*....|....*....|....*....|.
gi 25143934 257 EVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06605 232 DFQDFVSQCLQKDPTERPSYKELMEHPFIKR 262
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
23-284 2.33e-23

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: 99.27  E-value: 2.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  23 GFSKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewARINGEQVP-------MEICMLAKCSKVRGVI 95
Cdd:cd14181   4 GAKEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTA----ERLSPEQLEevrsstlKEIHILRQVSGHPSII 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  96 RLLDWYSIPEGFLIV---MERPypciDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGS 172
Cdd:cd14181  80 TLIDSYESSTFIFLVfdlMRRG----ELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLD-DQLH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 173 TKLIDFGAATVLRRSQ-YSDFQGTRLYCPPEWF------LHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL 245
Cdd:cd14181 155 IKLSDFGFSCHLEPGEkLRELCGTPGYLAPEILkcsmdeTHPGY-GKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMI 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 25143934 246 --GPLPFFVPV----SAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14181 234 meGRYQFSSPEwddrSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
31-285 2.52e-23

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: 98.49  E-value: 2.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARingeQVPMEICMLAKCSKV-----RGVIRLLDWYSIPE 105
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIK--NNKDYLD----QSLDEIRLLELLNKKdkadkYHIVRLKDVFYFKN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMErpYPCIDMFDFIKGQGKISEDMARFlfRQIAVTVHECVQ----NRVLHRDLKDENIVI-DLVTGSTKLIDFGA 180
Cdd:cd14133  75 HLCIVFE--LLSQNLYEFLKQNKFQYLSLPRI--RKIAQQILEALVflhsLGLIHCDLKPENILLaSYSRCQIKIIDFGS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRSQYSDFQgTRLYCPPEWFLHSLYLGReAAVWSLGVLLYNSLNGRLPFRNEKDI----CTAHLLGPLPFFVPVSA 256
Cdd:cd14133 151 SCFLTQRLYSYIQ-SRYYRAPEVILGLPYDEK-IDMWSLGCILAELYTGEPLFPGASEVdqlaRIIGTIGIPPAHMLDQG 228
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 257 -----EVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14133 229 kaddeLFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
31-285 2.98e-23

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: 98.39  E-value: 2.98e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewARINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFL-I 109
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRAS--PDFVQKFLPRELSILRRVNH-PNIVQMFECIEVANGRLyI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPypCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLrrSQY 189
Cdd:cd14164  79 VMEAA--ATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRKIKIADFGFARFV--EDY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SD----FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFrnekDICTAHLL-----GPL-PFFVPVSAEVK 259
Cdd:cd14164 155 PElsttFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPF----DETNVRRLrlqqrGVLyPSGVALEEPCR 230
                       250       260
                ....*....|....*....|....*.
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14164 231 ALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
38-285 3.21e-23

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: 98.14  E-value: 3.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  38 GRGGFGVVYRAVRTCDNALVAVKFI--ERSNVKEWARINGEQVPMEicMLAKCSKVRgvirlldWYSIP---EGFLIVME 112
Cdd:cd06626   9 GEGTFGKVYTAVNLDTGELMAMKEIrfQDNDPKTIKEIADEMKVLE--GLDHPNLVR-------YYGVEvhrEEVYIFME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 rpYpCID--MFDFIKgQGKI-SEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA-------T 182
Cdd:cd06626  80 --Y-CQEgtLEELLR-HGRIlDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLD-SNGLIKLGDFGSAvklknntT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRSQYSDFQGTRLYCPPEWFLHSLYLGREAA--VWSLGVLLYNSLNGRLP---FRNEKDI---CTAHLLGPLPFFVPV 254
Cdd:cd06626 155 TMAPGEVNSLVGTPAYMAPEVITGNKGEGHGRAadIWSLGCVVLEMATGKRPwseLDNEWAImyhVGMGHKPPIPDSLQL 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 25143934 255 SAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06626 235 SPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
29-285 3.55e-23

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: 98.01  E-value: 3.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEI-CMLAKCSkvrgVIRLLDWYSIPEGF 107
Cdd:cd14186   1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIhCQLKHPS----ILELYNYFEDSNYV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERPYPCiDMFDFIKGQGK-ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR 186
Cdd:cd14186  77 YLVLEMCHNG-EMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLT-RNMNIKIADFGLATQLKM 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQ--GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE--KDICTAHLLGPLPFFVPVSAEVKDLI 262
Cdd:cd14186 155 PHEKHFTmcGTPNYISPEIATRSAH-GLESDVWSLGCMFYTLLVGRPPFDTDtvKNTLNKVVLADYEMPAFLSREAQDLI 233
                       250       260
                ....*....|....*....|...
gi 25143934 263 SKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14186 234 HQLLRKNPADRLSLSSVLDHPFM 256
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
31-284 4.41e-23

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: 97.71  E-value: 4.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVyRAVRTCD-NALVAVKFIERSNVKEwariNGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:cd14185   2 YEIGRTIGDGNFAVV-KECRHWNeNQEYAMKIIDKSKLKG----KEDMIESEILIIKSLSH-PNIVKLFEVYETEKEIYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDL-VTGST--KLIDFGAATVLRR 186
Cdd:cd14185  76 ILEY-VRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHnPDKSTtlKLADFGLAKYVTG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSdFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFR----NEKDICTAHLLGPLPFFVP----VSAEV 258
Cdd:cd14185 155 PIFT-VCGTPTYVAPEILSEKGY-GLEVDMWAAGVILYILLCGFPPFRsperDQEELFQIIQLGHYEFLPPywdnISEAA 232
                       250       260
                ....*....|....*....|....*.
gi 25143934 259 KDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14185 233 KDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
28-284 5.92e-23

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: 97.44  E-value: 5.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwariNGEQVPMEICMLAKCsKVRGVIRLLDWYSIPEGF 107
Cdd:cd14083   2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKG----KEDSLENEIAVLRKI-KHPNIVQLLDIYESKSHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLI--DFGAATVLR 185
Cdd:cd14083  77 YLVMEL-VTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMisDFGLSKMED 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD------ICTAHLLGPLPFFVPVSAEVK 259
Cdd:cd14083 156 SGVMSTACGTPGYVAPEVLAQKPY-GKAVDCWSIGVISYILLCGYPPFYDENDsklfaqILKAEYEFDSPYWDDISDSAK 234
                       250       260
                ....*....|....*....|....*
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14083 235 DFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
31-285 1.28e-22

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 96.95  E-value: 1.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWAR-INGEQVPMEICMLAKCSKVrGVIRLLDWYSIPEGFLI 109
Cdd:cd14196   7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgVSREEIEREVSILRQVLHP-NIITLHDVYENRTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI---DLVTGSTKLIDFGAA-TVLR 185
Cdd:cd14196  86 ILEL-VSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldkNIPIPHIKLIDFGLAhEIED 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK------DICTAHLLGPLPFFVPVSAEVK 259
Cdd:cd14196 165 GVEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGDTkqetlaNITAVSYDFDEEFFSHTSELAK 243
                       250       260
                ....*....|....*....|....*.
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14196 244 DFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
37-281 1.49e-22

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: 96.07  E-value: 1.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAvrTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMErpY- 115
Cdd:cd13999   1 IGSGSFGEVYKG--KWRGTDVAIKKLKVEDDNDELL---KEFRREVSILSKLRH-PNIVQFIGACLSPPPLCIVTE--Ym 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQG---------KISEDMAR---FLfrqiavtvHecvQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATV 183
Cdd:cd13999  73 PGGSLYDLLHKKKiplswslrlKIALDIARgmnYL--------H---SPPIIHRDLKSLNILLDE-NFTVKIADFGLSRI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LrrSQYSDFQGTRLYCP----PEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI------CTAHLLGPLPFFVP 253
Cdd:cd13999 141 K--NSTTEKMTGVVGTPrwmaPEVLRGEPY-TEKADVYSFGIVLWELLTGEVPFKELSPIqiaaavVQKGLRPPIPPDCP 217
                       250       260
                ....*....|....*....|....*...
gi 25143934 254 VsaEVKDLISKCLTFDPFQRCSLEAILN 281
Cdd:cd13999 218 P--ELSKLIKRCWNEDPEKRPSFSEIVK 243
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
37-283 1.86e-22

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: 95.90  E-value: 1.86e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRA-VRTCDNALVAVKFIERSNVKEWARINGEqvpmEICMLaKCSKVRGVIRLLDWYSIPEGFLIVMErpY 115
Cdd:cd14120   1 IGHGAFAVVFKGrHRKKPDLPVAIKCITKKNLSKSQNLLGK----EIKIL-KELSHENVVALLDCQETSSSVYLVME--Y 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pC--IDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST--------KLIDFGAATVLR 185
Cdd:cd14120  74 -CngGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKpspndirlKIADFGFARFLQ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYS-DFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPF--------RN--EKdicTAHLLGPLPffVPV 254
Cdd:cd14120 153 DGMMAaTLCGSPMYMAPE-VIMSLQYDAKADLWSIGTIVYQCLTGKAPFqaqtpqelKAfyEK---NANLRPNIP--SGT 226
                       250       260
                ....*....|....*....|....*....
gi 25143934 255 SAEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd14120 227 SPALKDLLLGLLKRNPKDRIDFEDFFSHP 255
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
36-293 2.32e-22

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: 96.01  E-value: 2.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVrgVIRLLDWYSIPEGFLIVMERpY 115
Cdd:cd05611   3 PISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPY--VAKLYYSFQSKDYLYLVMEY-L 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG-AATVLRRSQYSDFQG 194
Cdd:cd05611  80 NGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLID-QTGHLKLTDFGlSRNGLEKRHNKKFVG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 195 TRLYCPPEWFLHslyLGREAAV--WSLGVLLYNSLNGRLPFRNE------KDICTAHLLGPLPFFVPVSAEVKDLISKCL 266
Cdd:cd05611 159 TPDYLAPETILG---VGDDKMSdwWSLGCVIFEFLFGYPPFHAEtpdavfDNILSRRINWPEEVKEFCSPEAVDLINRLL 235
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 267 TFDPFQRCS---LEAILNHPWVKqqTLSWD 293
Cdd:cd05611 236 CMDPAKRLGangYQEIKSHPFFK--SINWD 263
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
28-289 2.98e-22

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: 96.21  E-value: 2.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEqvpmeICMLAKCsKVRGVIRLLDWYSIPEGF 107
Cdd:cd14166   2 RETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENE-----IAVLKRI-KHENIVTLEDIYESTTHY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLI--DFGAATVLR 185
Cdd:cd14166  76 YLVMQL-VSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMitDFGLSKMEQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD------ICTAHLLGPLPFFVPVSAEVK 259
Cdd:cd14166 155 NGIMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVITYILLCGYPPFYEETEsrlfekIKEGYYEFESPFWDDISESAK 233
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWVKQQT 289
Cdd:cd14166 234 DFIRHLLEKNPSKRYTCEKALSHPWIIGNT 263
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
27-301 5.16e-22

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: 95.47  E-value: 5.16e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewaRINGEqvpmEICMLAKCSKVRGVIRLLDWYSIPEG 106
Cdd:cd14178   1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSK-----RDPSE----EIEILLRYGQHPNIITLKDVYDDGKF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTG---STKLIDFGAATV 183
Cdd:cd14178  72 VYLVMELMRGG-ELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGnpeSIRICDFGFAKQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQ-------YsdfqgTRLYCPPEWFLHSlylGREAA--VWSLGVLLYNSLNGRLPFRNEKDICTAHLL---GPLPFF 251
Cdd:cd14178 151 LRAENgllmtpcY-----TANFVAPEVLKRQ---GYDAAcdIWSLGILLYTMLAGFTPFANGPDDTPEEILariGSGKYA 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 252 V------PVSAEVKDLISKCLTFDPFQRCSLEAILNHPW-VKQQTLSWDALTKNKVQ 301
Cdd:cd14178 223 LsggnwdSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWiVNREYLSQNQLSRQDVH 279
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
37-288 5.75e-22

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: 95.23  E-value: 5.75e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFI----ERSNVKEWARingeqvpmEICMLA--KCSKVRGVIRLLDWYsipegfliv 110
Cdd:cd06917   9 VGRGSYGAVYRGYHVKTGRVVALKVLnldtDDDDVSDIQK--------EVALLSqlKLGQPKNIIKYYGSY--------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERPYPCIDMfDFIKG--------QGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAAT 182
Cdd:cd06917  72 LKGPSLWIIM-DYCEGgsirtlmrAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTN-TGNVKLCDFGVAA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLR--RSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLG-------PLPFFvp 253
Cdd:cd06917 150 SLNqnSSKRSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPkskpprlEGNGY-- 227
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 254 vSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQ 288
Cdd:cd06917 228 -SPLLKEFVAACLDEEPKDRLSADELLKSKWIKQH 261
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
37-285 7.46e-22

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: 94.25  E-value: 7.46e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewaRI-NGEQ-VPMEICMLAKCsKVRGVIRLLDWYSIPEG--FLIVME 112
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLR---RIpNGEAnVKREIQILRRL-NHRNVIKLVDVLYNEEKqkLYMVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 rpYpCI----DMFDFIKgQGKISEDMARFLFRQIAVT---VHECvqnRVLHRDLKDENIvidLVT--GSTKLIDFGAATV 183
Cdd:cd14119  77 --Y-CVgglqEMLDSAP-DKRLPIWQAHGYFVQLIDGleyLHSQ---GIIHKDIKPGNL---LLTtdGTLKISDFGVAEA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQYSD----FQGTRLYCPPE--WFLHSlYLGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAhllgplPFF 251
Cdd:cd14119 147 LDLFAEDDtcttSQGSPAFQPPEiaNGQDS-FSGFKVDIWSAGVTLYNMTTGKYPFEGDniyklfENIGKG------EYT 219
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 25143934 252 VP--VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14119 220 IPddVDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
31-285 8.45e-22

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: 94.47  E-value: 8.45e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNAL-----VAVKFIERSNVKEWARINgeQVPMEICMLaKCSKVRGVIRLLDWYSIPE 105
Cdd:cd14076   3 YILGRTLGEGEFGKVKLGWPLPKANHrsgvqVAIKLIRRDTQQENCQTS--KIMREINIL-KGLTHPNIVRLLDVLKTKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlvTGSTKLI-DFGAATVL 184
Cdd:cd14076  80 YIGIVLEFVSGG-ELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLD--KNRNLVItDFGFANTF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYSDFQ---GTRLYCPPEWF-LHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKD-------------ICTAhllgP 247
Cdd:cd14076 157 DHFNGDLMStscGSPCYAAPELVvSDSMYAGRKADIWSCGVILYAMLAGYLPFDDDPHnpngdnvprlyryICNT----P 232
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 25143934 248 LPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14076 233 LIFPEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
31-303 9.12e-22

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: 94.71  E-value: 9.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewaRINGEqvpmEICMLAKCSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd14175   3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSK-----RDPSE----EIEILLRYGQHPNIITLKDVYDDGKHVYLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTG---STKLIDFGAATVLRrs 187
Cdd:cd14175  74 TELMRGG-ELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGnpeSLRICDFGFAKQLR-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 qySDFQGTRLYCPPEWFLHSLYLGREAA-----VWSLGVLLYNSLNGRLPFRNEKDICTAHLL---GPLPFFV------P 253
Cdd:cd14175 151 --AENGLLMTPCYTANFVAPEVLKRQGYdegcdIWSLGILLYTMLAGYTPFANGPSDTPEEILtriGSGKFTLsggnwnT 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 25143934 254 VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQtlswDALTKNKVQKK 303
Cdd:cd14175 229 VSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQK----DKLPQSQLNHQ 274
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
31-333 9.90e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 97.39  E-value: 9.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   31 YKLKAELGRGGFGVVYRAVRTCDNA-LVAVKFIERSNVKE--WARingeqvpMEICMLAKCSKVrGVIRLLDWYSIPEGF 107
Cdd:PTZ00267  69 YVLTTLVGRNPTTAAFVATRGSDPKeKVVAKFVMLNDERQaaYAR-------SELHCLAACDHF-GIVKHFDDFKSDDKL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  108 LIVMERPYPCiDMFDFIKGQGK----ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIdLVTGSTKLIDFGAAtv 183
Cdd:PTZ00267 141 LLIMEYGSGG-DLNKQIKQRLKehlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFL-MPTGIIKLGDFGFS-- 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  184 lrrSQYSD---------FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFR--NEKDICTAHLLGPL-PFF 251
Cdd:PTZ00267 217 ---KQYSDsvsldvassFCGTPYYLAPELWERKRY-SKKADMWSLGVILYELLTLHRPFKgpSQREIMQQVLYGKYdPFP 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  252 VPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQTLSWDALTKNkvqkktSESSDDHHSETLGDHSETEEDRSPPTS 331
Cdd:PTZ00267 293 CPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFLKYVANLFQDIVRH------SETISPHDREEILRQLQESGERAPPPS 366

                 ..
gi 25143934  332 SV 333
Cdd:PTZ00267 367 SI 368
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
25-285 9.96e-22

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: 94.29  E-value: 9.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  25 SKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewARINGEQVPMEICMLAKCsKVRGVIRLLDWYSIP 104
Cdd:cd14183   2 ASISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSK----CRGKEHMIQNEVSILRRV-KHPNIVLLIEEMDMP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI---DLVTGSTKLIDFGAA 181
Cdd:cd14183  77 TELYLVMEL-VKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehQDGSKSLKLGDFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQYSdFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD--------ICTAHLLGPLPFFVP 253
Cdd:cd14183 156 TVVDGPLYT-VCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRGSGDdqevlfdqILMGQVDFPSPYWDN 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 25143934 254 VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14183 234 VSDSAKELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
30-283 1.03e-21

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: 94.00  E-value: 1.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQvpmEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVN---EIRLLASVNH-PNIIRYKEAFLDGNRLCI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpY-PCIDMFDFIKGQGK----ISEDMARFLFRQIAV---TVHECvqnRVLHRDLKDENIVI---DLVtgstKLIDF 178
Cdd:cd08530  77 VME--YaPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRglkALHDQ---KILHRDLKSANILLsagDLV----KIGDL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 GAATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPV-S 255
Cdd:cd08530 148 GISKVLKKNLAKTQIGTPLYAAPEVWKGRPY-DYKSDIWSLGCLLYEMATFRPPFeaRTMQELRYKVCRGKFPPIPPVyS 226
                       250       260
                ....*....|....*....|....*...
gi 25143934 256 AEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd08530 227 QDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
27-288 1.22e-21

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: 94.53  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPME--ICMLAKCSKVrgvIRLLDWYSiP 104
Cdd:cd14094   1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREasICHMLKHPHI---VELLETYS-S 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIV----MERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST--KLIDF 178
Cdd:cd14094  77 DGMLYMvfefMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApvKLGGF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 GAATVLRRSQY--SDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEK-DICTAHLLGPLPFFVP-- 253
Cdd:cd14094 157 GVAIQLGESGLvaGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKeRLFEGIIKGKYKMNPRqw 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 25143934 254 --VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQ 288
Cdd:cd14094 236 shISESAKDLVRRMLMLDPAERITVYEALNHPWIKER 272
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-306 1.47e-21

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: 94.12  E-value: 1.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSnvkewarINGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIV 110
Cdd:cd14085   5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKT-------VDKKIVRTEIGVLLRLSHPN-IIKLKEIFETPTEISLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST--KLIDFGAATVL-RRS 187
Cdd:cd14085  77 LEL-VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAplKIADFGLSKIVdQQV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 QYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE-------KDICTAHLLGPLPFFVPVSAEVKD 260
Cdd:cd14085 156 TMKTVCGTPGYCAPEILRGCAY-GPEVDMWSVGVITYILLCGFEPFYDErgdqymfKRILNCDYDFVSPWWDDVSLNAKD 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 25143934 261 LISKCLTFDPFQRCSLEAILNHPWVKQQTLSWDALtkNKVQKKTSE 306
Cdd:cd14085 235 LVKKLIVLDPKKRLTTQQALQHPWVTGKAANFAHM--DTAQKKLQE 278
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
36-285 1.57e-21

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: 93.57  E-value: 1.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERPy 115
Cdd:cd14106  15 PLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCR---NEILHEIAVLELCKDCPRVVNLHEVYETRSELILILELA- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIV--IDLVTGSTKLIDFGAATVLRRS-QYSDF 192
Cdd:cd14106  91 AGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILltSEFPLGDIKLCDFGISRVIGEGeEIREI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 193 QGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK------DICTAHLLGPLPFFVPVSAEVKDLISKCL 266
Cdd:cd14106 171 LGTPDYVAPE-ILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDkqetflNISQCNLDFPEELFKDVSPLAIDFIKRLL 249
                       250
                ....*....|....*....
gi 25143934 267 TFDPFQRCSLEAILNHPWV 285
Cdd:cd14106 250 VKDPEKRLTAKECLEHPWL 268
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
30-284 1.87e-21

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: 93.09  E-value: 1.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVyRAVRTCDNALV-AVKFIERsnvkewaringeqvpmeicmlAKCSK---VRGVIRLLDwysipe 105
Cdd:cd05578   1 HFQILRVIGKGSFGKV-CIVQKKDTKKMfAMKYMNK---------------------QKCIEkdsVRNVLNELE------ 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 gFLIVMERPYPC---------IDMF---DFIKG---------QGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENI 164
Cdd:cd05578  53 -ILQELEHPFLVnlwysfqdeEDMYmvvDLLLGgdlryhlqqKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNI 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 165 VIDlVTGSTKLIDFGAATVLRRSQYSD-FQGTRLYCPPEWFLHSLYlgrEAAV--WSLGVLLYNSLNGRLPFRN-----E 236
Cdd:cd05578 132 LLD-EQGHVHITDFNIATKLTDGTLATsTSGTKPYMAPEVFMRAGY---SFAVdwWSLGVTAYEMLRGKRPYEIhsrtsI 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 25143934 237 KDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQR-CSLEAILNHPW 284
Cdd:cd05578 208 EEIRAKFETASVLYPAGWSEEAIDLINKLLERDPQKRlGDLSDLKNHPY 256
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
30-284 2.28e-21

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 93.54  E-value: 2.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVK-FIERSNVKEWARIngeqVPMEICMLaKCSKVRGVIRLLDWYSIPEGFL 108
Cdd:cd07833   2 KYEVLGVVGEGAYGVVLKCRNKATGEIVAIKkFKESEDDEDVKKT----ALREVKVL-RQLRHENIVNLKEAFRRKGRLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMErpYPCIDMFDFIKGQ-GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLR-- 185
Cdd:cd07833  77 LVFE--YVERTLLELLEASpGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSE-SGVLKLCDFGFARALTar 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 -RSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHL----LGPLP----------- 249
Cdd:cd07833 154 pASPLTDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLiqkcLGPLPpshqelfssnp 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 25143934 250 -------------------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07833 234 rfagvafpepsqpeslerrYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
25-281 2.45e-21

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: 93.13  E-value: 2.45e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  25 SKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEWARingEQVPMEICMLAKCSKVrGVIRLLDWYSIP 104
Cdd:cd13996   2 SRYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKI-RLTEKSSAS---EKVLREVKALAKLNHP-NIVRYYTAWVEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVME--RPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTV---HEcvqNRVLHRDLKDENIVIDLVTGSTKLIDFG 179
Cdd:cd13996  77 PPLYIQMElcEGGTLRDWIDRRNSSSKNDRKLALELFKQILKGVsyiHS---KGIVHRDLKPSNIFLDNDDLQVKIGDFG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVL----------------RRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH 243
Cdd:cd13996 154 LATSIgnqkrelnnlnnnnngNTSNNSVGIGTPLYASPEQLDGENY-NEKADIYSLGIILFEMLHPFKTAMERSTILTDL 232
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 25143934 244 LLGPLP-FFVPVSAEVKDLISKCLTFDPFQRCSLEAILN 281
Cdd:cd13996 233 RNGILPeSFKAKHPKEADLIQSLLSKNPEERPSAEQLLR 271
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
31-284 2.58e-21

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: 92.65  E-value: 2.58e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIE-RSNVKEWARingeqvpMEICMLAKCSKVRgVIRLLDWYSIPEGFLI 109
Cdd:cd14107   4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPlRSSTRARAF-------QERDILARLSHRR-LTCLLDQFETRKTLIL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpypCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVT-GSTKLIDFGAATVLR- 185
Cdd:cd14107  76 ILEL---CSseELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTrEDIKICDFGFAQEITp 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 -RSQYSDFqGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICT------AHLLGPLPFFVPVSAEV 258
Cdd:cd14107 153 sEHQFSKY-GSPEFVAPE-IVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATllnvaeGVVSWDTPEITHLSEDA 230
                       250       260
                ....*....|....*....|....*.
gi 25143934 259 KDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14107 231 KDFIKRVLQPDPEKRPSASECLSHEW 256
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
30-281 2.87e-21

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: 92.78  E-value: 2.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKfieRSNVKEWARINgeQVPMEICMLAKCSKVRGVIRLLD---WYSIPE- 105
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALK---RMYFNDEEQLR--VAIKEIEIMKRLCGHPNIVQYYDsaiLSSEGRk 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMErpYPCIDMFDFIK--GQGKISEDMARFLFRQI--AVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA 181
Cdd:cd13985  76 EVLLLME--YCPGSLVDILEksPPSPLSEEEVLRIFYQIcqAVGHLHSQSPPIIHRDIKIENILFS-NTGRFKLCDFGSA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQYS--DFQ---------GTRLYCPPE-WFLHSLY-LGREAAVWSLGVLLYNSLNGRLPFRNEK--DICTAHLlg 246
Cdd:cd13985 153 TTEHYPLERaeEVNiieeeiqknTTPMYRAPEmIDLYSKKpIGEKADIWALGCLLYKLCFFKLPFDESSklAIVAGKY-- 230
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 247 PLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILN 281
Cdd:cd13985 231 SIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
31-287 3.19e-21

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: 92.69  E-value: 3.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERsnvkEWARINGEQVPMEICMLAKC----------SKVRGViRLldW 100
Cdd:cd06609   3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDL----EEAEDEIEDIQQEIQFLSQCdspyitkyygSFLKGS-KL--W 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 101 ysipegflIVMErpYpcID---MFDFIKgQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLID 177
Cdd:cd06609  76 --------IIME--Y--CGggsVLDLLK-PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLS-EEGDVKLAD 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 178 FGAATVLRRSQ--YSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFrnekdiCTAHLLGPLpFFVP-- 253
Cdd:cd06609 142 FGVSGQLTSTMskRNTFVGTPFWMAPEVIKQSGY-DEKADIWSLGITAIELAKGEPPL------SDLHPMRVL-FLIPkn 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 25143934 254 ---------VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06609 214 nppslegnkFSKPFKDFVELCLNKDPKERPSAKELLKHKFIKK 256
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
31-285 3.21e-21

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: 93.11  E-value: 3.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERsnvKEWARING------------------------EQVPMEICMLA 86
Cdd:cd14199   4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSK---KKLMRQAGfprrppprgaraapegctqprgpiERVYQEIAILK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  87 KCSKvRGVIRLLDWYSIPEGFLIVMerpypcidMFDFIKgQGKI---------SEDMARFLFRQIAVTVHECVQNRVLHR 157
Cdd:cd14199  81 KLDH-PNVVKLVEVLDDPSEDHLYM--------VFELVK-QGPVmevptlkplSEDQARFYFQDLIKGIEYLHYQKIIHR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 158 DLKDENIVIDlVTGSTKLIDFGAATVLRRSQ--YSDFQGTRLYCPPEWFLHS--LYLGREAAVWSLGVLLYNSLNGRLPF 233
Cdd:cd14199 151 DVKPSNLLVG-EDGHIKIADFGVSNEFEGSDalLTNTVGTPAFMAPETLSETrkIFSGKALDVWAMGVTLYCFVFGQCPF 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 234 RNEKDICTAHLLGPLPFFVP----VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14199 230 MDERILSLHSKIKTQPLEFPdqpdISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
31-284 3.27e-21

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: 93.01  E-value: 3.27e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarinGEQVPM--EICMLAKCSKvRGVIRLLDwysipegfl 108
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKE-----GFPITAirEIKLLQKLDH-PNVVRLKE--------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERPYPC----IDM-FDFI---------KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTK 174
Cdd:cd07840  66 IVTSKGSAKykgsIYMvFEYMdhdltglldNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILIN-NDGVLK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 175 LIDFGAATVLRRSQYSDFQG---TRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDI----CTAHLLGP 247
Cdd:cd07840 145 LADFGLARPYTKENNADYTNrviTLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELeqleKIFELCGS 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 248 -----------LPFFVPV------------------SAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07840 225 pteenwpgvsdLPWFENLkpkkpykrrlrevfknviDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
31-285 3.60e-21

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: 93.09  E-value: 3.60e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNV-KEWA-----------RINGEQ---------VPMEICMLAKCS 89
Cdd:cd14200   2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlKQYGfprrppprgskAAQGEQakplaplerVYQEIAILKKLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  90 KVrGVIRLLDWYSIP--EGFLIVME--RPYPCIDmfdfIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIV 165
Cdd:cd14200  82 HV-NIVKLIEVLDDPaeDNLYMVFDllRKGPVME----VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 166 IDlVTGSTKLIDFGAATVLR--RSQYSDFQGTRLYCPPEWFLHS--LYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICT 241
Cdd:cd14200 157 LG-DDGHVKIADFGVSNQFEgnDALLSSTAGTPAFMAPETLSDSgqSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILAL 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 25143934 242 AHLLGPLPFFVP----VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14200 236 HNKIKNKPVEFPeepeISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
18-286 3.74e-21

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: 92.30  E-value: 3.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  18 GESSRGFSKFKKnyklkaeLGRGGFGVVYRAVRTCDNALVAVKfieRSNVKEWARinGEQVPMEIcMLAKCSKVRGVIRL 97
Cdd:cd06647   3 GDPKKKYTRFEK-------IGQGASGTVYTAIDVATGQEVAIK---QMNLQQQPK--KELIINEI-LVMRENKNPNIVNY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  98 LDWYSIPEGFLIVMErpypcidmfdFIKGqGKISEDMARFLFR--QIAVTVHECVQ-------NRVLHRDLKDENIVIDL 168
Cdd:cd06647  70 LDSYLVGDELWVVME----------YLAG-GSLTDVVTETCMDegQIAAVCRECLQaleflhsNQVIHRDIKSDNILLGM 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 169 vTGSTKLIDFG--AATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLG 246
Cdd:cd06647 139 -DGSVKLTDFGfcAQITPEQSKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 25143934 247 P-----LPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06647 217 TngtpeLQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
29-283 4.68e-21

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 91.90  E-value: 4.68e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCD-------NALVAVKFIERSNVKewARINGEQVPMEIcmLAKCSKVRGVIrlldwY 101
Cdd:cd14019   1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSP--SRILNELECLER--LGGSNNVSGLI-----T 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 102 SIPEGFLIVMERPY-PCIDMFDFIKgqgKIS-EDMARF---LFRQIAvTVHecvQNRVLHRDLKDENIVIDLVTGSTKLI 176
Cdd:cd14019  72 AFRNEDQVVAVLPYiEHDDFRDFYR---KMSlTDIRIYlrnLFKALK-HVH---SFGIIHRDVKPGNFLYNRETGKGVLV 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAATVL--RRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTA-----HLLGplp 249
Cdd:cd14019 145 DFGLAQREedRPEQRAPRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRFPFFFSSDDIDAlaeiaTIFG--- 221
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 250 ffvpvSAEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd14019 222 -----SDEAYDLLDKLLELDPSKRITAEEALKHP 250
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
28-286 4.70e-21

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: 92.86  E-value: 4.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKfieRSNVKEWARinGEQVPMEICMLAKcSKVRGVIRLLDWYSIPEGF 107
Cdd:cd06656  18 KKKYTRFEKIGQGASGTVYTAIDIATGQEVAIK---QMNLQQQPK--KELIINEILVMRE-NKNPNIVNYLDSYLVGDEL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMErpypcidmfdFIKGqGKISEDMARFLFR--QIAVTVHECVQ-------NRVLHRDLKDENIVIDLvTGSTKLIDF 178
Cdd:cd06656  92 WVVME----------YLAG-GSLTDVVTETCMDegQIAAVCRECLQaldflhsNQVIHRDIKSDNILLGM-DGSVKLTDF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 G--AATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL---GPLPFFVP 253
Cdd:cd06656 160 GfcAQITPEQSKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIatnGTPELQNP 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 254 --VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06656 239 erLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 273
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
29-285 4.98e-21

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 92.23  E-value: 4.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLaKCSKVRGVIRLLDWYSIPEGFL 108
Cdd:cd14097   1 KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAV---KLLEREVDIL-KHVNHAHIIHLEEVFETPKRMY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERpypCID--MFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI--DLVTGSTKLI----DFGA 180
Cdd:cd14097  77 LVMEL---CEDgeLKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVksSIIDNNDKLNikvtDFGL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRSQYSDFQ---GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPF----F 251
Cdd:cd14097 154 SVQKYGLGEDMLQetcGTPIYMAPEVISAHGY-SQQCDIWSIGVIMYMLLCGEPPFvaKSEEKLFEEIRKGDLTFtqsvW 232
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 252 VPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14097 233 QSVSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
36-285 5.92e-21

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: 92.04  E-value: 5.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFI----------------ERSNVKEWARING--EQVPMEICMLAKCS--KVRGVI 95
Cdd:cd14118   1 EIGKGSYGIVKLAYNEEDNTLYAMKILskkkllkqagffrrppPRRKPGALGKPLDplDRVYREIAILKKLDhpNVVKLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  96 RLLD------WYSIPEgfLI----VMERPypcidmfdfikGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIV 165
Cdd:cd14118  81 EVLDdpnednLYMVFE--LVdkgaVMEVP-----------TDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 166 IDlVTGSTKLIDFGAATVLRRSQ--YSDFQGTRLYCPPEWFLHS--LYLGREAAVWSLGVLLYNSLNGRLPFRNE----- 236
Cdd:cd14118 148 LG-DDGHVKIADFGVSNEFEGDDalLSSTAGTPAFMAPEALSESrkKFSGKALDIWAMGVTLYCFVFGRCPFEDDhilgl 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 25143934 237 -KDICTAHLLGPLPFFVpvSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14118 227 hEKIKTDPVVFPDDPVV--SEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
31-285 6.23e-21

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: 91.83  E-value: 6.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSnvkewaRINGEQVPMEICMLakcSKVR--GVIRLLDWYSIPEGFL 108
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETK------CRGREVCESELNVL---RRVRhtNIIQLIEVFETKERVY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLI--DFGAATVLRR 186
Cdd:cd14087  74 MVMELATGG-ELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMitDFGLASTRKK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQ---GTRLYCPPEWFLHSLYLgREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLLGPLPFFVPVSAE 257
Cdd:cd14087 153 GPNCLMKttcGTPEYIAPEILLRKPYT-QSVDMWAVGVIAYILLSGTMPFDDDnrtrlyRQILRAKYSYSGEPWPSVSNL 231
                       250       260
                ....*....|....*....|....*...
gi 25143934 258 VKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14087 232 AKDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
37-286 1.09e-20

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: 91.46  E-value: 1.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNV-KEWARingEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMERPy 115
Cdd:cd14117  14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIeKEGVE---HQLRREIEIQSHLRH-PNILRLYNYFHDRKRIYLILEYA- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFG---AATVLRRSQYSdf 192
Cdd:cd14117  89 PRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGY-KGELKIADFGwsvHAPSLRRRTMC-- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 193 qGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPL----PFFVPVSAevKDLISKCLTF 268
Cdd:cd14117 166 -GTLDYLPPEMIEGRTH-DEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVdlkfPPFLSDGS--RDLISKLLRY 241
                       250
                ....*....|....*...
gi 25143934 269 DPFQRCSLEAILNHPWVK 286
Cdd:cd14117 242 HPSERLPLKGVMEHPWVK 259
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
31-285 1.11e-20

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: 91.71  E-value: 1.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAE-LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingeqVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14090   3 YKLTGElLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSR-----VFREVETLHQCQGHPNILQLIEYFEDDERFYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPY--PcidMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIV---IDLVTgSTKLIDFGAATVL 184
Cdd:cd14090  78 VFEKMRggP---LLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVS-PVKICDFDLGSGI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYS-------DFQ---GTRLYCPPE----WFLHSLYLGREAAVWSLGVLLYNSLNGRLPF-----------RNEK-D 238
Cdd:cd14090 154 KLSSTSmtpvttpELLtpvGSAEYMAPEvvdaFVGEALSYDKRCDLWSLGVILYIMLCGYPPFygrcgedcgwdRGEAcQ 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 239 ICTAHLL-----GPLPF----FVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14090 234 DCQELLFhsiqeGEYEFpekeWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
22-285 3.53e-20

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: 91.24  E-value: 3.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  22 RGFSKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewaRINGEqvpmEICMLAKCSKVRGVIRLLDWY 101
Cdd:cd14176  12 RNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-----RDPTE----EIEILLRYGQHPNIITLKDVY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 102 SIPEGFLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTG---STKLIDF 178
Cdd:cd14176  83 DDGKYVYVVTEL-MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpeSIRICDF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 GAATVLRRSQ-------YsdfqgTRLYCPPEWFLHSlylGREAA--VWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLP 249
Cdd:cd14176 162 GFAKQLRAENgllmtpcY-----TANFVAPEVLERQ---GYDAAcdIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIG 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 25143934 250 ---------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14176 234 sgkfslsggYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
28-286 3.92e-20

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 92.62  E-value: 3.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwARINGEQVpmEICMLAKCskvrgvirllDWYSI---- 103
Cdd:PTZ00283  31 AKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSE-ADKNRAQA--EVCCLLNC----------DFFSIvkch 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  104 ----------PEGFLIV-MERPYPCI-DMFDFIKGQGKIS----EDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVId 167
Cdd:PTZ00283  98 edfakkdprnPENVLMIaLVLDYANAgDLRQEIKSRAKTNrtfrEHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILL- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  168 LVTGSTKLIDFG-----AATVlrrsqySD-----FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE- 236
Cdd:PTZ00283 177 CSNGLVKLGDFGfskmyAATV------SDdvgrtFCGTPYYVAPEIWRRKPY-SKKADMFSLGVLLYELLTLKRPFDGEn 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 25143934  237 -KDICTAHLLG---PLPffVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:PTZ00283 250 mEEVMHKTLAGrydPLP--PSISPEMQEIVTALLSSDPKRRPSSSKLLNMPICK 301
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
28-234 4.20e-20

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: 89.68  E-value: 4.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAV-RTCDNALVAVKFIERSNVKEWARINGEQVPmeicmLAKCSKVRGVIRLLDWYSIPEG 106
Cdd:cd14202   1 KFEFSRKDLIGHGAFAVVFKGRhKEKHDLEVAVKCINKKNLAKSQTLLGKEIK-----ILKELKHENIVALYDFQEIANS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERpypCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGS--------TKLI 176
Cdd:cd14202  76 VYLVMEY---CNggDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGRksnpnnirIKIA 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 177 DFGAATVLRRSQY-SDFQGTRLYCPPEWFLHSLYLGReAAVWSLGVLLYNSLNGRLPFR 234
Cdd:cd14202 153 DFGFARYLQNNMMaATLCGSPMYMAPEVIMSQHYDAK-ADLWSIGTIIYQCLTGKAPFQ 210
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
31-285 4.77e-20

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: 90.30  E-value: 4.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARingeQVPMEICMLAKCSK-----VRGVIRLLDWYSIPE 105
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIR--NKKRFHQ----QALVEVKILKHLNDndpddKHNIVRYKDSFIFRG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMErpYPCIDMFDFIKGQG--KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST-KLIDFGAAT 182
Cdd:cd14210  89 HLCIVFE--LLSINLYELLKSNNfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSiKVIDFGSSC 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRSQYSDFQgTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGR--LPFRNEKDI--CTAHLLGPLP--------- 249
Cdd:cd14210 167 FEGEKVYTYIQ-SRFYRAPEVILGLPY-DTAIDMWSLGCILAELYTGYplFPGENEEEQlaCIMEVLGVPPkslidkasr 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 250 ---FF--------VPVSAEVK--------------------DLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14210 245 rkkFFdsngkprpTTNSKGKKrrpgskslaqvlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
31-287 7.18e-20

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: 89.89  E-value: 7.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSnvkEWARINGEQVPMEICMLaKCSKVRGVIRLLDWYSIPEG---- 106
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNV---FDDLIDAKRILREIKIL-RHLKHENIIGLLDILRPPSPeefn 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 -FLIVMErpYPCIDMFDFIKGQGKISEDMARFLFRQIAVT---VHECvqnRVLHRDLKDENIVI----DLvtgstKLIDF 178
Cdd:cd07834  78 dVYIVTE--LMETDLHKVIKSPQPLTDDHIQYFLYQILRGlkyLHSA---GVIHRDLKPSNILVnsncDL-----KICDF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 GaatvLRRSQYSDFQG--------TRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR--LPFRNEKD----ICtaHL 244
Cdd:cd07834 148 G----LARGVDPDEDKgflteyvvTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKplFPGRDYIDqlnlIV--EV 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143934 245 LG----------------------------PLPFFVPV-SAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd07834 222 LGtpseedlkfissekarnylkslpkkpkkPLSEVFPGaSPEAIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
30-301 7.98e-20

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: 89.42  E-value: 7.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersNVKEWARINGEQ-VPMEICMLAKCSKVRgVIRLLdWYSIPEGFL 108
Cdd:cd05612   2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVM---AIPEVIRLKQEQhVHNEKRVLKEVSHPF-IIRLF-WTEHDQRFL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQ 188
Cdd:cd05612  77 YMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLD-KEGHIKLTDFGFAKKLRDRT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSdFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK--DICTAHLLGPLPFFVPVSAEVKDLISKCL 266
Cdd:cd05612 156 WT-LCGTPEYLAPE-VIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNpfGIYEKILAGKLEFPRHLDLYAKDLIKKLL 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 25143934 267 TFDPFQRC-----SLEAILNHPWVKqqTLSWDALTKNKVQ 301
Cdd:cd05612 234 VVDRTRRLgnmknGADDVKNHRWFK--SVDWDDVPQRKLK 271
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
31-285 8.62e-20

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: 88.48  E-value: 8.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsnvkewarINGEQVPM--EICMLAKCsKVRGVIRLLDWYSIPEGFL 108
Cdd:cd06612   5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVP---------VEEDLQEIikEISILKQC-DSPYIVKYYGSYFKNTDLW 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMErpYpC-----IDMfdfIKGQGK-ISEDmarflfrQIAVTVHECVQ-------NRVLHRDLKDENIVIDlVTGSTKL 175
Cdd:cd06612  75 IVME--Y-CgagsvSDI---MKITNKtLTEE-------EIAAILYQTLKgleylhsNKKIHRDIKAGNILLN-EEGQAKL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 176 IDFGAATVL--RRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLP---F 250
Cdd:cd06612 141 ADFGVSGQLtdTMAKRNTVIGTPFWMAPEVIQEIGY-NNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPpptL 219
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 25143934 251 FVP--VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06612 220 SDPekWSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
28-286 9.12e-20

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: 89.40  E-value: 9.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersNVKEWARinGEQVPMEIcMLAKCSKVRGVIRLLDWYSIPEGF 107
Cdd:cd06655  18 KKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQI---NLQKQPK--KELIINEI-LVMKELKNPNIVNFLDSFLVGDEL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMErpypcidmfdFIKGqGKISEDMARFLF--RQIAVTVHECVQ-------NRVLHRDLKDENIVIDLvTGSTKLIDF 178
Cdd:cd06655  92 FVVME----------YLAG-GSLTDVVTETCMdeAQIAAVCRECLQaleflhaNQVIHRDIKSDNVLLGM-DGSVKLTDF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 G--AATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL---GPLPFFVP 253
Cdd:cd06655 160 GfcAQITPEQSKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIatnGTPELQNP 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 254 --VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06655 239 ekLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
28-286 1.13e-19

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: 89.01  E-value: 1.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKfieRSNVKEWARinGEQVPMEICMLAKcSKVRGVIRLLDWYSIPEGF 107
Cdd:cd06654  19 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIR---QMNLQQQPK--KELIINEILVMRE-NKNPNIVNYLDSYLVGDEL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMErpypcidmfdFIKGqGKISEDMARFLFR--QIAVTVHECVQ-------NRVLHRDLKDENIVIDLvTGSTKLIDF 178
Cdd:cd06654  93 WVVME----------YLAG-GSLTDVVTETCMDegQIAAVCRECLQaleflhsNQVIHRDIKSDNILLGM-DGSVKLTDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 G--AATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL---GPLPFFVP 253
Cdd:cd06654 161 GfcAQITPEQSKRSTMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIatnGTPELQNP 239
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 254 --VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06654 240 ekLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 274
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
31-285 1.43e-19

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: 88.49  E-value: 1.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersnvkewaRI-NGEQ-VPM----EICMLAKCSKVR--GVIRLLDWYS 102
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV---------RVpLSEEgIPLstirEIALLKQLESFEhpNVVRLLDVCH 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 103 IPEG-----FLIVMErpYPCIDMFDFIKGQGK--ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVT--GST 173
Cdd:cd07838  72 GPRTdrelkLTLVFE--HVDQDLATYLDKCPKpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNI---LVTsdGQV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 174 KLIDFGAATVL-RRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH----LLG-- 246
Cdd:cd07838 147 KLADFGLARIYsFEMALTSVVVTLWYRAPEVLLQSSY-ATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGkifdVIGlp 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143934 247 --------------------PLPF--FVP-VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd07838 226 seeewprnsalprssfpsytPRPFksFVPeIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
30-283 1.48e-19

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: 87.87  E-value: 1.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFI--ERSNVKEwaringEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGF 107
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpvEQMTKEE------RQAALNEVKVLSMLHHPNIIEYYESFLEDKAL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERPyPCIDMFDFIKGQGK--ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLR 185
Cdd:cd08220  75 MIVMEYA-PGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVKIGDFGISKILS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 -RSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYN--SLNGRLPFRNEKDICTAHLLGPL-PFFVPVSAEVKDL 261
Cdd:cd08220 154 sKSKAYTVVGTPCYISPELCEGKPY-NQKSDIWALGCVLYElaSLKRAFEAANLPALVLKIMRGTFaPISDRYSEELRHL 232
                       250       260
                ....*....|....*....|..
gi 25143934 262 ISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd08220 233 ILSMLHLDPNKRPTLSEIMAQP 254
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
22-284 2.15e-19

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: 88.53  E-value: 2.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  22 RGFSKFKkNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQvpmEICMLaKCSKVRGVIRLLDW- 100
Cdd:cd07866   2 YGCSKLR-DYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPITALR---EIKIL-KKLKHPNVVPLIDMa 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 101 YSIPEGFL-----IVMERPYPCIDMFDFIKGQG-KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTK 174
Cdd:cd07866  77 VERPDKSKrkrgsVYMVTPYMDHDLSGLLENPSvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILID-NQGILK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 175 LIDFGAATVLR-------------RSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICT 241
Cdd:cd07866 156 IADFGLARPYDgpppnpkggggggTRKYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQ 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 242 AH----LLGP-----------LP-----------------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07866 236 LHlifkLCGTpteetwpgwrsLPgcegvhsftnyprtleeRFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
31-285 2.75e-19

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: 86.87  E-value: 2.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewaRINGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIV 110
Cdd:cd14114   4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPH-----ESDKETVRKEIQIMNQLHHPK-LINLHDAFEDDNEMVLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFIKGQG-KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST-KLIDFGAATVLRRSQ 188
Cdd:cd14114  78 LEF-LSGGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEvKLIDFGLATHLDPKE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSDFQ-GTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGP------LPFFVPVSAEVKDL 261
Cdd:cd14114 157 SVKVTtGTAEFAAPE-IVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKScdwnfdDSAFSGISEEAKDF 235
                       250       260
                ....*....|....*....|....
gi 25143934 262 ISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14114 236 IRKLLLADPNKRMTIHQALEHPWL 259
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
109-284 3.63e-19

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 86.24  E-value: 3.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERPYPciDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI-DLVTGSTKLIDFGAATVLR-- 185
Cdd:cd14022  62 VFFERSYG--DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFkDEERTRVKLESLEDAYILRgh 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQGTRLYCPPEWFLHS-LYLGREAAVWSLGVLLYNSLNGRLPFRnekDICTAHLLGPL---PFFVP--VSAEVK 259
Cdd:cd14022 140 DDSLSDKHGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFH---DIEPSSLFSKIrrgQFNIPetLSPKAK 216
                       170       180
                ....*....|....*....|....*
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14022 217 CLIRSILRREPSERLTSQEILDHPW 241
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
34-285 3.92e-19

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: 86.67  E-value: 3.92e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  34 KAEL-GRGGFGVVYRAVRTCDNALVAVKFIERSnvkewARINGEQVPMEICMLAKCSKVRGVIRLLDWYSI--------- 103
Cdd:cd06629   5 KGELiGKGTYGRVYLAMNATTGEMLAVKQVELP-----KTSSDRADSRQKTVVDALKSEIDTLKDLDHPNIvqylgfeet 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 PEGFLIVMErpY-------PCIDMFdfikgqGKISEDMARFLFRQIA---VTVHEcvqNRVLHRDLKDENIVIDLvTGST 173
Cdd:cd06629  80 EDYFSIFLE--YvpggsigSCLRKY------GKFEEDLVRFFTRQILdglAYLHS---KGILHRDLKADNILVDL-EGIC 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 174 KLIDFGAAtvlRRSQ--YSDF-----QGTRLYCPPEwFLHSLYLGREAAV--WSLGVLLYNSLNGRLPFRNEKDICTAHL 244
Cdd:cd06629 148 KISDFGIS---KKSDdiYGNNgatsmQGSVFWMAPE-VIHSQGQGYSAKVdiWSLGCVVLEMLAGRRPWSDDEAIAAMFK 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 25143934 245 LG------PLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06629 224 LGnkrsapPVPEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
30-283 3.97e-19

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: 87.60  E-value: 3.97e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWaRINgeqvpMEICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14132  19 DYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLK--PVKKK-KIK-----REIKILQNLRGGPNIVKLLDVVKDPQSKTP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYpcIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRRSQ- 188
Cdd:cd14132  91 SLIFEY--VNNTDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRKLRLIDWGLAEFYHPGQe 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDI-----CTAHLLG----------------- 246
Cdd:cd14132 169 YNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvKIAKVLGtddlyayldkygielpp 248
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 247 ------------PLPFFVP------VSAEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd14132 249 rlndilgrhskkPWERFVNsenqhlVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
25-335 1.02e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 86.80  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   25 SKFK-KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNV---KEWARINGE-QVPMEICMLAKCSKVRGVIRLLD 99
Cdd:PTZ00263  13 SSWKlSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREIlkmKQVQHVAQEkSILMELSHPFIVNMMCSFQDENR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  100 WYSIPEgFLIVMErpypcidMFDFIKGQGKISEDMARFLFRQIAVT---VHECvqnRVLHRDLKDENIVIDlVTGSTKLI 176
Cdd:PTZ00263  93 VYFLLE-FVVGGE-------LFTHLRKAGRFPNDVAKFYHAELVLAfeyLHSK---DIIYRDLKPENLLLD-NKGHVKVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  177 DFGAATVLRRSQYSdFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH--LLGPLPFFVPV 254
Cdd:PTZ00263 161 DFGFAKKVPDRTFT-LCGTPEYLAPE-VIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEkiLAGRLKFPNWF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  255 SAEVKDLISKCLTFDPFQRC-----SLEAILNHPWVKQqtLSWDALTKNKVQK----KTSESSDDHHSETlgdHSETEED 325
Cdd:PTZ00263 239 DGRARDLVKGLLQTDHTKRLgtlkgGVADVKNHPYFHG--ANWDKLYARYYPApipvRVKSPGDTSNFEK---YPDSPVD 313
                        330
                 ....*....|
gi 25143934  326 RSPPTSSVSQ 335
Cdd:PTZ00263 314 RLPPLTAAQQ 323
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
37-310 1.18e-18

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: 86.30  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTC---DNALVAVKFIER----SNVKEWARINGEQVPME------ICMLAKCSKVRGVIRL-LDWYS 102
Cdd:cd05584   4 LGKGGYGKVFQVRKTTgsdKGKIFAMKVLKKasivRNQKDTAHTKAERNILEavkhpfIVDLHYAFQTGGKLYLiLEYLS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 103 IPEGFLIvMERpypcidmfdfikgQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA- 181
Cdd:cd05584  84 GGELFMH-LER-------------EGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLD-AQGHVKLTDFGLCk 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 -TVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPVSAEV 258
Cdd:cd05584 149 eSIHDGTVTHTFCGTIEYMAPEILTRSGH-GKAVDWWSLGALMYDMLTGAPPFtaENRKKTIDKILKGKLNLPPYLTNEA 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 259 KDLISKCLTFDPFQRC-----SLEAILNHPWVKqqTLSWDALTKNKVQ---KKTSESSDD 310
Cdd:cd05584 228 RDLLKKLLKRNVSSRLgsgpgDAEEIKAHPFFR--HINWDDLLAKKVEppfKPLLQSEED 285
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
26-300 1.39e-18

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: 85.84  E-value: 1.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  26 KFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewaRINGEqvpmEICMLAKCSKVRGVIRLLDWYSipE 105
Cdd:cd14177   1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSK-----RDPSE----EIEILMRYGQHPNIITLKDVYD--D 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 G-FLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTG---STKLIDFGAA 181
Cdd:cd14177  70 GrYVYLVTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSAnadSIRICDFGFA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQ-------YsdfqgTRLYCPPEWFLHSlylGREAA--VWSLGVLLYNSLNGRLPFRNEKDICTAHLL---GPLP 249
Cdd:cd14177 150 KQLRGENgllltpcY-----TANFVAPEVLMRQ---GYDAAcdIWSLGVLLYTMLAGYTPFANGPNDTPEEILlriGSGK 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 250 FFVP------VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK-QQTLSWDALTKNKV 300
Cdd:cd14177 222 FSLSggnwdtVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWIAcRDQLPHYQLNRQDA 279
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
28-298 1.43e-18

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: 85.87  E-value: 1.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwariNGEQVPMEICMLAKCsKVRGVIRLLDWYSIPEGF 107
Cdd:cd14168   9 KKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKG----KESSIENEIAVLRKI-KHENIVALEDIYESPNHL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLI--DFGAATVLR 185
Cdd:cd14168  84 YLVMQL-VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMisDFGLSKMEG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQ-YSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD------ICTAHLLGPLPFFVPVSAEV 258
Cdd:cd14168 163 KGDvMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDsklfeqILKADYEFDSPYWDDISDSA 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 25143934 259 KDLISKCLTFDPFQRCSLEAILNHPWVKQQTlswdALTKN 298
Cdd:cd14168 242 KDFIRNLMEKDPNKRYTCEQALRHPWIAGDT----ALCKN 277
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
30-285 1.60e-18

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: 84.71  E-value: 1.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLI 109
Cdd:cd06625   1 NWKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKALECEIQLLKNLQHER-IVQYYGCLQDEKSLSI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLR--R 186
Cdd:cd06625  80 FME--YmPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDS-NGNVKLGDFGASKRLQtiC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQ--YSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEK------DICTAHLLGPLPffVPVSAEV 258
Cdd:cd06625 157 SStgMKSVTGTPYWMSPEVINGEGY-GRKADIWSVGCTVVEMLTTKPPWAEFEpmaaifKIATQPTNPQLP--PHVSEDA 233
                       250       260
                ....*....|....*....|....*..
gi 25143934 259 KDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06625 234 RDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
29-310 1.66e-18

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: 86.21  E-value: 1.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVkeWARINGEQVPMEICMLAKcSKVRGVIRLLDWYSIPEGFL 108
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSET--LAQEEVSFFEEERDIMAK-ANSPWITKLQYAFQDSENLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERpYPCIDMFDFIKGQGKI-SEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS 187
Cdd:cd05601  78 LVMEY-HPGGDLLSLLSRYDDIfEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILID-RTGHIKLADFGSAAKLSSD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 QYSDFQ---GTRLYCPPEwFLHSL------YLGREAAVWSLGVLLYNSLNGRLPFRNEKDICT-AHLLGPLPFF-----V 252
Cdd:cd05601 156 KTVTSKmpvGTPDYIAPE-VLTSMnggskgTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTySNIMNFKKFLkfpedP 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 253 PVSAEVKDLISKCLTfDPFQRCSLEAILNHPWVKQqtLSWDALtKNKVQK--KTSESSDD 310
Cdd:cd05601 235 KVSESAVDLIKGLLT-DAKERLGYEGLCCHPFFSG--IDWNNL-RQTVPPfvPTLTSDDD 290
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
28-285 1.68e-18

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: 85.08  E-value: 1.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewarinGEQVPME--ICMLAKCsKVRGVIRLLDWYSIPE 105
Cdd:cd14167   2 RDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALE------GKETSIEneIAVLHKI-KHPNIVALDDIYESGG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLI--DFGAATV 183
Cdd:cd14167  75 HLYLIMQL-VSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMisDFGLSKI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRR-SQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD------ICTAHLLGPLPFFVPVSA 256
Cdd:cd14167 154 EGSgSVMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDaklfeqILKAEYEFDSPYWDDISD 232
                       250       260
                ....*....|....*....|....*....
gi 25143934 257 EVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14167 233 SAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
31-286 1.76e-18

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: 85.06  E-value: 1.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAV-RTCDNALVAVKFIERSNVKEWARINGEQVPmeicmLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14201   8 YSRKDLVGHGAFAVVFKGRhRKKTDWEVAIKSINKKNLSKSQILLGKEIK-----ILKELQHENIVALYDVQEMPNSVFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpypCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDL-------VTG-STKLIDFG 179
Cdd:cd14201  83 VMEY---CNggDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYasrkkssVSGiRIKIADFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVLRRSQY-SDFQGTRLYCPPEWFLHSLYLGReAAVWSLGVLLYNSLNGRLPFR--NEKDI-----CTAHLLGPLPff 251
Cdd:cd14201 160 FARYLQSNMMaATLCGSPMYMAPEVIMSQHYDAK-ADLWSIGTVIYQCLVGKPPFQanSPQDLrmfyeKNKNLQPSIP-- 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 252 VPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd14201 237 RETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
27-286 1.90e-18

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: 85.48  E-value: 1.90e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAE---LGRGGFGVVYRAVRTCDNALVAVKFIERsnvkewaRINGeQVPMEICMLAKCSKVRGVIRLLDWYSI 103
Cdd:cd14179   2 FYQHYELDLKdkpLGEGSFSICRKCLHKKTNQEYAVKIVSK-------RMEA-NTQREIAALKLCEGHPNIVKLHEVYHD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 PEGFLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST--KLIDFGAA 181
Cdd:cd14179  74 QLHTFLVMEL-LKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSeiKIIDFGFA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 tvlrRSQYSDFQG------TRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFR-NEKDI-CTAHL-------LG 246
Cdd:cd14179 153 ----RLKPPDNQPlktpcfTLHYAAPELLNYNGY-DESCDLWSLGVILYTMLSGQVPFQcHDKSLtCTSAEeimkkikQG 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 25143934 247 PLPF----FVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd14179 228 DFSFegeaWKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQ 271
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
37-285 1.94e-18

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: 84.80  E-value: 1.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVrTCDNALVAVKFIE-RSNVKEWARINGEQVPMEICMLaKCSKVRGVIRLLDwYSIPEGFL-IVMErp 114
Cdd:cd06631   9 LGKGAYGTVYCGL-TSTGQLIAVKQVElDTSDKEKAEKEYEKLQEEVDLL-KTLKHVNIVGYLG-TCLEDNVVsIFME-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 115 ypcidmfdFIKGqGKISEDMARF------LF----RQIAVTVHECVQNRVLHRDLKDENIVIdLVTGSTKLIDFGAAT-- 182
Cdd:cd06631  84 --------FVPG-GSIASILARFgaleepVFcrytKQILEGVAYLHNNNVIHRDIKGNNIML-MPNGVIKLIDFGCAKrl 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 --VLRRSQYSDF----QGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVP--- 253
Cdd:cd06631 154 ciNLSSGSQSQLlksmRGTPYWMAPEVINETGH-GRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPrlp 232
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 254 --VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06631 233 dkFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
37-301 2.11e-18

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: 85.73  E-value: 2.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVK------FIERSNVkEWARingeqvpMEICMLAKCSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd05570   3 LGKGSFGKVMLAERKKTDELYAIKvlkkevIIEDDDV-ECTM-------TEKRVLALANRHPFLTGLHACFQTEDRLYFV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MErpypcidmfdFIKG---------QGKISEDMARFLFRQIAVTV---HEcvqNRVLHRDLKDENIVIDLvTGSTKLIDF 178
Cdd:cd05570  75 ME----------YVNGgdlmfhiqrARRFTEERARFYAAEICLALqflHE---RGIIYRDLKLDNVLLDA-EGHIKIADF 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 GAAT--VLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFR--NEKDICTAHLLGPLPFFVPV 254
Cdd:cd05570 141 GMCKegIWGGNTTSTFCGTPDYIAPEILREQDY-GFSVDWWALGVLLYEMLAGQSPFEgdDEDELFEAILNDEVLYPRWL 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 25143934 255 SAEVKDLISKCLTFDPFQR--CSL---EAILNHPWVKqqTLSWDALTKNKVQ 301
Cdd:cd05570 220 SREAVSILKGLLTKDPARRlgCGPkgeADIKAHPFFR--NIDWDKLEKKEVE 269
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
119-310 2.23e-18

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: 85.32  E-value: 2.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTVhECVQN-RVLHRDLKDENIVIDLvTGSTKLIDFGAATV-LRRSQYSD-FQGT 195
Cdd:cd05585  80 ELFHHLQREGRFDLSRARFYTAELLCAL-ECLHKfNVIYRDLKPENILLDY-TGHIALCDFGLCKLnMKDDDKTNtFCGT 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 196 RLYCPPEWFLHslyLGREAAV--WSLGVLLYNSLNGRLPFRNEK--DICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPF 271
Cdd:cd05585 158 PEYLAPELLLG---HGYTKAVdwWTLGVLLYEMLTGLPPFYDENtnEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPT 234
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 25143934 272 QRCSL---EAILNHPWVKQqtLSWDALTKNKVQ---KKTSESSDD 310
Cdd:cd05585 235 KRLGYngaQEIKNHPFFDQ--IDWKRLLMKKIQppfKPAVENAID 277
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
119-284 2.29e-18

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 84.02  E-value: 2.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIV-IDLVTGSTKLIDFGAATVLR--RSQYSDFQGT 195
Cdd:cd13976  70 DLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVfADEERTKLRLESLEDAVILEgeDDSLSDKHGC 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 196 RLYCPPEwFLHS--LYLGREAAVWSLGVLLYNSLNGRLPFrneKDICTAHLLGPL---PFFVP--VSAEVKDLISKCLTF 268
Cdd:cd13976 150 PAYVSPE-ILNSgaTYSGKAADVWSLGVILYTMLVGRYPF---HDSEPASLFAKIrrgQFAIPetLSPRARCLIRSLLRR 225
                       170
                ....*....|....*.
gi 25143934 269 DPFQRCSLEAILNHPW 284
Cdd:cd13976 226 EPSERLTAEDILLHPW 241
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
31-284 3.10e-18

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: 84.63  E-value: 3.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEWARINgeQVPmEICMLAKCSKVRGVIRLLD-WYSIPEGFL- 108
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCM-KKHFKSLEQVN--NLR-EIQALRRLSPHPNILRLIEvLFDRKTGRLa 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMErpypCIDM--FDFIKGQGK-ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGstKLIDFG-AATVL 184
Cdd:cd07831  77 LVFE----LMDMnlYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDIL--KLADFGsCRGIY 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYN--SLNGRLPFRNEKD-ICTAH-LLG-PLP---------- 249
Cdd:cd07831 151 SKPPYTEYISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEilSLFPLFPGTNELDqIAKIHdVLGtPDAevlkkfrksr 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 25143934 250 ---FFVP-------------VSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07831 231 hmnYNFPskkgtglrkllpnASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
27-285 5.02e-18

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: 83.83  E-value: 5.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKA--ELGRGGFGVVYRAVRTCDNALVAVKFIERsnvkewaRINGEQVPMEICM------LAKCSKvrGVIRLL 98
Cdd:cd14197   5 FQERYSLSPgrELGRGKFAVVRKCVEKDSGKEFAAKFMRK-------RRKGQDCRMEIIHeiavleLAQANP--WVINLH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  99 DWYSIPEGFLIVMERPYPCiDMFD--FIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI--DLVTGSTK 174
Cdd:cd14197  76 EVYETASEMILVLEYAAGG-EIFNqcVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLtsESPLGDIK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 175 LIDFGAATVLRRS-QYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFR-NEK-----DICTAHLLGP 247
Cdd:cd14197 155 IVDFGLSRILKNSeELREIMGTPEYVAPE-ILSYEPISTATDMWSIGVLAYVMLTGISPFLgDDKqetflNISQMNVSYS 233
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 25143934 248 LPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14197 234 EEEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
31-286 6.33e-18

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: 83.54  E-value: 6.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAEL-GRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingeqVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14174   3 YRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSR-----VFREVETLYQCQGNKNILELIEFFEDDTRFYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLV--TGSTKLIDF--------- 178
Cdd:cd14174  78 VFEKLRGG-SILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPdkVSPVKICDFdlgsgvkln 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 GAATVLRRSQYSDFQGTRLYCPPE----WFLHSLYLGREAAVWSLGVLLYNSLNGRLPF-----------RNEK-DICTA 242
Cdd:cd14174 157 SACTPITTPELTTPCGSAEYMAPEvvevFTDEATFYDKRCDLWSLGVILYIMLSGYPPFvghcgtdcgwdRGEVcRVCQN 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 25143934 243 HLL-----GPLPF----FVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd14174 237 KLFesiqeGKYEFpdkdWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
38-295 6.58e-18

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: 84.20  E-value: 6.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  38 GRGGFGVVyRAVRTCD-NALVAVKFIERSNVKEWARIngEQVPMEICMLAKCSKvRGVIRLldWYSI--PEGFLIVMErp 114
Cdd:cd05599  10 GRGAFGEV-RLVRKKDtGHVYAMKKLRKSEMLEKEQV--AHVRAERDILAEADN-PWVVKL--YYSFqdEENLYLIME-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 115 Y-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQ--YSD 191
Cdd:cd05599  82 FlPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLD-ARGHIKLSDFGLCTGLKKSHlaYST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FqGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICT--------AHLlgPLPFFVPVSAEVKDLIS 263
Cdd:cd05599 161 V-GTPDYIAPEVFLQKGY-GKECDWWSLGVIMYEMLIGYPPFCSDDPQETcrkimnwrETL--VFPPEVPISPEAKDLIE 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 264 KCLTfDPFQRC---SLEAILNHPWVKQqtLSWDAL 295
Cdd:cd05599 237 RLLC-DAEHRLganGVEEIKSHPFFKG--VDWDHI 268
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
31-289 7.16e-18

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: 83.37  E-value: 7.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringEQVPMEICMLAKcSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQ------VLVKKEISILNI-ARHRNILRLHESFESHEELVMI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFIKGQG-KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST-KLIDFGAATVLRRSQ 188
Cdd:cd14104  75 FEF-ISGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYiKIIEFGQSRQLKPGD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSDFQGTRL-YCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPF------RNEKDICTAHLLGPLPFFVPVSAEVKDL 261
Cdd:cd14104 154 KFRLQYTSAeFYAPE-VHQHESVSTATDMWSLGCLVYVLLSGINPFeaetnqQTIENIRNAEYAFDDEAFKNISIEALDF 232
                       250       260
                ....*....|....*....|....*...
gi 25143934 262 ISKCLTFDPFQRCSLEAILNHPWVKQQT 289
Cdd:cd14104 233 VDRLLVKERKSRMTAQEALNHPWLKQGM 260
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
34-285 9.02e-18

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: 83.05  E-value: 9.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  34 KAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCSKVRGVIRLLDWYsipegflivmER 113
Cdd:cd14198  13 SKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCR---AEILHEIAVLELAKSNPRVVNLHEVY----------ET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 PYPCIDMFDFIKG-----------QGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVT--GSTKLIDFGA 180
Cdd:cd14198  80 TSEIILILEYAAGgeifnlcvpdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplGDIKIVDFGM 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRS-QYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK------DICTAHLLGPLPFFVP 253
Cdd:cd14198 160 SRKIGHAcELREIMGTPEYLAPE-ILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDnqetflNISQVNVDYSEETFSS 238
                       250       260       270
                ....*....|....*....|....*....|..
gi 25143934 254 VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14198 239 VSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
37-285 9.30e-18

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: 82.70  E-value: 9.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarinGEQVPMEICMLAKCSKVrGVIRLLDWYSIPEGFLIVMERpyp 116
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKE-----REEVKNEINIMNQLNHV-NLIQLYDAFESKTNLTLIMEY--- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 cID---MFDFIKGQGKISEDMARFLF-RQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST-KLIDFGAATVLR-RSQYS 190
Cdd:cd14192  83 -VDggeLFDRITDESYQLTELDAILFtRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQiKIIDFGLARRYKpREKLK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 191 DFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPF------FVPVSAEVKDLISK 264
Cdd:cd14192 162 VNFGTPEFLAPE-VVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWdfdaeaFENLSEEAKDFISR 240
                       250       260
                ....*....|....*....|.
gi 25143934 265 CLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14192 241 LLVKEKSCRMSATQCLKHEWL 261
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
30-281 9.89e-18

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: 82.70  E-value: 9.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSN-VKEWARINGEQvpmEICMLAKCSKVRgVIRLLDWYsIPEGFL 108
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEmMDAKARQDCLK---EIDLLQQLNHPN-IIKYLASF-IENNEL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 -IVMERPyPCIDMFDFIK---GQGK-ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLID------ 177
Cdd:cd08224  76 nIVLELA-DAGDLSRLIKhfkKQKRlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFIT-ANGVVKLGDlglgrf 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 178 FGAATVLRRSQYsdfqGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK----DIC---TAHLLGPLPF 250
Cdd:cd08224 154 FSSKTTAAHSLV----GTPYYMSPE-RIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKmnlySLCkkiEKCEYPPLPA 228
                       250       260       270
                ....*....|....*....|....*....|.
gi 25143934 251 FVpVSAEVKDLISKCLTFDPFQRCSLEAILN 281
Cdd:cd08224 229 DL-YSQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
87-284 1.09e-17

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: 82.34  E-value: 1.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  87 KCSKVRGVIRLLDWY-SIPEG---FLIVMErpypCI---DMFDFI--KGQGKISEDMARFLFRQIAVTVHECVQNRVLHR 157
Cdd:cd14089  49 RASGCPHIVRIIDVYeNTYQGrkcLLVVME----CMeggELFSRIqeRADSAFTEREAAEIMRQIGSAVAHLHSMNIAHR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 158 DLKDENIvidLVTGST-----KLIDFGAA------TVLRRSQYsdfqgTRLYCPPEwflhslYLGRE-----AAVWSLGV 221
Cdd:cd14089 125 DLKPENL---LYSSKGpnailKLTDFGFAketttkKSLQTPCY-----TPYYVAPE------VLGPEkydksCDMWSLGV 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25143934 222 LLYNSLNGRLPFRN----------EKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14089 191 IMYILLCGYPPFYSnhglaispgmKKRIRNGQYEFPNPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
31-285 1.15e-17

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: 82.77  E-value: 1.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWaringEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIV 110
Cdd:cd06643   7 WEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEEL-----EDYMVEIDILASCDH-PNIVKLLDAFYYENNLWIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpypC----IDMFdFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAA----- 181
Cdd:cd06643  81 IEF---CaggaVDAV-MLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTL-DGDIKLADFGVSakntr 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQysdFQGTRLYCPPEWFLHSLYLGR----EAAVWSLGVLLYNSLNGRLPfrnekdictAHLLGPLPFFVPV--- 254
Cdd:cd06643 156 TLQRRDS---FIGTPYWMAPEVVMCETSKDRpydyKADVWSLGVTLIEMAQIEPP---------HHELNPMRVLLKIaks 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 25143934 255 -----------SAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06643 224 epptlaqpsrwSPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
31-289 1.28e-17

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: 82.77  E-value: 1.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWaringEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIV 110
Cdd:cd06644  14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEEL-----EDYMVEIEILATCNH-PYIVKLLGAFYWDGKLWIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MER-PYPCID--MFDFIKGqgkISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFG-AATVLRR 186
Cdd:cd06644  88 IEFcPGGAVDaiMLELDRG---LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTL-DGDIKLADFGvSAKNVKT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSD-FQGTRLYCPPEWFL-----HSLYlGREAAVWSLGVLL---------YNSLNgrlPFRNEKDICTAH---LLGPL 248
Cdd:cd06644 164 LQRRDsFIGTPYWMAPEVVMcetmkDTPY-DYKADIWSLGITLiemaqieppHHELN---PMRVLLKIAKSEpptLSQPS 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25143934 249 PFfvpvSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQT 289
Cdd:cd06644 240 KW----SMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVT 276
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
37-285 1.44e-17

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: 82.07  E-value: 1.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERpYP 116
Cdd:cd06624  16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDSRE------VQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQ-VP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIK---GQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLRR--SQYSD 191
Cdd:cd06624  89 GGSLSALLRskwGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVVKISDFGTSKRLAGinPCTET 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRLYCPPEWFLHSL--YlGREAAVWSLGVLLYNSLNGRLPFrnekdictaHLLGP-------LPFF-----VP--VS 255
Cdd:cd06624 169 FTGTLQYMAPEVIDKGQrgY-GPPADIWSLGCTIIEMATGKPPF---------IELGEpqaamfkVGMFkihpeIPesLS 238
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 256 AEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06624 239 EEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
27-285 1.91e-17

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: 82.41  E-value: 1.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKfIERSNvKEWARINGEQVPMEICMLAKCSKVRG---VIRLLDWYSI 103
Cdd:cd14040   4 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVK-IHQLN-KSWRDEKKENYHKHACREYRIHKELDhprIVKLYDYFSL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 -PEGFLIVMErpYPCIDMFDFIKGQGKI-SEDMARFLFRQI--AVTVHECVQNRVLHRDLKDENIVI--DLVTGSTKLID 177
Cdd:cd14040  82 dTDTFCTVLE--YCEGNDLDFYLKQHKLmSEKEARSIVMQIvnALRYLNEIKPPIIHYDLKPGNILLvdGTACGEIKITD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 178 FGAATVLRRSQY--------SDFQGTRLYCPPEWFLhslyLGREAA-------VWSLGVLLYNSLNGRLPF---RNEKDI 239
Cdd:cd14040 160 FGLSKIMDDDSYgvdgmdltSQGAGTYWYLPPECFV----VGKEPPkisnkvdVWSVGVIFFQCLYGRKPFghnQSQQDI 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 25143934 240 CTAHLL-----GPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14040 236 LQENTIlkateVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
37-283 2.04e-17

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: 81.66  E-value: 2.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKfieRSNVKEWARINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERpyp 116
Cdd:cd13997   8 IGSGSFSEVFKVRSKVDGCLYAVK---KSKKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMEL--- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 C-----IDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSqYSD 191
Cdd:cd13997  82 CengslQDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFIS-NKGTCKIGDFGLATRLETS-GDV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNG-RLPFRNE--KDICTAHLlgPLPFFVPVSAEVKDLISKCLTF 268
Cdd:cd13997 160 EEGDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATGePLPRNGQqwQQLRQGKL--PLPPGLVLSQELTRLLKVMLDP 237
                       250
                ....*....|....*
gi 25143934 269 DPFQRCSLEAILNHP 283
Cdd:cd13997 238 DPTRRPTADQLLAHD 252
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
36-286 2.37e-17

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: 82.04  E-value: 2.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwariNGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERPY 115
Cdd:cd06618  22 EIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKE----ENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDVFICMELMS 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFdFIKGQGKISEDMARFLFRQIAVTVHECVQNR-VLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQYSDFQ- 193
Cdd:cd06618  98 TCLDKL-LKRIQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDE-SGNVKLCDFGISGRLVDSKAKTRSa 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 194 GTRLYCPPEWF---LHSLYLGReAAVWSLGVLLYNSLNGRLPFRN---EKDICTAHLLGPLPFFVP---VSAEVKDLISK 264
Cdd:cd06618 176 GCAAYMAPERIdppDNPKYDIR-ADVWSLGISLVELATGQFPYRNcktEFEVLTKILNEEPPSLPPnegFSPDFCSFVDL 254
                       250       260
                ....*....|....*....|..
gi 25143934 265 CLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06618 255 CLTKDHRYRPKYRELLQHPFIR 276
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
37-285 2.39e-17

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 81.50  E-value: 2.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarinGEQVPMEICMLAKCSKVrGVIRLLDWYSIPEGFLIVMERpYP 116
Cdd:cd14193  12 LGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKE-----KEEVKNEIEVMNQLNHA-NLIQLYDAFESRNDIVLVMEY-VD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIKGQGKISEDMARFLF-RQIAVTVHECVQNRVLHRDLKDENIV-IDLVTGSTKLIDFGAATVLR-RSQYSDFQ 193
Cdd:cd14193  85 GGELFDRIIDENYNLTELDTILFiKQICEGIQYMHQMYILHLDLKPENILcVSREANQVKIIDFGLARRYKpREKLRVNF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 194 GTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPF------FVPVSAEVKDLISKCLT 267
Cdd:cd14193 165 GTPEFLAPE-VVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWdfedeeFADISEEAKDFISKLLI 243
                       250
                ....*....|....*...
gi 25143934 268 FDPFQRCSLEAILNHPWV 285
Cdd:cd14193 244 KEKSWRMSASEALKHPWL 261
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
37-301 3.69e-17

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: 81.88  E-value: 3.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVrgVIRLLDWYSIPEGFLIVMERPYP 116
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPF--LTQLYCCFQTPDRLFFVMEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIKGQgKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAAT--VLRRSQYSDFQG 194
Cdd:cd05590  81 GDLMFHIQKSR-RFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDH-EGHCKLADFGMCKegIFNGKTTSTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 195 TRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQ 272
Cdd:cd05590 159 TPDYIAPEILQEMLY-GPSVDWWAMGVLLYEMLCGHAPFeaENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTM 237
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 273 RCSL------EAILNHPWVKQqtLSWDALTKNKVQ 301
Cdd:cd05590 238 RLGSltlggeEAILRHPFFKE--LDWEKLNRRQIE 270
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
31-285 3.85e-17

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: 81.64  E-value: 3.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKfIERSNvKEWARINGEQVPMEICMLAKCSKVRG---VIRLLDWYSI-PEG 106
Cdd:cd14041   8 YLLLHLLGRGGFSEVYKAFDLTEQRYVAVK-IHQLN-KNWRDEKKENYHKHACREYRIHKELDhprIVKLYDYFSLdTDS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMErpYPCIDMFDFIKGQGKI-SEDMARFLFRQI--AVTVHECVQNRVLHRDLKDENIVI--DLVTGSTKLIDFGAA 181
Cdd:cd14041  86 FCTVLE--YCEGNDLDFYLKQHKLmSEKEARSIIMQIvnALKYLNEIKPPIIHYDLKPGNILLvnGTACGEIKITDFGLS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQYSDFQGTRL---------YCPPEWFLhslyLGREAA-------VWSLGVLLYNSLNGRLPF---RNEKDI--- 239
Cdd:cd14041 164 KIMDDDSYNSVDGMELtsqgagtywYLPPECFV----VGKEPPkisnkvdVWSVGVIFYQCLYGRKPFghnQSQQDIlqe 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 25143934 240 -----CTAHLLGPLPFfvpVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14041 240 ntilkATEVQFPPKPV---VTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
34-285 4.02e-17

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: 80.73  E-value: 4.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  34 KAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarinGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMER 113
Cdd:cd14190   9 KEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKD-----KEMVLLEIQVMNQLNH-RNLIQLYEAIETPNEIVLFMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 pYPCIDMFDFIKGQG-KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGS-TKLIDFGAATVLR-RSQYS 190
Cdd:cd14190  83 -VEGGELFERIVDEDyHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHqVKIIDFGLARRYNpREKLK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 191 DFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH--LLGPLPF----FVPVSAEVKDLISK 264
Cdd:cd14190 162 VNFGTPEFLSPE-VVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNnvLMGNWYFdeetFEHVSDEAKDFVSN 240
                       250       260
                ....*....|....*....|.
gi 25143934 265 CLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14190 241 LIIKERSARMSATQCLKHPWL 261
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
28-295 4.05e-17

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: 82.77  E-value: 4.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINgeQVPMEICMLAKcSKVRGVIRLLDWYSIPEGF 107
Cdd:cd05600  10 LSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVN--HVLTERDILTT-TNSPWLVKLLYAFQDPENV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT---- 182
Cdd:cd05600  87 YLAME--YvPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLID-SSGHIKLTDFGLASgtls 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 ------------------VLRRSQYSDFQGTRL-----------------YCPPEwFLHSLYLGREAAVWSLGVLLYNSL 227
Cdd:cd05600 164 pkkiesmkirleevkntaFLELTAKERRNIYRAmrkedqnyansvvgspdYMAPE-VLRGEGYDLTVDYWSLGCILFECL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 228 NGRLPF--RNEKDIcTAHLL-------------GPLPFFVPVSAEvkDLISKCLTFDPFQRCSLEAILNHPWVKQqtLSW 292
Cdd:cd05600 243 VGFPPFsgSTPNET-WANLYhwkktlqrpvytdPDLEFNLSDEAW--DLITKLITDPQDRLQSPEQIKNHPFFKN--IDW 317

                ...
gi 25143934 293 DAL 295
Cdd:cd05600 318 DRL 320
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
131-300 6.23e-17

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: 81.25  E-value: 6.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 131 SEDMARFLFRQI--AVT-VHECvqnRVLHRDLKDENIVIDlVTGSTKLIDFGaatvLRRSQYSD------FQGTRLYCPP 201
Cdd:cd05571  93 SEDRTRFYGAEIvlALGyLHSQ---GIVYRDLKLENLLLD-KDGHIKITDFG----LCKEEISYgattktFCGTPEYLAP 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 202 EWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQRC----- 274
Cdd:cd05571 165 EVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFynRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLgggpr 243
                       170       180
                ....*....|....*....|....*.
gi 25143934 275 SLEAILNHPWVkqQTLSWDALTKNKV 300
Cdd:cd05571 244 DAKEIMEHPFF--ASINWDDLYQKKI 267
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
37-285 9.74e-17

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: 79.75  E-value: 9.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCS-----KVRGVIRLLDWYSI-----PEG 106
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKQLEQEIALLSKLRhpnivQYYGTEREEDNLYIfleyvPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPYpcidmfdfikgqGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR 186
Cdd:cd06632  88 SIHKLLQRY------------GAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVD-TNGVVKLADFGMAKHVEA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQY-SDFQGTRLYCPPEWFL--HSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVPV----SAEVK 259
Cdd:cd06632 155 FSFaKSFKGSPYWMAPEVIMqkNSGY-GLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPPIpdhlSPDAK 233
                       250       260
                ....*....|....*....|....*.
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06632 234 DFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
37-301 1.00e-16

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: 80.61  E-value: 1.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVkewarINGEQVPMEIC---MLAKCSKVRGVIRLLDWYSIPEGFLIVMER 113
Cdd:cd05591   3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVI-----LQDDDVDCTMTekrILALAAKHPFLTALHSCFQTKDRLFFVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 PYPCIDMFDfIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT--VLRRSQYSD 191
Cdd:cd05591  78 VNGGDLMFQ-IQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLD-AEGHCKLADFGMCKegILNGKTTTT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFR--NEKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFD 269
Cdd:cd05591 156 FCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEadNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKN 234
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 25143934 270 PFQR-------CSLEAILNHPWVKQqtLSWDALTKNKVQ 301
Cdd:cd05591 235 PAKRlgcvasqGGEDAIRQHPFFRE--IDWEALEQRKVK 271
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
30-284 1.03e-16

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: 80.31  E-value: 1.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFI---ERSNVKEwaRINGEQVpMEIcMLAKCSKVRGVIRLLDWYSipeg 106
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIklgERKEAKD--GINFTAL-REI-KLLQELKHPNIIGLLDVFG---- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 flivmERPYPCIdMFDFIKGQ-GKISEDMARFL--------FRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLID 177
Cdd:cd07841  73 -----HKSNINL-VFEFMETDlEKVIKDKSIVLtpadiksyMLMTLRGLEYLHSNWILHRDLKPNNLLIA-SDGVLKLAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 178 FGAATVL----RRSQYSDFqgTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR--LPFRNEKD----ICTAhlLG- 246
Cdd:cd07841 146 FGLARSFgspnRKMTHQVV--TRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVpfLPGDSDIDqlgkIFEA--LGt 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25143934 247 ----------------------PLPF---FVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07841 222 pteenwpgvtslpdyvefkpfpPTPLkqiFPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
30-285 1.37e-16

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: 79.23  E-value: 1.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFI--ERSNVKEwarinGEQVPMEICMLAKCsKVRGVIRLLDWYSIPEGF 107
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIdlTKMPVKE-----KEASKKEVILLAKM-KHPNIVTFFASFQENGRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERpypCI--DMFDFIKGQGKI--SEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATV 183
Cdd:cd08225  75 FIVMEY---CDggDLMKRINRQRGVlfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAKLGDFGIARQ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQYSDFQ--GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEK------DICTAHLLGPLPFFvpvS 255
Cdd:cd08225 152 LNDSMELAYTcvGTPYYLSPEICQNRPY-NNKTDIWSLGCVLYELCTLKHPFEGNNlhqlvlKICQGYFAPISPNF---S 227
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 256 AEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd08225 228 RDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
31-285 1.48e-16

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: 79.27  E-value: 1.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEwariNGEQVPMEICMLAKCSKVRGVIRLLDWY-----SIPE 105
Cdd:cd06608   8 FELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD--IIED----EEEEIKLEINILRKFSNHPNIATFYGAFikkdpPGGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFL-IVME--RPYPCIDMFDFIKGQGK-ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVT--GSTKLIDFG 179
Cdd:cd06608  82 DQLwLVMEycGGGSVTDLVKGLRKKGKrLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNI---LLTeeAEVKLVDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 -----AATVLRRSQysdFQGTRLYCPPEWFLHSLYLGR----EAAVWSLGVLLYNSLNGRLPFrnekdiCTAHLLGPLpF 250
Cdd:cd06608 159 vsaqlDSTLGRRNT---FIGTPYWMAPEVIACDQQPDAsydaRCDVWSLGITAIELADGKPPL------CDMHPMRAL-F 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 25143934 251 FVPV------------SAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06608 229 KIPRnppptlkspekwSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
30-285 1.92e-16

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: 78.71  E-value: 1.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARI--NGEQVPMEICMLakcsKVRGVIRLLDWYSIPEGF 107
Cdd:cd14070   3 SYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVtkNLRREGRIQQMI----RHPNITQLLDILETENSY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS 187
Cdd:cd14070  79 YLVMEL-CPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLD-ENDNIKLIDFGLSNCAGIL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 QYSD---FQ-GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEK-DICTAHL------LGPLPffVPVSA 256
Cdd:cd14070 157 GYSDpfsTQcGSPAYAAPELLARKKY-GPKVDVWSIGVNMYAMLTGTLPFTVEPfSLRALHQkmvdkeMNPLP--TDLSP 233
                       250       260
                ....*....|....*....|....*....
gi 25143934 257 EVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14070 234 GAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
30-284 2.05e-16

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: 78.87  E-value: 2.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIE---RSNVKEWARINGEQvpmeicmlakcsKVRGVIRLLDWYSIPEG 106
Cdd:cd14010   1 NYVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDkskRPEVLNEVRLTHEL------------KHPNVLKFYEWYETSNH 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMErpYpCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVL 184
Cdd:cd14010  69 LWLVVE--Y-CTggDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLD-GNGTLKLSDFGLARRE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 ------------------RRSQYSDFQGTRLYCPPEWF---LHSLylgrEAAVWSLGVLLYNSLNGRLPFRNE------K 237
Cdd:cd14010 145 geilkelfgqfsdegnvnKVSKKQAKRGTPYYMAPELFqggVHSF----ASDLWALGCVLYEMFTGKPPFVAEsftelvE 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 25143934 238 DICTAHLLGP-LPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHP-W 284
Cdd:cd14010 221 KILNEDPPPPpPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
27-286 2.27e-16

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: 79.53  E-value: 2.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAE---LGRGGFGVVYRAVRTCDNALVAVKFIERsnvkewaRINgEQVPMEICMLAKCSKVRGVIRLLDWYSI 103
Cdd:cd14180   1 FFQCYELDLEepaLGEGSFSVCRKCRHRQSGQEYAVKIISR-------RME-ANTQREVAALRLCQSHPNIVALHEVLHD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 PEGFLIVMERpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI-DLVTGST-KLIDFGAA 181
Cdd:cd14180  73 QYHTYLVMEL-LRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYaDESDGAVlKVIDFGFA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TvLRRSQYSDFQG---TRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTA-------HLLGPLPFF 251
Cdd:cd14180 152 R-LRPQGSRPLQTpcfTLQYAAPELFSNQGY-DESCDLWSLGVILYTMLSGQVPFQSKRGKMFHnhaadimHKIKEGDFS 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25143934 252 VP------VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd14180 230 LEgeawkgVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQ 270
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
31-285 2.37e-16

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: 78.92  E-value: 2.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAE-LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingeqVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14173   3 YQLQEEvLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSR-----VFREVEMLYQCQGHRNVLELIEFFEEEDKFYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLV--TGSTKLIDFGAATVLR-R 186
Cdd:cd14173  78 VFEKMRGG-SILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPnqVSPVKICDFDLGSGIKlN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQ--------GTRLYCPPEWFLH-----SLYLGReAAVWSLGVLLYNSLNGRLPF-----------RNEK-DICT 241
Cdd:cd14173 157 SDCSPIStpelltpcGSAEYMAPEVVEAfneeaSIYDKR-CDLWSLGVILYIMLSGYPPFvgrcgsdcgwdRGEAcPACQ 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 25143934 242 AHLL-----GPLPF----FVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14173 236 NMLFesiqeGKYEFpekdWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
119-285 2.38e-16

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 78.38  E-value: 2.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI-DLVTGSTKLIDFGAATVLRRSQYS--DFQGT 195
Cdd:cd14024  70 DMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFtDELRTKLVLVNLEDSCPLNGDDDSltDKHGC 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 196 RLYCPPEwFLHSL--YLGREAAVWSLGVLLYNSLNGRLPFrneKDICTAHLLGPL---PFFVP--VSAEVKDLISKCLTF 268
Cdd:cd14024 150 PAYVGPE-ILSSRrsYSGKAADVWSLGVCLYTMLLGRYPF---QDTEPAALFAKIrrgAFSLPawLSPGARCLVSCMLRR 225
                       170
                ....*....|....*..
gi 25143934 269 DPFQRCSLEAILNHPWV 285
Cdd:cd14024 226 SPAERLKASEILLHPWL 242
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
37-284 2.42e-16

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: 78.52  E-value: 2.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVK--EWARingeqvpmEICMLAKCSKVRGVIRLLD-WYSIPEGFLIVMER 113
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKlkDFLR--------EYNISLELSVHPHIIKTYDvAFETEDYYVFAQEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 -PYPciDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI-DLVTGSTKLIDFGA-----ATVLRR 186
Cdd:cd13987  73 aPYG--DLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDCRRVKLCDFGLtrrvgSTVKRV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SqysdfqGTRLYCPPE--------WF--LHSLylgreaAVWSLGVLLYNSLNGRLPFRNEKDICTAH----------LLG 246
Cdd:cd13987 151 S------GTIPYTAPEvceakkneGFvvDPSI------DVWAFGVLLFCCLTGNFPWEKADSDDQFYeefvrwqkrkNTA 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25143934 247 PLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAI---LNHPW 284
Cdd:cd13987 219 VPSQWRRFTPKALRMFKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
37-301 2.89e-16

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: 79.54  E-value: 2.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNV---KEWARINGEQVPMEICMLAKCSKVRGvirLLDWYSIPEGFLIVMEr 113
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIvakKEVAHTIGERNILVRTALDESPFIVG---LKFSFQTPTDLYLVTD- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 pYPCI-DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG--AATVLRRSQYS 190
Cdd:cd05586  77 -YMSGgELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLD-ANGHIALCDFGlsKADLTDNKTTN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 191 DFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLLGPLPFfvpVSAEVKDLISK 264
Cdd:cd05586 155 TFCGTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEdtqqmyRNIAFGKVRFPKDV---LSDEGRSFVKG 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25143934 265 CLTFDPFQRCSL----EAILNHPWVKQqtLSWDALTKNKVQ 301
Cdd:cd05586 232 LLNRNPKHRLGAhddaVELKEHPFFAD--IDWDLLSKKKIT 270
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
151-289 3.82e-16

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: 78.62  E-value: 3.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 151 QNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGR 230
Cdd:cd06621 123 SRKIIHRDIKPSNILLTR-KGQVKLCDFGVSGELVNSLAGTFTGTSYYMAPERIQGGPY-SITSDVWSLGLTLLEVAQNR 200
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 231 LPFRNEKDictaHLLGPLPF-------FVPV-----------SAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQT 289
Cdd:cd06621 201 FPFPPEGE----PPLGPIELlsyivnmPNPElkdepengikwSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQE 273
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
37-295 4.51e-16

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: 77.95  E-value: 4.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewaRINGEQVPM-EICMLAKCSKvRGVIRLLDWYSIPEGFLIVM---- 111
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIK---KKKGETMALnEKIILEKVSS-PFIVSLAYAFETKDKLCLVLtlmn 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 --ERPYPCIDMfdfikGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQ- 188
Cdd:cd05577  77 ggDLKYHIYNV-----GTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLD-DHGHVRISDLGLAVEFKGGKk 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVPV------SAEVKDLI 262
Cdd:cd05577 151 IKGRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVeypdsfSPEARSLC 230
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 25143934 263 SKCLTFDPFQRC-----SLEAILNHPWVKqqTLSWDAL 295
Cdd:cd05577 231 EGLLQKDPERRLgcrggSADEVKEHPFFR--SLNWQRL 266
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
31-285 4.56e-16

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: 77.73  E-value: 4.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEqvpmeICMLAKCsKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd06613   2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQE-----ISMLKEC-RHPNIVAYFGSYLRRDKLWIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MErpYpC----IDmfDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVT--GSTKLIDFGAATVL 184
Cdd:cd06613  76 ME--Y-CgggsLQ--DIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANI---LLTedGDVKLADFGVSAQL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRS--QYSDFQGTRLYCPPEWFL---HSLYLGReAAVWSLGVLLYNSLNGrLPFRNEKDICTAHLLGPLPFFVPV----- 254
Cdd:cd06613 148 TATiaKRKSFIGTPYWMAPEVAAverKGGYDGK-CDIWALGITAIELAEL-QPPMFDLHPMRALFLIPKSNFDPPklkdk 225
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 255 ---SAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06613 226 ekwSPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
37-300 4.77e-16

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: 78.58  E-value: 4.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARIngEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERPYP 116
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDV--ECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDfIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA--TVLRRSQYSDFQG 194
Cdd:cd05592  81 GDLMFH-IQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLD-REGHIKIADFGMCkeNIYGENKASTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 195 TRLYCPPEWFLHSLYlgrEAAV--WSLGVLLYNSLNGRLPFRNE-KDICTAHLLGPLPFF-VPVSAEVKDLISKCLTFDP 270
Cdd:cd05592 159 TPDYIAPEILKGQKY---NQSVdwWSFGVLLYEMLIGQSPFHGEdEDELFWSICNDTPHYpRWLTKEAASCLSLLLERNP 235
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 271 FQR-----CSLEAILNHPWVKqqTLSWDALTKNKV 300
Cdd:cd05592 236 EKRlgvpeCPAGDIRDHPFFK--TIDWDKLERREI 268
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
37-299 5.60e-16

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: 78.51  E-value: 5.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVkewarINGEQ---VPMEICMLAKCSKvRGVIRLldWYSI--PEGFLIVM 111
Cdd:cd05598   9 IGVGAFGEVSLVRKKDTNALYAMKTLRKKDV-----LKRNQvahVKAERDILAEADN-EWVVKL--YYSFqdKENLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 ErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVhECVQNR-VLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQY 189
Cdd:cd05598  81 D--YiPGGDLMSLLIKKGIFEEDLARFYIAELVCAI-ESVHKMgFIHRDIKPDNILIDR-DGHIKLTDFGLCTGFRWTHD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SDFQ------GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF-------RNEKDICTAHLLgPLPFFVPVSA 256
Cdd:cd05598 157 SKYYlahslvGTPNYIAPEVLLRTGY-TQLCDWWSVGVILYEMLVGQPPFlaqtpaeTQLKVINWRTTL-KIPHEANLSP 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 25143934 257 EVKDLISKCLTfDPFQRCSLEA---ILNHPWVKqqTLSWDALTKNK 299
Cdd:cd05598 235 EAKDLILRLCC-DAEDRLGRNGadeIKAHPFFA--GIDWEKLRKQK 277
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
31-285 5.86e-16

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


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 77.35  E-value: 5.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarinGEQVPMEICMLaKCSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd14191   4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKE-----KENIRQEISIM-NCLHHPKLVQCVDAFEEKANIVMV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFIKGQG-KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST-KLIDFGAATVLRRS- 187
Cdd:cd14191  78 LEM-VSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKiKLIDFGLARRLENAg 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 QYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKD------ICTAHLLGPLPFFVPVSAEVKDL 261
Cdd:cd14191 157 SLKVLFGTPEFVAPE-VINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDnetlanVTSATWDFDDEAFDEISDDAKDF 235
                       250       260
                ....*....|....*....|....
gi 25143934 262 ISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14191 236 ISNLLKKDMKARLTCTQCLQHPWL 259
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
119-300 5.87e-16

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: 77.83  E-value: 5.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTV---HECvqnRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQYSdFQGT 195
Cdd:cd14209  87 EMFSHLRRIGRFSEPHARFYAAQIVLAFeylHSL---DLIYRDLKPENLLIDQ-QGYIKVTDFGFAKRVKGRTWT-LCGT 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 196 RLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRN-------EKdICTAHLLGPLPFfvpvSAEVKDLISKCLTF 268
Cdd:cd14209 162 PEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFAdqpiqiyEK-IVSGKVRFPSHF----SSDLKDLLRNLLQV 235
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 25143934 269 DPFQRC-SLEA----ILNHPWVKqqTLSWDALTKNKV 300
Cdd:cd14209 236 DLTKRFgNLKNgvndIKNHKWFA--TTDWIAIYQRKV 270
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
37-283 6.56e-16

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


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 77.73  E-value: 6.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLaKCSKVRGVIRLLDWYSIPEGFLIVMErpYP 116
Cdd:cd07848   9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVK---ETTLRELKML-RTLKQENIVELKEAFRRRGKLYLVFE--YV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIKG--QGKISEDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR---SQYSD 191
Cdd:cd07848  83 EKNMLELLEEmpNGVPPEKVRSYIY-QLIKAIHWCHKNDIVHRDIKPENLLIS-HNDVLKLCDFGFARNLSEgsnANYTE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI----CTAHLLGPLP------FFV--------- 252
Cdd:cd07848 161 YVATRWYRSPELLLGAPY-GKAVDMWSVGCILGELSDGQPLFPGESEIdqlfTIQKVLGPLPaeqmklFYSnprfhglrf 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 25143934 253 -----PVSAEVK----------DLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd07848 240 pavnhPQSLERRylgilsgvllDLMKNLLKLNPTDRYLTEQCLNHP 285
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
37-287 7.31e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 77.61  E-value: 7.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingeQVPMEICMLAKCSKvrgvIRLLDWYsipeGFLIVMERPYP 116
Cdd:cd06619   9 LGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQK----QIMSELEILYKCDS----PYIIGFY----GAFFVENRISI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDfiKGQGKISEDMARFLFRQIAVTVHECVQN----RVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSDF 192
Cdd:cd06619  77 CTEFMD--GGSLDVYRKIPEHVLGRIAVAVVKGLTYlwslKILHRDVKPSNMLVN-TRGQVKLCDFGVSTQLVNSIAKTY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 193 QGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLP----FRNEKDICTAHLLGPL----PFFVPV---SAEVKDL 261
Cdd:cd06619 154 VGTNAYMAPERISGEQY-GIHSDVWSLGISFMELALGRFPypqiQKNQGSLMPLQLLQCIvdedPPVLPVgqfSEKFVHF 232
                       250       260
                ....*....|....*....|....*.
gi 25143934 262 ISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06619 233 ITQCMRKQPKERPAPENLMDHPFIVQ 258
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
119-284 7.55e-16

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 76.62  E-value: 7.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI-DLVTGSTKLIDFGAATVLRRSQ--YSDFQGT 195
Cdd:cd14023  70 DMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFsDEERTQLRLESLEDTHIMKGEDdaLSDKHGC 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 196 RLYCPPEwFLHSL--YLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVP--VSAEVKDLISKCLTFDPF 271
Cdd:cd14023 150 PAYVSPE-ILNTTgtYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPdhVSPKARCLIRSLLRREPS 228
                       170
                ....*....|...
gi 25143934 272 QRCSLEAILNHPW 284
Cdd:cd14023 229 ERLTAPEILLHPW 241
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
31-284 7.77e-16

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 77.99  E-value: 7.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVK---EWARIngeqvpmEICMLAKCSKVRG-----VIRLLDWYS 102
Cdd:cd14134  14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIR--NVEkyrEAAKI-------EIDVLETLAEKDPngkshCVQLRDWFD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 103 IPEGFLIVMERPYPCIdmFDFIKGQGKIS------EDMARFLFRQIAVtVHECvqnRVLHRDLKDENIVidLVTGST--- 173
Cdd:cd14134  85 YRGHMCIVFELLGPSL--YDFLKKNNYGPfplehvQHIAKQLLEAVAF-LHDL---KLTHTDLKPENIL--LVDSDYvkv 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 174 -----------------KLIDFGAATvLRRSQYSDFQGTRLYCPPEWFLHslyLG--REAAVWSLGVLLYNSLNGRLPFR 234
Cdd:cd14134 157 ynpkkkrqirvpkstdiKLIDFGSAT-FDDEYHSSIVSTRHYRAPEVILG---LGwsYPCDVWSIGCILVELYTGELLFQ 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 235 NEKDIctAHL------LGPLP------------------------------------------FFVPVSAEVK---DLIS 263
Cdd:cd14134 233 THDNL--EHLammeriLGPLPkrmirrakkgakyfyfyhgrldwpegsssgrsikrvckplkrLMLLVDPEHRllfDLIR 310
                       330       340
                ....*....|....*....|.
gi 25143934 264 KCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14134 311 KMLEYDPSKRITAKEALKHPF 331
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
31-284 8.48e-16

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 76.86  E-value: 8.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIE-RSNVKEWARingeqvpMEICMLAKCSKVRgVIRLLDWYSIPEGFLI 109
Cdd:cd14108   4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPvRAKKKTSAR-------RELALLAELDHKS-IVRFHDAFEKRRVVII 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpypCI-DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI-DLVTGSTKLIDFGAATVLR-- 185
Cdd:cd14108  76 VTEL---CHeELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMaDQKTDQVRICDFGNAQELTpn 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFqGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTahLLGPLPF--------FVPVSAE 257
Cdd:cd14108 153 EPQYCKY-GTPEFVAPE-IVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTT--LMNIRNYnvafeesmFKDLCRE 228
                       250       260
                ....*....|....*....|....*..
gi 25143934 258 VKDLISKCLTFDPFqRCSLEAILNHPW 284
Cdd:cd14108 229 AKGFIIKVLVSDRL-RPDAEETLEHPW 254
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
36-287 9.23e-16

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: 77.41  E-value: 9.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEWARIngeQVPMEICMLAKCSKVRGVIRlldWYSI--PEG-FLIVME 112
Cdd:cd06616  13 EIGRGAFGTVNKMLHKPSGTIMAVKRI-RSTVDEKEQK---RLLMDLDVVMRSSDCPYIVK---FYGAlfREGdCWICME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 RPYPCID---MFDFIKGQGKISEDMarflFRQIAVTV-----HECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVL 184
Cdd:cd06616  86 LMDISLDkfyKYVYEVLDSVIPEEI----LGKIAVATvkalnYLKEELKIIHRDVKPSNILLDR-NGNIKLCDFGISGQL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRS--QYSDfQGTRLYCPPEWFLHSL----YLGReAAVWSLGVLLYNSLNGRLPFRNEKDI---CTAHLLGPLPFFVP-- 253
Cdd:cd06616 161 VDSiaKTRD-AGCRPYMAPERIDPSAsrdgYDVR-SDVWSLGITLYEVATGKFPYPKWNSVfdqLTQVVKGDPPILSNse 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 25143934 254 ---VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06616 239 ereFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKM 275
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
36-287 1.35e-15

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: 76.81  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEwARINgeQVPMEICMLAKCSKVRgvirLLDWYsipeGFLIVMERPY 115
Cdd:cd06622   8 ELGKGNYGSVYKVLHRPTGVTMAMKEI-RLELDE-SKFN--QIIMELDILHKAVSPY----IVDFY----GAFFIEGAVY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDF-----IKGQGKISEDMARFLFRQIA-VTVH--ECV--QNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLR 185
Cdd:cd06622  76 MCMEYMDAgsldkLYAGGVATEGIPEDVLRRITyAVVKglKFLkeEHNIIHRDVKPTNVLVN-GNGQVKLCDFGVSGNLV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQGTRLYCPPEWFLHSLYLGR-----EAAVWSLGVLLYNSLNGRLPFRNEK-----DICTAHLLGPLPFFVP-V 254
Cdd:cd06622 155 ASLAKTNIGCQSYMAPERIKSGGPNQNptytvQSDVWSLGLSILEMALGRYPYPPETyanifAQLSAIVDGDPPTLPSgY 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 25143934 255 SAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06622 235 SDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVK 267
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
34-284 1.40e-15

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 76.56  E-value: 1.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  34 KAE-LGRGGFGVVYRAVRTCDNALVAVKFIersnvkewaRINGEQ--VP----MEICMLaKCSKVRGVIRLLD-WYSIPE 105
Cdd:cd07835   3 KLEkIGEGTYGVVYKARDKLTGEIVALKKI---------RLETEDegVPstaiREISLL-KELNHPNIVRLLDvVHSENK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIvmerpYPCIDM-----FDFIKGQGKISEDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGA 180
Cdd:cd07835  73 LYLV-----FEFLDLdlkkyMDSSPLTGLDPPLIKSYLY-QLLQGIAFCHSHRVLHRDLKPQNLLID-TEGALKLADFGL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATV----LRrsQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH----LLG-P---- 247
Cdd:cd07835 146 ARAfgvpVR--TYTHEVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFrifrTLGtPdedv 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 248 ------LPFFVPV----------------SAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07835 224 wpgvtsLPDYKPTfpkwarqdlskvvpslDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
37-284 1.55e-15

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: 76.69  E-value: 1.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVK-FIERSNVKEWARIngeqVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMErpy 115
Cdd:cd07846   9 VGEGSYGMVMKCRHKETGQIVAIKkFLESEDDKMVKKI----AMREIKMLKQLRH-ENLVNLIEVFRRKKRWYLVFE--- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pCID---MFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQ--YS 190
Cdd:cd07846  81 -FVDhtvLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQ-SGVVKLCDFGFARTLAAPGevYT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 191 DFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH----LLGPL-----------PFFVPV- 254
Cdd:cd07846 159 DYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYhiikCLGNLiprhqelfqknPLFAGVr 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 25143934 255 -----------------SAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07846 239 lpevkeveplerrypklSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
37-282 1.64e-15

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: 76.12  E-value: 1.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNV-KEWARingEQVPMEIcMLAKCSKVRGVIRLLDWYSIPEGFLIVMERpy 115
Cdd:cd14189   9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRVaKPHQR---EKIVNEI-ELHRDLHHKHVVKFSHHFEDAENIYIFLEL-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQY--SD 191
Cdd:cd14189  83 -CSrkSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFIN-ENMELKVGDFGLAARLEPPEQrkKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRN----EKDICTAHLLGPLPFFVPVSAevKDLISKCLT 267
Cdd:cd14189 161 ICGTPNYLAPEVLLRQGH-GPESDVWSLGCVMYTLLCGNPPFETldlkETYRCIKQVKYTLPASLSLPA--RHLLAGILK 237
                       250
                ....*....|....*
gi 25143934 268 FDPFQRCSLEAILNH 282
Cdd:cd14189 238 RNPGDRLTLDQILEH 252
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
95-286 1.96e-15

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 76.05  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   95 IRLLDWYSIPEGFLIVMErpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST 173
Cdd:PHA03390  72 IKLYYSVTTLKGHVLIMD--YiKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDRI 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  174 KLIDFGaaTVLRRSQYSDFQGTRLYCPPEWFLHSLYlgreaAV----WSLGVLLYNSLNGRLPFRNEKD--ICTAHLLG- 246
Cdd:PHA03390 150 YLCDYG--LCKIIGTPSCYDGTLDYFSPEKIKGHNY-----DVsfdwWAVGVLTYELLTGKHPFKEDEDeeLDLESLLKr 222
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 25143934  247 ---PLPFFVPVSAEVKDLISKCLTFDPFQR-CSLEAILNHPWVK 286
Cdd:PHA03390 223 qqkKLPFIKNVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFLK 266
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
37-280 2.05e-15

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: 75.84  E-value: 2.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAvrTCDNALVAVKfIERSNVKEWARINGEQVPMEICMLAkcskvrgvirLLDWYSIPEGFLIVMERPYP 116
Cdd:cd14146   2 IGVGGFGKVYRA--TWKGQEVAVK-AARQDPDEDIKATAESVRQEAKLFS----------MLRHPNIIKLEGVCLEEPNL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMfDFIKG-------QGKISEDMARFLFR-----------QIA---VTVHECVQNRVLHRDLKDENIVI-------DL 168
Cdd:cd14146  69 CLVM-EFARGgtlnralAAANAAPGPRRARRipphilvnwavQIArgmLYLHEEAVVPILHRDLKSSNILLlekiehdDI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 169 VTGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH----- 243
Cdd:cd14146 148 CNKTLKITDFGLAREWHRTTKMSAAGTYAWMAPEVIKSSLF-SKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYgvavn 226
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 25143934 244 -LLGPLPFFVPvsAEVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd14146 227 kLTLPIPSTCP--EPFAKLMKECWEQDPHIRPSFALIL 262
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
37-282 2.48e-15

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: 75.43  E-value: 2.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNV-KEWARingEQVPMEIcMLAKCSKVRGVIRLLDWYSIPEGFLIVMERpy 115
Cdd:cd14188   9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVsKPHQR---EKIDKEI-ELHRILHHKHVVQFYHYFEDKENIYILLEY-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLR--RSQYSD 191
Cdd:cd14188  83 -CSrrSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN-ENMELKVGDFGLAARLEplEHRRRT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVPVS--AEVKDLISKCLTFD 269
Cdd:cd14188 161 ICGTPNYLSPE-VLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSllAPAKHLIASMLSKN 239
                       250
                ....*....|...
gi 25143934 270 PFQRCSLEAILNH 282
Cdd:cd14188 240 PEDRPSLDEIIRH 252
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
30-238 2.67e-15

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 75.37  E-value: 2.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFiersnvkEWARINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14017   1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKV-------ESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTK---LIDFGAATVLRR 186
Cdd:cd14017  74 VMTLLGPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDERtvyILDFGLARQYTN 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143934 187 SQYSD---------FQGTRLYCPPEWFLHSlYLGREAAVWSLGVLLYNSLNGRLPFRNEKD 238
Cdd:cd14017 154 KDGEVerpprnaagFRGTVRYASVNAHRNK-EQGRRDDLWSWFYMLIEFVTGQLPWRKLKD 213
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
37-233 2.68e-15

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: 75.77  E-value: 2.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTcDNALVAVKFIERSN----VKEWARingeqvpmEICMLAKCsKVRGVIRLLDWYSIPEGFLIVMe 112
Cdd:cd14066   1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMNcaasKKEFLT--------ELEMLGRL-RHPNLVRLLGYCLESDEKLLVY- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 rPY-PCIDMFDFIKGQG-----------KISEDMAR---FLfrqiavtvHECVQNRVLHRDLKDENIVIDLVTgSTKLID 177
Cdd:cd14066  70 -EYmPNGSLEDRLHCHKgspplpwpqrlKIAKGIARgleYL--------HEECPPPIIHGDIKSSNILLDEDF-EPKLTD 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 178 FGAATVLRRSQY----SDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPF 233
Cdd:cd14066 140 FGLARLIPPSESvsktSAVKGTIGYLAPE-YIRTGRVSTKSDVYSFGVVLLELLTGKPAV 198
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
31-285 2.88e-15

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: 75.99  E-value: 2.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQvpmEICMLAKCSKvRGVIRL----------LDW 100
Cdd:cd07864   9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIR---EIKILRQLNH-RSVVNLkeivtdkqdaLDF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 101 YSIPEGFLIVMErpYPCIDMFDFIK-GQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG 179
Cdd:cd07864  85 KKDKGAFYLVFE--YMDHDLMGLLEsGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLN-NKGQIKLADFG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVLRRSQ---YSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDI----CTAHLLG-PLPFF 251
Cdd:cd07864 162 LARLYNSEEsrpYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELaqleLISRLCGsPCPAV 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143934 252 VP---------------------------VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd07864 242 WPdviklpyfntmkpkkqyrrrlreefsfIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
37-280 3.07e-15

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: 75.41  E-value: 3.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNalVAVKFIeRSNVKEWARINGEQVPME---ICMLAKcskvRGVIRLLDwysipegflIVMER 113
Cdd:cd14148   2 IGVGGFGKVYKGLWRGEE--VAVKAA-RQDPDEDIAVTAENVRQEarlFWMLQH----PNIIALRG---------VCLNP 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 PYPCIDMfDFIKGqGKISEDMA------RFLFR---QIAVT---VHECVQNRVLHRDLKDENIVI-------DLVTGSTK 174
Cdd:cd14148  66 PHLCLVM-EYARG-GALNRALAgkkvppHVLVNwavQIARGmnyLHNEAIVPIIHRDLKSSNILIlepiendDLSGKTLK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 175 LIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH------LLGPL 248
Cdd:cd14148 144 ITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLF-SKSSDVWSFGVLLWELLTGEVPYREIDALAVAYgvamnkLTLPI 222
                       250       260       270
                ....*....|....*....|....*....|..
gi 25143934 249 PFFVPvsAEVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd14148 223 PSTCP--EPFARLLEECWDPDPHGRPDFGSIL 252
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
19-293 3.15e-15

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: 76.97  E-value: 3.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  19 ESSRGFSKFKKNYKLKAE-------LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSkv 91
Cdd:cd05624  55 EWAKPFTQLVKEMQLHRDdfeiikvIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQ-- 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  92 rgVIRLLDWYSIPEGFLIVMERPYPCIDMFDFI-KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVT 170
Cdd:cd05624 133 --WITTLHYAFQDENYLYLVMDYYVGGDLLTLLsKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLD-MN 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 171 GSTKLIDFGAATVLRRS---QYSDFQGTRLYCPPEwFLHSL-----YLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTa 242
Cdd:cd05624 210 GHIRLADFGSCLKMNDDgtvQSSVAVGTPDYISPE-ILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVET- 287
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25143934 243 hlLGPL-----PFFVP-----VSAEVKDLISK--CLTFDPFQRCSLEAILNHPWVkqQTLSWD 293
Cdd:cd05624 288 --YGKImnheeRFQFPshvtdVSEEAKDLIQRliCSRERRLGQNGIEDFKKHAFF--EGLNWE 346
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
81-285 3.30e-15

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: 75.45  E-value: 3.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  81 EICMLaKCSKVRGVIRLLDWYSIPEGFLIVMERPyPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLK 160
Cdd:cd14088  49 EINIL-KMVKHPNILQLVDVFETRKEYFIFLELA-TGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLK 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 161 DENIVIDLVTGSTKLI--DFGAATvLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE-- 236
Cdd:cd14088 127 LENLVYYNRLKNSKIVisDFHLAK-LENGLIKEPCGTPEYLAPEVVGRQRY-GRPVDCWAIGVIMYILLSGNPPFYDEae 204
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143934 237 --------KDICTAHLLGPLPFFVP----VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14088 205 eddyenhdKNLFRKILAGDYEFDSPywddISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
37-297 5.09e-15

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: 75.09  E-value: 5.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERsnvkEWARINGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIVMERpYP 116
Cdd:cd06642  12 IGKGSFGEVYKGIDNRTKEVVAIKIIDL----EEAEDEIEDIQQEITVLSQCDSPY-ITRYYGSYLKGTKLWIIMEY-LG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIKgQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQY--SDFQG 194
Cdd:cd06642  86 GGSALDLLK-PGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLS-EQGDVKLADFGVAGQLTDTQIkrNTFVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 195 TRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFrneKDICTAHLLGPLPFFVPVSAE------VKDLISKCLTF 268
Cdd:cd06642 164 TPFWMAPEVIKQSAY-DFKADIWSLGITAIELAKGEPPN---SDLHPMRVLFLIPKNSPPTLEgqhskpFKEFVEACLNK 239
                       250       260
                ....*....|....*....|....*....
gi 25143934 269 DPFQRCSLEAILNHPWVKQQTLSWDALTK 297
Cdd:cd06642 240 DPRFRPTAKELLKHKFITRYTKKTSFLTE 268
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
30-289 5.10e-15

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: 75.16  E-value: 5.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsnVKEWARIngEQVPMEICMLAKCsKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd06611   6 IWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQ---IESEEEL--EDFMVEIDILSEC-KHPNIVGLYEAYFYENKLWI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpypcidmfdFIKGQ--GKISEDMARFLFR-QIAVTVHECVQ-------NRVLHRDLKDENIVIDLvTGSTKLIDFG 179
Cdd:cd06611  80 LIE----------FCDGGalDSIMLELERGLTEpQIRYVCRQMLEalnflhsHKVIHRDLKAGNILLTL-DGDVKLADFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVLRRS--QYSDFQGTRLYCPPEWFLHSLYLGR----EAAVWSLGVLLYNSLNGRLPfrnekdictAHLLGPLPFFVP 253
Cdd:cd06611 149 VSAKNKSTlqKRDTFIGTPYWMAPEVVACETFKDNpydyKADIWSLGITLIELAQMEPP---------HHELNPMRVLLK 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 25143934 254 V--------------SAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQT 289
Cdd:cd06611 220 IlksepptldqpskwSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQS 269
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
28-283 6.19e-15

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: 74.85  E-value: 6.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVK-FIERSNVKewariNGEqvpMEICMLAKCskvRGVIRLLDWYSIPEG 106
Cdd:cd14137   3 EISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKkVLQDKRYK-----NRE---LQIMRRLKH---PNIVKLKYFFYSSGE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 -----FL-IVMErpypCI--DMFDFIKGQGKISEDMARF--------LFRQIAvTVHEcvQNrVLHRDLKDENIVIDLVT 170
Cdd:cd14137  72 kkdevYLnLVME----YMpeTLYRVIRHYSKNKQTIPIIyvklysyqLFRGLA-YLHS--LG-ICHRDIKPQNLLVDPET 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 171 GSTKLIDFGAATVLRRSQYS-DFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKD------ICtaH 243
Cdd:cd14137 144 GVLKLCDFGSAKRLVPGEPNvSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSvdqlveII--K 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 244 LLG-----------------PLP----------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd14137 222 VLGtptreqikamnpnytefKFPqikphpwekvFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
119-301 6.46e-15

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: 75.34  E-value: 6.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA----TVLRRSQYSdFQG 194
Cdd:cd05614  91 ELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLD-SEGHVVLTDFGLSkeflTEEKERTYS-FCG 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 195 TRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPF-----RNEKDICTAHLLGPLPFFVPV-SAEVKDLISKCLTF 268
Cdd:cd05614 169 TIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFtlegeKNTQSEVSRRILKCDPPFPSFiGPVARDLLQKLLCK 248
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 25143934 269 DPFQRC-----SLEAILNHPWVKQqtLSWDALTKNKVQ 301
Cdd:cd05614 249 DPKKRLgagpqGAQEIKEHPFFKG--LDWEALALRKVN 284
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
31-284 7.00e-15

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: 74.72  E-value: 7.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRavrtCDN----ALVAVK-FIERS---NVKEWA-RingeqvpmEICMLaKCSKVRGVIRLLDWY 101
Cdd:cd07847   3 YEKLSKIGEGSYGVVFK----CRNretgQIVAIKkFVESEddpVIKKIAlR--------EIRML-KQLKHPNLVNLIEVF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 102 SIPEGFLIVMER-PYPCIDMFDfiKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGA 180
Cdd:cd07847  70 RRKRKLHLVFEYcDHTVLNELE--KNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILIT-KQGQIKLCDFGF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRR--SQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHL----LGPL------ 248
Cdd:cd07847 147 ARILTGpgDDYTDYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLirktLGDLiprhqq 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 249 -----PFF----VPVSAEVKDLISK--------------CLTFDPFQRCSLEAILNHPW 284
Cdd:cd07847 227 ifstnQFFkglsIPEPETREPLESKfpnisspalsflkgCLQMDPTERLSCEELLEHPY 285
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
37-280 1.02e-14

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: 73.58  E-value: 1.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAvrTCDNALVAVKfIERSNVKEWARINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMErpyp 116
Cdd:cd14061   2 IGVGGFGKVYRG--IWRGEEVAVK-AARQDPDEDISVTLENVRQEARLFWMLRH-PNIIALRGVCLQPPNLCLVME---- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 cidmfdFIKGqGKISEDMARFLFR---------QIAVTV---HECVQNRVLHRDLKDENIVI-------DLVTGSTKLID 177
Cdd:cd14061  74 ------YARG-GALNRVLAGRKIPphvlvdwaiQIARGMnylHNEAPVPIIHRDLKSSNILIleaieneDLENKTLKITD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 178 FGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLG------PLPFF 251
Cdd:cd14061 147 FGLAREWHKTTRMSAAGTYAWMAPEVIKSSTF-SKASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAvnkltlPIPST 225
                       250       260
                ....*....|....*....|....*....
gi 25143934 252 VPvsAEVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd14061 226 CP--EPFAQLMKDCWQPDPHDRPSFADIL 252
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
94-285 1.09e-14

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: 73.87  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  94 VIRLLDWY-SIPEG---FLIVMErpypCI---DMFDFIKGQGK--ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENI 164
Cdd:cd14172  59 IVHILDVYeNMHHGkrcLLIIME----CMeggELFSRIQERGDqaFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENL 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 165 VIDLV--TGSTKLIDFGAATvlRRSQYSDFQG---TRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRN---- 235
Cdd:cd14172 135 LYTSKekDAVLKLTDFGFAK--ETTVQNALQTpcyTPYYVAPEVLGPEKY-DKSCDMWSLGVIMYILLCGFPPFYSntgq 211
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 236 ------EKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14172 212 aispgmKRRIRMGQYGFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
32-280 1.16e-14

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 73.72  E-value: 1.16e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934     32 KLKAELGRGGFGVVYRAVRTCDN----ALVAVKFI----ERSNVKEWARingeqvpmEICMLAKCSKvRGVIRLLDWYSI 103
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGgkkkVEVAVKTLkedaSEQQIEEFLR--------EARIMRKLDH-PNVVKLLGVCTE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    104 PEGFLIVMErpY-PCIDMFDFIKG-QGKIS-EDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGA 180
Cdd:smart00219  73 EEPLYIVME--YmEGGDLLSYLRKnRPKLSlSDLLSFAL-QIARGMEYLESKNFIHRDLAARNCLVG-ENLVVKISDFGL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    181 ATVLRRSQYSDFQGTRL---YCPPEWFLHSLYlgREAA-VWSLGVLLYNSL-NGRLPFRNEKDICTAHLLG-----PLPF 250
Cdd:smart00219 149 SRDLYDDDYYRKRGGKLpirWMAPESLKEGKF--TSKSdVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLKngyrlPQPP 226
                          250       260       270
                   ....*....|....*....|....*....|
gi 25143934    251 FVPvsAEVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:smart00219 227 NCP--PELYDLMLQCWAEDPEDRPTFSELV 254
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
33-282 1.46e-14

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: 73.54  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  33 LKAELGRGGFGVVYRAVRTCDNalVAVKfIERSNVKEWARINGEQVPMEICMLAkcskvrgvirLLDWYSIPEGFLIVME 112
Cdd:cd14145  10 LEEIIGIGGFGKVYRAIWIGDE--VAVK-AARHDPDEDISQTIENVRQEAKLFA----------MLKHPNIIALRGVCLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 RPYPCIDMfDFIKG-------QGK-ISEDMARFLFRQIA---VTVHECVQNRVLHRDLKDENIVI-------DLVTGSTK 174
Cdd:cd14145  77 EPNLCLVM-EFARGgplnrvlSGKrIPPDILVNWAVQIArgmNYLHCEAIVPVIHRDLKSSNILIlekvengDLSNKILK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 175 LIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH------LLGPL 248
Cdd:cd14145 156 ITDFGLAREWHRTTKMSAAGTYAWMAPEVIRSSMF-SKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYgvamnkLSLPI 234
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 249 PFFVPvsAEVKDLISKCLTFDPFQRCSLEAILNH 282
Cdd:cd14145 235 PSTCP--EPFARLMEDCWNPDPHSRPPFTNILDQ 266
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
29-283 1.60e-14

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: 73.16  E-value: 1.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERsnvkEWARINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFL 108
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDL----EKCQTSMDELRKEIQAMSQCNH-PNVVSYYTSFVVGDELW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMerPY----PCIDMFDFIKGQGKISEDMarflfrqIAVTVHECVQ-------NRVLHRDLKDENIVIDlVTGSTKLID 177
Cdd:cd06610  76 LVM--PLlsggSLLDIMKSSYPRGGLDEAI-------IATVLKEVLKgleylhsNGQIHRDVKAGNILLG-EDGSVKIAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 178 FGAATVL-------RRSQYsDFQGTRLYCPPEwFLHSL--YlGREAAVWSLGVLLYNSLNGRLPFrnekdictaHLLGPL 248
Cdd:cd06610 146 FGVSASLatggdrtRKVRK-TFVGTPCWMAPE-VMEQVrgY-DFKADIWSFGITAIELATGAAPY---------SKYPPM 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 25143934 249 PFFV-----------------PVSAEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd06610 214 KVLMltlqndppsletgadykKYSKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
129-332 2.48e-14

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: 73.54  E-value: 2.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 129 KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS---QYSDFQGTRLYCPPEWFL 205
Cdd:cd05597  98 RLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLD-RNGHIRLADFGSCLKLREDgtvQSSVAVGTPDYISPEILQ 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 206 -----HSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICT-AHLLG-----PLPFFVP-VSAEVKDLISK--CLTFDPF 271
Cdd:cd05597 177 amedgKGRY-GPECDWWSLGVCMYEMLYGETPFYAESLVETyGKIMNhkehfSFPDDEDdVSEEAKDLIRRliCSRERRL 255
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143934 272 QRCSLEAILNHPWVKQqtLSWDALTKNK---VQKKTSESsdDHHSETLGDHSETEEDRSPPTSS 332
Cdd:cd05597 256 GQNGIDDFKKHPFFEG--IDWDNIRDSTppyIPEVTSPT--DTSNFDVDDDDLRHTDSLPPPSN 315
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
31-285 3.15e-14

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: 72.46  E-value: 3.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAV---RTCDNALVAVKFIERSNVKEWARIngeQVPMEICMLAKCSKvRGVIRLLDWYSIPEGF 107
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSdlkATADEELKVLKEISVGELQPDETV---DANREAKLLSKLDH-PAIVKFHDSFVEKESF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERpypCI--DMFDFI----KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVidLVTGSTKLIDFGAA 181
Cdd:cd08222  78 CIVTEY---CEggDLDDKIseykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIF--LKNNVIKVGDFGIS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRS--QYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPV-SA 256
Cdd:cd08222 153 RILMGTsdLATTFTGTPYYMSPEVLKHEGY-NSKSDIWSLGCILYEMCCLKHAFdgQNLLSVMYKIVEGETPSLPDKySK 231
                       250       260
                ....*....|....*....|....*....
gi 25143934 257 EVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd08222 232 ELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
72-287 3.93e-14

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: 72.76  E-value: 3.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  72 RINGEQVPMEicMLAKCSKVR-------------GVIRLLDWY-SIPEG---FLIVMErpypCID---MFDFIKGQGK-- 129
Cdd:cd14170  24 KRTQEKFALK--MLQDCPKARrevelhwrasqcpHIVRIVDVYeNLYAGrkcLLIVME----CLDggeLFSRIQDRGDqa 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 130 ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST--KLIDFGAAtvlRRSQYSDFQGTRLYCPpeWFLHS 207
Cdd:cd14170  98 FTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAilKLTDFGFA---KETTSHNSLTTPCYTP--YYVAP 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 208 LYLGRE-----AAVWSLGVLLYNSLNGRLPFRN----------EKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQ 272
Cdd:cd14170 173 EVLGPEkydksCDMWSLGVIMYILLCGYPPFYSnhglaispgmKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQ 252
                       250
                ....*....|....*
gi 25143934 273 RCSLEAILNHPWVKQ 287
Cdd:cd14170 253 RMTITEFMNHPWIMQ 267
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
119-286 4.97e-14

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: 72.04  E-value: 4.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG-----AATVLRRSqYSdFQ 193
Cdd:cd05583  85 ELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLD-SEGHVVLTDFGlskefLPGENDRA-YS-FC 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 194 GTRLYCPPEwFLHSLYLGREAAV--WSLGVLLYNSLNGRLPF-----RN-EKDICTAHLLGPLPFFVPVSAEVKDLISKC 265
Cdd:cd05583 162 GTIEYMAPE-VVRGGSDGHDKAVdwWSLGVLTYELLTGASPFtvdgeRNsQSEISKRILKSHPPIPKTFSAEAKDFILKL 240
                       170       180
                ....*....|....*....|....*.
gi 25143934 266 LTFDPFQR-----CSLEAILNHPWVK 286
Cdd:cd05583 241 LEKDPKKRlgagpRGAHEIKEHPFFK 266
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
105-280 5.03e-14

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: 71.54  E-value: 5.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFL-IVMERpypCI--DMFDFIKGQ-GKI-SEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFG 179
Cdd:cd08219  70 DGHLyIVMEY---CDggDLMQKIKLQrGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQ-NGKVKLGDFG 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVLRR--SQYSDFQGTRLYCPPE-WflHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK------DICTAHlLGPLPf 250
Cdd:cd08219 146 SARLLTSpgAYACTYVGTPYYVPPEiW--ENMPYNNKSDIWSLGCILYELCTLKHPFQANSwknlilKVCQGS-YKPLP- 221
                       170       180       190
                ....*....|....*....|....*....|
gi 25143934 251 fVPVSAEVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd08219 222 -SHYSYELRSLIKQMFKRNPRSRPSATTIL 250
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
28-285 6.08e-14

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: 71.39  E-value: 6.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVyravRTCDNALVAVKFIERsnVKEWARINGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGF 107
Cdd:cd14111   2 QKPYTFLDEKARGRFGVI----RRCRENATGKNFPAK--IVPYQAEEKQGVLQEYEILKSLHHER-IMALHEAYITPRYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERP------YPCIDMFDFikgqgkiSEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA 181
Cdd:cd14111  75 VLIAEFCsgkellHSLIDRFRY-------SEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVT-NLNAIKIVDFGSA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 T-----VLRrsQYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICT-AHLLG----PLPFF 251
Cdd:cd14111 147 QsfnplSLR--QLGRRTGTLEYMAPE-MVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETeAKILVakfdAFKLY 223
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 252 VPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14111 224 PNVSQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
30-273 6.10e-14

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: 71.60  E-value: 6.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsnVKEWARINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd08228   3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQ---IFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYP--CIDMFDFIKGQGK-ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVL-- 184
Cdd:cd08228  80 VLELADAgdLSQMIKYFKKQKRlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFIT-ATGVVKLGDLGLGRFFss 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYSDFQGTRLYCPPEWfLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK----DICTAHL---LGPLPfFVPVSAE 257
Cdd:cd08228 159 KTTAAHSLVGTPYYMSPER-IHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKmnlfSLCQKIEqcdYPPLP-TEHYSEK 236
                       250
                ....*....|....*.
gi 25143934 258 VKDLISKCLTFDPFQR 273
Cdd:cd08228 237 LRELVSMCIYPDPDQR 252
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
37-329 9.40e-14

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: 71.95  E-value: 9.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARIngEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERPYP 116
Cdd:cd05616   8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDV--ECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA--TVLRRSQYSDFQG 194
Cdd:cd05616  86 G-DLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLD-SEGHIKIADFGMCkeNIWDGVTTKTFCG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 195 TRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLLGPLPFFVPVSAEVKDLISKcltf 268
Cdd:cd05616 164 TPDYIAPEIIAYQPY-GKSVDWWAFGVLLYEMLAGQAPFEGEdedelfQSIMEHNVAYPKSMSKEAVAICKGLMTK---- 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 269 DPFQR--CSLEA---ILNHPWVKQqtLSWDALTKNKVQKKTSESSDDHHSETLgdhsETEEDRSPP 329
Cdd:cd05616 239 HPGKRlgCGPEGerdIKEHAFFRY--IDWEKLERKEIQPPYKPKACGRNAENF----DRFFTRHPP 298
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
131-300 9.89e-14

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: 71.96  E-value: 9.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 131 SEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT--VLRRSQYSDFQGTRLYCPPEWFLHSL 208
Cdd:cd05595  93 TEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLD-KDGHIKITDFGLCKegITDGATMKTFCGTPEYLAPEVLEDND 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 209 YlGREAAVWSLGVLLYNSLNGRLPFRNE--KDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQRC-----SLEAILN 281
Cdd:cd05595 172 Y-GRAVDWWGLGVVMYEMMCGRLPFYNQdhERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLgggpsDAKEVME 250
                       170
                ....*....|....*....
gi 25143934 282 HPWVkqQTLSWDALTKNKV 300
Cdd:cd05595 251 HRFF--LSINWQDVVQKKL 267
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
37-300 9.97e-14

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: 71.92  E-value: 9.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNV---KEWARINGEQvpmeiCMLAKCSKVRGVIRLLDWYSIPEGFLIVMER 113
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTIlkkKEQNHIMAER-----NVLLKNLKHPFLVGLHYSFQTSEKLYFVLDY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 PYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT--VLRRSQYSD 191
Cdd:cd05603  78 VNGG-ELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLD-CQGHVVLTDFGLCKegMEPEETTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPVSAEVKDLISKCLTFD 269
Cdd:cd05603 156 FCGTPEYLAPEVLRKEPY-DRTVDWWCLGAVLYEMLYGLPPFysRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKD 234
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 270 pfQRCSLEAILNHPWVKQQT----LSWDALTKNKV 300
Cdd:cd05603 235 --QRRRLGAKADFLEIKNHVffspINWDDLYHKRI 267
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
36-287 1.06e-13

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: 71.30  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIERS-NVKEWARINGEqvpMEICMLAKCskvrgVIRLLDWYS--IPEG-FLIVM 111
Cdd:cd06617   8 ELGRGAYGVVDKMRHVPTGTIMAVKRIRATvNSQEQKRLLMD---LDISMRSVD-----CPYTVTFYGalFREGdVWICM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 ERPYPCIDMF--DFIKGQGKISEDmarfLFRQIAVTV-------HEcvQNRVLHRDLKDENIVIDLvTGSTKLIDFGAAT 182
Cdd:cd06617  80 EVMDTSLDKFykKVYDKGLTIPED----ILGKIAVSIvkaleylHS--KLSVIHRDVKPSNVLINR-NGQVKLCDFGISG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRSQYSDFQ-GTRLYCPPEWF---LHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDI---CTAHLLGPLPFFV--P 253
Cdd:cd06617 153 YLVDSVAKTIDaGCKPYMAPERInpeLNQKGYDVKSDVWSLGITMIELATGRFPYDSWKTPfqqLKQVVEEPSPQLPaeK 232
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 254 VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06617 233 FSPEFQDFVNKCLKKNYKERPNYPELLQHPFFEL 266
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
37-279 1.10e-13

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 70.54  E-value: 1.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAvrTCDNALVAVKFIERSNVKEWARIngeqvpmEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMERPyP 116
Cdd:cd14058   1 VGRGSFGVVCKA--RWRNQIVAVKIIESESEKKAFEV-------EVRQLSRVDH-PNIIKLYGACSNQKPVCLVMEYA-E 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIKGQG-----KISEDMARFLfrQIAVTV---HECVQNRVLHRDLKDENIVidLVTGST--KLIDFGAATVLrR 186
Cdd:cd14058  70 GGSLYNVLHGKEpkpiyTAAHAMSWAL--QCAKGVaylHSMKPKALIHRDLKPPNLL--LTNGGTvlKICDFGTACDI-S 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRnekdictaHLLGPLPFFV---------PVSAE 257
Cdd:cd14058 145 THMTNNKGSAAWMAPEVFEGSKY-SEKCDVFSWGIILWEVITRRKPFD--------HIGGPAFRIMwavhngerpPLIKN 215
                       250       260
                ....*....|....*....|....*.
gi 25143934 258 ----VKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd14058 216 cpkpIESLMTRCWSKDPEKRPSMKEI 241
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
129-282 1.15e-13

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


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 71.28  E-value: 1.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 129 KISEDMARFLFRQIaVTVHECVQNR-VLHRDLKDENIVIDLVTGSTKLIDF--GAATVLRRSQYSDFQGTRLYCPPEWFL 205
Cdd:cd13974 128 RLSEREALVIFYDV-VRVVEALHKKnIVHRDLKLGNMVLNKRTRKITITNFclGKHLVSEDDLLKDQRGSPAYISPDVLS 206
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 206 HSLYLGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLLgpLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd13974 207 GKPYLGKPSDMWALGVVLFTMLYGQFPFYDSipqelfRKIKAAEYT--IPEDGRVSENTVCLIRKLLVLNPQKRLTASEV 284

                ...
gi 25143934 280 LNH 282
Cdd:cd13974 285 LDS 287
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
25-224 1.52e-13

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: 70.67  E-value: 1.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  25 SKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvKEWARingEQVPMEICMLAKCSKvRGVIRLLD-WYSI 103
Cdd:cd14048   2 SRFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPN-NELAR---EKVLREVRALAKLDH-PGIVRYFNaWLER 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 -PEGFLIVMERPYPCIDM--------FDFIKGQGKIsEDMARF----LFRQIAVTVhECVQNR-VLHRDLKDENIVIDLv 169
Cdd:cd14048  77 pPEGWQEKMDEVYLYIQMqlcrkenlKDWMNRRCTM-ESRELFvclnIFKQIASAV-EYLHSKgLIHRDLKPSNVFFSL- 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 170 TGSTKLIDFGAAT----------VLRRSQYSDFQ----GTRLYCPPEWFLHSLYlGREAAVWSLGVLLY 224
Cdd:cd14048 154 DDVVKVGDFGLVTamdqgepeqtVLTPMPAYAKHtgqvGTRLYMSPEQIHGNQY-SEKVDIFALGLILF 221
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
49-285 1.60e-13

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: 70.57  E-value: 1.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  49 VRTCdnalvavkfIERSNVKEWA---RINGEQVPMEICMLAKCSKVRGVIRLLDWY---------SIPEG-FLIVMERpY 115
Cdd:cd14171  22 VRVC---------VKKSTGERFAlkiLLDRPKARTEVRLHMMCSGHPNIVQIYDVYansvqfpgeSSPRArLLIVMEL-M 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI-DLVTGST-KLIDFGAATV----LRRSQY 189
Cdd:cd14171  92 EGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkDNSEDAPiKLCDFGFAKVdqgdLMTPQF 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 sdfqgTRLYCPPEWFLHSLYLGREAA----------------VWSLGVLLYNSLNGRLPFRNE-----------KDICTA 242
Cdd:cd14171 172 -----TPYYVAPQVLEAQRRHRKERSgiptsptpytydkscdMWSLGVIIYIMLCGYPPFYSEhpsrtitkdmkRKIMTG 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 25143934 243 HLLGPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14171 247 SYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
30-284 2.21e-13

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: 70.15  E-value: 2.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewariNGEQVP----MEICMLaKCSKVRGVIRLLDWYSIPE 105
Cdd:cd07839   1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDD-------DDEGVPssalREICLL-KELKHKNIVRLYDVLHSDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMErpYPCIDMFDFIKG-QGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAtvl 184
Cdd:cd07839  73 KLTLVFE--YCDQDLKKYFDScNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLIN-KNGELKLADFGLA--- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 rRS------QYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLP--------------FR-----NEKDI 239
Cdd:cd07839 147 -RAfgipvrCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPlfpgndvddqlkriFRllgtpTEESW 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 240 CTAHLLGPLPFFVPV-------------SAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07839 226 PGVSKLPDYKPYPMYpattslvnvvpklNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
30-301 2.23e-13

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: 70.80  E-value: 2.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARIngEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd05615  11 DFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDV--ECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT--VLRRS 187
Cdd:cd05615  89 VMEYVNGG-DLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLD-SEGHIKIADFGMCKehMVEGV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 QYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPVSAEVKDLISKC 265
Cdd:cd05615 167 TTRTFCGTPDYIAPEIIAYQPY-GRSVDWWAYGVLLYEMLAGQPPFdgEDEDELFQSIMEHNVSYPKSLSKEAVSICKGL 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25143934 266 LTFDPFQR--CSLEA---ILNHPWVKQqtLSWDALTKNKVQ 301
Cdd:cd05615 246 MTKHPAKRlgCGPEGerdIREHAFFRR--IDWDKLENREIQ 284
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
32-289 2.71e-13

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: 69.75  E-value: 2.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAELGRGGFGVVYRAVRTcdNALVAVKFIERSNvKEWARINGEQVPMEICMLaKCSKVRGVIRLLD-WYSIPEGfliv 110
Cdd:cd14031  13 KFDIELGRGAFKTVYKGLDT--ETWVEVAWCELQD-RKLTKAEQQRFKEEAEML-KGLQHPNIVRFYDsWESVLKG---- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 merpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQ------------NRVLHRDLKDENIVIDLVTGSTKLIDF 178
Cdd:cd14031  85 ----KKCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQilkglqflhtrtPPIIHRDLKCDNIFITGPTGSVKIGDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 GAATVLRRSQYSDFQGTRLYCPPEwfLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHL-----LGPLPFFVP 253
Cdd:cd14031 161 GLATLMRTSFAKSVIGTPEFMAPE--MYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRkvtsgIKPASFNKV 238
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 25143934 254 VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQT 289
Cdd:cd14031 239 TDPEVKEIIEGCIRQNKSERLSIKDLLNHAFFAEDT 274
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
30-284 2.73e-13

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: 69.84  E-value: 2.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersnvkewaRINGEQ--VP----MEICMLaKCSKVRGVIRLLDWYSI 103
Cdd:cd07860   1 NFQKVEKIGEGTYGVVYKARNKLTGEVVALKKI---------RLDTETegVPstaiREISLL-KELNHPNIVKLLDVIHT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 PEGFLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT- 182
Cdd:cd07860  71 ENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLIN-TEGAIKLADFGLARa 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 --VLRRSqYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTA----HLLG---------- 246
Cdd:cd07860 150 fgVPVRT-YTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLfrifRTLGtpdevvwpgv 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 247 ----------------PLPFFVP-VSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07860 229 tsmpdykpsfpkwarqDFSKVVPpLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
29-287 4.34e-13

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: 69.89  E-value: 4.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVK-----FIERSNVKEWARingeqvpmEICMLAKCSKVRGVIRLL----- 98
Cdd:cd07852   7 RRYEILKKLGKGAYGIVWKAIDKKTGEVVALKkifdaFRNATDAQRTFR--------EIMFLQELNDHPNIIKLLnvira 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  99 ----DWYSIPEgfliVMErpypcIDMFDFIKGqgKISEDM-ARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGST 173
Cdd:cd07852  79 endkDIYLVFE----YME-----TDLHAVIRA--NILEDIhKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLN-SDCRV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 174 KLIDFG-AATVLRRSQYS------DFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR---------------- 230
Cdd:cd07852 147 KLADFGlARSLSQLEEDDenpvltDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKplfpgtstlnqlekii 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143934 231 --LPFRNEKDI------CTAHLLGPLP---------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd07852 227 evIGRPSAEDIesiqspFAATMLESLPpsrpksldeLFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
37-301 4.78e-13

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: 69.73  E-value: 4.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVkewarINGEQVpmEICMLAKcskvrgviRLLDWYSIPEgFLI------- 109
Cdd:cd05587   4 LGKGSFGKVMLAERKGTDELYAIKILKKDVI-----IQDDDV--ECTMVEK--------RVLALSGKPP-FLTqlhscfq 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCID-------MFDfIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT 182
Cdd:cd05587  68 TMDRLYFVMEyvnggdlMYH-IQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLD-AEGHIKIADFGMCK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 --VLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPVSAEV 258
Cdd:cd05587 146 egIFGGKTTRTFCGTPDYIAPEIIAYQPY-GKSVDWWAYGVLLYEMLAGQPPFdgEDEDELFQSIMEHNVSYPKSLSKEA 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 25143934 259 KDLISKCLTFDPFQR--CSLEA---ILNHPWVKqqTLSWDALTKNKVQ 301
Cdd:cd05587 225 VSICKGLLTKHPAKRlgCGPTGerdIKEHPFFR--RIDWEKLERREIQ 270
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
32-281 4.82e-13

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: 68.73  E-value: 4.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934     32 KLKAELGRGGFGVVYRAVRTCDNA----LVAVKFI----ERSNVKEWARingeqvpmEICMLAKCSKvRGVIRLLDWYSI 103
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKGDgkevEVAVKTLkedaSEQQIEEFLR--------EARIMRKLDH-PNIVKLLGVCTE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    104 PEGFLIVMErpY-PCIDMFDFIKGQGK--IS-EDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG 179
Cdd:smart00221  73 EEPLMIVME--YmPGGDLLDYLRKNRPkeLSlSDLLSFAL-QIARGMEYLESKNFIHRDLAARNCLVG-ENLVVKISDFG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    180 AATVLRRSQYSDFQGTRL---YCPPEWFLHSLYlgREAA-VWSLGVLLYNSL-NGRLPFRNEKDICTAHLLG-----PLP 249
Cdd:smart00221 149 LSRDLYDDDYYKVKGGKLpirWMAPESLKEGKF--TSKSdVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLKkgyrlPKP 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 25143934    250 FFVPvsAEVKDLISKCLTFDPFQRCSLEAILN 281
Cdd:smart00221 227 PNCP--PELYKLMLQCWAEDPEDRPTFSELVE 256
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
37-301 5.28e-13

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: 69.59  E-value: 5.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVrgVIRLLDWYSIPEGFLIVMERPYP 116
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAWENPF--LTHLYCTFQTKEHLFFVMEFLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDfIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAA--TVLRRSQYSDFQG 194
Cdd:cd05620  81 GDLMFH-IQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDR-DGHIKIADFGMCkeNVFGDNRASTFCG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 195 TRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFR-NEKDICTAHLLGPLPFFvP--VSAEVKDLISKCLTFDPF 271
Cdd:cd05620 159 TPDYIAPE-ILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHgDDEDELFESIRVDTPHY-PrwITKESKDILEKLFERDPT 236
                       250       260       270
                ....*....|....*....|....*....|.
gi 25143934 272 QRCSLEA-ILNHPWVKqqTLSWDALTKNKVQ 301
Cdd:cd05620 237 RRLGVVGnIRGHPFFK--TINWTALEKRELD 265
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
30-237 5.63e-13

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: 68.64  E-value: 5.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKfIERSNVKEwaringEQVPMEICMLAKCSKVRGVIRLLdWYSIPEGF-L 108
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIK-IEKKDSKH------PQLEYEAKVYKLLQGGPGIPRLY-WFGQEGDYnV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERPYPciDMFD-FIKGQGKISEDMARFLFRQIAVTVhECVQNR-VLHRDLKDENIVIDLVTGSTK--LIDFGAATVL 184
Cdd:cd14016  73 MVMDLLGP--SLEDlFNKCGRKFSLKTVLMLADQMISRL-EYLHSKgYIHRDIKPENFLMGLGKNSNKvyLIDFGLAKKY 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 185 RRSQ------YSD---FQGTRLYCPpewfLHSLyLGREAA----VWSLG-VLLYnSLNGRLPFRNEK 237
Cdd:cd14016 150 RDPRtgkhipYREgksLTGTARYAS----INAH-LGIEQSrrddLESLGyVLIY-FLKGSLPWQGLK 210
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
94-286 7.10e-13

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: 68.24  E-value: 7.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  94 VIRLLDWYSIPEGFLIVMErpypcidmfdFIKG--------QGKISEDmarflfrQIAVTVHECVQ-------NRVLHRD 158
Cdd:cd06648  66 IVEMYSSYLVGDELWVVME----------FLEGgaltdivtHTRMNEE-------QIATVCRAVLKalsflhsQGVIHRD 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 159 LKDENIVIDLvTGSTKLIDFGAATVL------RRSqysdFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLP 232
Cdd:cd06648 129 IKSDSILLTS-DGRVKLSDFGFCAQVskevprRKS----LVGTPYWMAPEVISRLPY-GTEVDIWSLGIMVIEMVDGEPP 202
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 233 FRNEKDICTAHLL--GPLPFF---VPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06648 203 YFNEPPLQAMKRIrdNEPPKLknlHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
30-300 7.44e-13

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 68.87  E-value: 7.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVY--RAVRTCDNA-LVAVKFIERSNVKEWARiNGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEG 106
Cdd:cd05613   1 NFELLKVLGTGAYGKVFlvRKVSGHDAGkLYAMKVLKKATIVQKAK-TAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMerpypcidmfDFIKGqGKISEDMA---RFLFRQIAVTVHECV-------QNRVLHRDLKDENIVIDlVTGSTKLI 176
Cdd:cd05613  80 LHLIL----------DYING-GELFTHLSqreRFTENEVQIYIGEIVlalehlhKLGIIYRDIKLENILLD-SSGHVVLT 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAATVLRRSQYS---DFQGTRLYCPPEwFLHSLYLGREAAV--WSLGVLLYNSLNGRLPF------RNEKDICTAHLL 245
Cdd:cd05613 148 DFGLSKEFLLDENEraySFCGTIEYMAPE-IVRGGDSGHDKAVdwWSLGVLMYELLTGASPFtvdgekNSQAEISRRILK 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 246 GPLPFFVPVSAEVKDLISKCLTFDPFQRC-----SLEAILNHPWVkqQTLSWDALTKNKV 300
Cdd:cd05613 227 SEPPYPQEMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFF--QKINWDDLAAKKV 284
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
37-273 8.01e-13

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: 68.25  E-value: 8.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVK--------FIERSNVKEWARIngeqvpMEIcmlakcSKVRGVIRLLDWYSIPEGFL 108
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKclhsspncIEERKALLKEAEK------MER------ARHSYVLPLLGVCVERRSLG 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMErpYpcIDMFDFIKGQGKISEDMA---RF-LFRQIAVTVH--ECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT 182
Cdd:cd13978  69 LVME--Y--MENGSLKSLLEREIQDVPwslRFrIIHEIALGMNflHNMDPPLLHHDLKPENILLD-NHFHVKISDFGLSK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VL-------RRSQYSDFQGTRLYCPPEWFLHSLYLGREAA-VWSLGVLLYNSLNGRLPFRNEKDICTAHL---------L 245
Cdd:cd13978 144 LGmksisanRRRGTENLGGTPIYMAPEAFDDFNKKPTSKSdVYSFAIVIWAVLTRKEPFENAINPLLIMQivskgdrpsL 223
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 246 GPL--PFFVPVSAEVKDLISKCLTFDPFQR 273
Cdd:cd13978 224 DDIgrLKQIENVQELISLMIRCWDGNPDAR 253
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
25-282 8.04e-13

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: 68.29  E-value: 8.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  25 SKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsnvkewarINGEQVPMEICMLAKCSKVRGVIRLLDWysip 104
Cdd:cd14047   2 ERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK---------LNNEKAEREVKALAKLDHPNIVRYNGCW---- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVME----------RPYPCIDMfDFI-----------KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDEN 163
Cdd:cd14047  69 DGFDYDPEtsssnssrskTKCLFIQM-EFCekgtleswiekRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSN 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 164 IVIDlVTGSTKLIDFGAATVLRRS-QYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTA 242
Cdd:cd14047 148 IFLV-DTGKVKIGDFGLVTSLKNDgKRTKSKGTLSYMSPEQISSQDY-GKEVDIYALGLILFELLHVCDSAFEKSKFWTD 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 25143934 243 HLLGPLP--FFVPVSAEVKdLISKCLTFDPFQRCSLEAILNH 282
Cdd:cd14047 226 LRNGILPdiFDKRYKIEKT-IIKKMLSKKPEDRPNASEILRT 266
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
32-282 8.68e-13

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: 67.91  E-value: 8.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    32 KLKAELGRGGFGVVYRAVRTCD----NALVAVKFI-ERSNVKEWaringEQVPMEICMLAKCSKVRgVIRLLDWYSIPEG 106
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTLKGEgentKIKVAVKTLkEGADEEER-----EDFLEEASIMKKLDHPN-IVKLLGVCTQGEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   107 FLIVMErpY-PCIDMFDFIKGQG-KIS-EDMARFLfRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFG-AAT 182
Cdd:pfam07714  76 LYIVTE--YmPGGDLLDFLRKHKrKLTlKDLLSMA-LQIAKGMEYLESKNFVHRDLAARNCLVSE-NLVVKISDFGlSRD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   183 VLRRSQYSDFQGTRL---YCPPEWFLHSLYlgREAA-VWSLGVLLYNSL-NGRLPFRNEKDICTAHLL---GPLPFFVPV 254
Cdd:pfam07714 152 IYDDDYYRKRGGGKLpikWMAPESLKDGKF--TSKSdVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLedgYRLPQPENC 229
                         250       260
                  ....*....|....*....|....*...
gi 25143934   255 SAEVKDLISKCLTFDPFQRCSLEAILNH 282
Cdd:pfam07714 230 PDELYDLMKQCWAYDPEDRPTFSELVED 257
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
119-273 9.07e-13

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: 68.95  E-value: 9.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT--VLRRSQYSDFQGTR 196
Cdd:cd05593 101 ELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLD-KDGHIKITDFGLCKegITDAATMKTFCGTP 179
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 197 LYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE--KDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQR 273
Cdd:cd05593 180 EYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQdhEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPNKR 257
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
31-223 9.85e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 68.90  E-value: 9.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARingeQVPMEICMLAKCSKVRGvirllDWYSIPEGFLIV 110
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILK--NHPSYAR----QGQIEVGILARLSNENA-----DEFNFVRAYECF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERPYPCI-------DMFDFIKgQGKISE---DMARFLFRQIAVTVHECVQNRVLHRDLKDENI-VIDLVTG--STKLID 177
Cdd:cd14229  71 QHRNHTCLvfemleqNLYDFLK-QNKFSPlplKVIRPILQQVATALKKLKSLGLIHADLKPENImLVDPVRQpyRVKVID 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 25143934 178 FGAATVLRRSQYSDFQGTRLYCPPEWFLhSLYLGREAAVWSLGVLL 223
Cdd:cd14229 150 FGSASHVSKTVCSTYLQSRYYRAPEIIL-GLPFCEAIDMWSLGCVI 194
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
31-286 9.92e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 68.31  E-value: 9.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkewariNGEQVP----MEICMLaKCSKVRGVIRLLDWYSIPEG 106
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQ-------EDEGVPstaiREISLL-KEMQHGNIVRLQDVVHSEKR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  107 FLIVMErpYPCIDMFDFIKGQGKISED--MARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATV- 183
Cdd:PLN00009  76 LYLVFE--YLDLDLKKHMDSSPDFAKNprLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALKLADFGLARAf 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  184 -LRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH----LLG-----------P 247
Cdd:PLN00009 154 gIPVRTFTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFkifrILGtpneetwpgvtS 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 25143934  248 LPFF---------------VP-VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:PLN00009 234 LPDYksafpkwppkdlatvVPtLEPAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
130-329 1.08e-12

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 68.94  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 130 ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGA-----ATVLRRSQYSdfQGTRLYCPPEWF 204
Cdd:cd05596 122 VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLD-ASGHLKLADFGTcmkmdKDGLVRSDTA--VGTPDYISPEVL 198
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 205 L---HSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICT--------AHLLGPLPffVPVSAEVKDLISKCLTfDPFQR 273
Cdd:cd05596 199 KsqgGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTygkimnhkNSLQFPDD--VEISKDAKSLICAFLT-DREVR 275
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143934 274 C---SLEAILNHPWVKQQTLSWDAL--TKNKVQKKTSESSDDHHSETLGDHSETEEDRSPP 329
Cdd:cd05596 276 LgrnGIEEIKAHPFFKNDQWTWDNIreTVPPVVPELSSDIDTSNFDDIEEDETPEETFPVP 336
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
29-282 1.12e-12

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: 67.75  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAvrTCDNALVAVKfIERSNVKEWARINGEQVPMEICMLAkcskvrgvirLLDWYSIPEGFL 108
Cdd:cd14147   3 QELRLEEVIGIGGFGKVYRG--SWRGELVAVK-AARQDPDEDISVTAESVRQEARLFA----------MLAHPNIIALKA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERPYPCIDMfDFIKGqGKISEDMARflfRQIA--VTVHECVQNR-------------VLHRDLKDENIVI------- 166
Cdd:cd14147  70 VCLEEPNLCLVM-EYAAG-GPLSRALAG---RRVPphVLVNWAVQIArgmhylhcealvpVIHRDLKSNNILLlqpiend 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 167 DLVTGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH--- 243
Cdd:cd14147 145 DMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPE-VIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYgva 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 25143934 244 ---LLGPLPFFVPvsAEVKDLISKCLTFDPFQRCSLEAILNH 282
Cdd:cd14147 224 vnkLTLPIPSTCP--EPFAQLMADCWAQDPHRRPDFASILQQ 263
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
31-288 1.15e-12

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: 68.21  E-value: 1.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringEQVPMEICMLAKCSKVRGVIRLLDWY------SIP 104
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEE------EEIKQEINMLKKYSHHRNIATYYGAFikknppGMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVME--RPYPCIDMFDFIKGQgKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT 182
Cdd:cd06637  82 DQLWLVMEfcGAGSVTDLIKNTKGN-TLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT-ENAEVKLVDFGVSA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRS--QYSDFQGTRLYCPPEWFL----HSLYLGREAAVWSLGVLLYNSLNGRLPfrnekdICTAHLLGPLpFFVPV-- 254
Cdd:cd06637 160 QLDRTvgRRNTFIGTPYWMAPEVIAcdenPDATYDFKSDLWSLGITAIEMAEGAPP------LCDMHPMRAL-FLIPRnp 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 25143934 255 ---------SAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQ 288
Cdd:cd06637 233 aprlkskkwSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQ 275
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
30-310 1.33e-12

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 68.41  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVkewarINGEQVpmeicmlaKCSKVRGVIRLLDW--------- 100
Cdd:cd05619   6 DFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVV-----LMDDDV--------ECTMVEKRVLSLAWehpflthlf 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 101 --YSIPEGFLIVMERPYPCIDMFDfIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDF 178
Cdd:cd05619  73 ctFQTKENLFFVMEYLNGGDLMFH-IQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDK-DGHIKIADF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 179 GAA--TVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVP--V 254
Cdd:cd05619 151 GMCkeNMLGDAKTSTFCGTPDYIAPEILLGQKY-NTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPrwL 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 255 SAEVKDLISKCLTFDPFQRCSLEA-ILNHPWVKQqtLSWDALTKNKVQ---KKTSESSDD 310
Cdd:cd05619 230 EKEAKDILVKLFVREPERRLGVRGdIRQHPFFRE--INWEALEEREIEppfKPKVKSPFD 287
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
36-286 2.09e-12

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 67.46  E-value: 2.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIERSnVKEWARingEQVPMEICMLAKCSKVRGVIRLLDWYSIPEgFLIVMERpy 115
Cdd:cd06615   8 ELGAGNGGVVTKVLHRPSGLIMARKLIHLE-IKPAIR---NQIIRELKVLHECNSPYIVGFYGAFYSDGE-ISICMEH-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pcID--MFDFI-KGQGKISEDmarFLFRqIAVTVHECV-----QNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS 187
Cdd:cd06615  81 --MDggSLDQVlKKAGRIPEN---ILGK-ISIAVLRGLtylreKHKIMHRDVKPSNILVN-SRGEIKLCDFGVSGQLIDS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 QYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF-------------RNEKDICTAHLLGPLPFFVP- 253
Cdd:cd06615 154 MANSFVGTRSYMSPERLQGTHY-TVQSDIWSLGLSLVEMAIGRYPIpppdakeleamfgRPVSEGEAKESHRPVSGHPPd 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 254 --------------------------VSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06615 233 sprpmaifelldyivnepppklpsgaFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
31-285 2.19e-12

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: 67.34  E-value: 2.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringEQVPMEICMLAKCSKVRGVIRLLDWY--SIPEG-- 106
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE------EEIKLEINMLKKYSHHRNIATYYGAFikKSPPGhd 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 --FLIVME--RPYPCIDMFDFIKGQGkISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT 182
Cdd:cd06636  92 dqLWLVMEfcGAGSVTDLVKNTKGNA-LKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT-ENAEVKLVDFGVSA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRS--QYSDFQGTRLYCPPEWFL-----HSLYLGReAAVWSLGVLLYNSLNGRLPfrnekdICTAHLLGPLpFFVPV- 254
Cdd:cd06636 170 QLDRTvgRRNTFIGTPYWMAPEVIAcdenpDATYDYR-SDIWSLGITAIEMAEGAPP------LCDMHPMRAL-FLIPRn 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25143934 255 ----------SAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06636 242 pppklkskkwSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
38-280 2.47e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 66.52  E-value: 2.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  38 GRGGFGVVYRAVRTCDNALVAVKfiersnvkewaRINgeQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMERPyPC 117
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVK-----------KLL--KIEKEAEILSVLSH-RNIIQFYGAILEAPNYGIVTEYA-SY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 118 IDMFDFIKGQGKISEDMARFLF--RQIAVT---VHECVQNRVLHRDLKDENIVIdLVTGSTKLIDFGAATVLRRSQYSDF 192
Cdd:cd14060  67 GSLFDYLNSNESEEMDMDQIMTwaTDIAKGmhyLHMEAPVKVIHRDLKSRNVVI-AADGVLKICDFGASRFHSHTTHMSL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 193 QGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL---GPLPfFVPVS--AEVKDLISKCLT 267
Cdd:cd14060 146 VGTFPWMAPE-VIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVvekNERP-TIPSScpRSFAELMRRCWE 223
                       250
                ....*....|...
gi 25143934 268 FDPFQRCSLEAIL 280
Cdd:cd14060 224 ADVKERPSFKQII 236
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
31-285 2.65e-12

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: 66.76  E-value: 2.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCsKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKER---EESRKEVAVLSKM-KHPNIVQYQESFEENGNLYIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpypCI--DMFDFIKGQGKI--SEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIdLVTGSTKLIDFGAATVLRR 186
Cdd:cd08218  78 MDY---CDggDLYKRINAQRGVlfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFL-TKDGIIKLGDFGIARVLNS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQ--YSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFR--NEKDICTAHLLGPLPffvPV----SAEV 258
Cdd:cd08218 154 TVelARTCIGTPYYLSPEICENKPY-NNKSDIWALGCVLYEMCTLKHAFEagNMKNLVLKIIRGSYP---PVpsrySYDL 229
                       250       260
                ....*....|....*....|....*..
gi 25143934 259 KDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd08218 230 RSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
24-284 2.77e-12

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: 67.06  E-value: 2.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  24 FSKFKKnyklkaeLGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEwaringEQVP----MEICMLaKCSKVRGVIRLLD 99
Cdd:cd07861   2 YTKIEK-------IGEGTYGVVYKGRNKKTGQIVAMKKI-RLESEE------EGVPstaiREISLL-KELQHPNIVCLED 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 100 WYSIPEGFLIVMErpYPCIDM---FDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLI 176
Cdd:cd07861  67 VLMQENRLYLVFE--FLSMDLkkyLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLID-NKGVIKLA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGaatvLRRS------QYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTA----HLLG 246
Cdd:cd07861 144 DFG----LARAfgipvrVYTHEVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLfrifRILG 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 247 -----------PLPFFVP---------VSAEVK-------DLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07861 220 tptediwpgvtSLPDYKNtfpkwkkgsLRTAVKnldedglDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
36-297 4.13e-12

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: 66.25  E-value: 4.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIERsnvkEWARINGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIVMER-- 113
Cdd:cd06641  11 KIGKGSFGEVFKGIDNRTQKVVAIKIIDL----EEAEDEIEDIQQEITVLSQCDSPY-VTKYYGSYLKDTKLWIIMEYlg 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 PYPCIDMFDfikgQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQY--SD 191
Cdd:cd06641  86 GGSALDLLE----PGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLS-EHGEVKLADFGVAGQLTDTQIkrN* 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNekdictahlLGPLP--FFVP----------VSAEVK 259
Cdd:cd06641 161 FVGTPFWMAPEVIKQSAY-DSKADIWSLGITAIELARGEPPHSE---------LHPMKvlFLIPknnpptlegnYSKPLK 230
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWVKQQTLSWDALTK 297
Cdd:cd06641 231 EFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTE 268
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
35-285 4.59e-12

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: 66.02  E-value: 4.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  35 AELGRGGFGVVYRAVRTCDNALVAVKFIERSNV----KEWARINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIV 110
Cdd:cd06628   6 ALIGSGSFGSVYLGMNASSGELMAVKQVELPSVsaenKDRKKSMLDALQREIALLRELQH-ENIVQYLGSSSDANHLNIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFIKGQGKISEDMARFLFRQIaVTVHECVQNR-VLHRDLKDENIVIDlVTGSTKLIDFGAATVL----- 184
Cdd:cd06628  85 LEY-VPGGSVATLLNNYGAFEESLVRNFVRQI-LKGLNYLHNRgIIHRDIKGANILVD-NKGGIKISDFGISKKLeansl 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 ---RRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGP--LPFFVP-VSAEV 258
Cdd:cd06628 162 stkNNGARPSLQGSVFWMAPEVVKQTSY-TRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGEnaSPTIPSnISSEA 240
                       250       260
                ....*....|....*....|....*..
gi 25143934 259 KDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06628 241 RDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
37-286 4.61e-12

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: 66.73  E-value: 4.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAV-RTCDNAlVAVKFI---ERSNVKEWARingeqvpmEICMLAKCS-----KVRGVI-----RLLDWYS 102
Cdd:cd07854  13 LGCGSNGLVFSAVdSDCDKR-VAVKKIvltDPQSVKHALR--------EIKIIRRLDhdnivKVYEVLgpsgsDLTEDVG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 103 IPEGF---LIVMErpYPCIDMFDFIKgQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFG 179
Cdd:cd07854  84 SLTELnsvYIVQE--YMETDLANVLE-QGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVLKIGDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVLrRSQYSD----FQG--TRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR------------------LPFRN 235
Cdd:cd07854 161 LARIV-DPHYSHkgylSEGlvTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKplfagaheleqmqlilesVPVVR 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 236 EKDicTAHLLGPLPFFV----------------PVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd07854 240 EED--RNELLNVIPSFVrndggeprrplrdllpGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
131-273 4.66e-12

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: 66.98  E-value: 4.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 131 SEDMARFLFRQIAVTV-HECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT--VLRRSQYSDFQGTRLYCPPEWFLHS 207
Cdd:cd05594 123 SEDRARFYGAEIVSALdYLHSEKNVVYRDLKLENLMLD-KDGHIKITDFGLCKegIKDGATMKTFCGTPEYLAPEVLEDN 201
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 208 LYlGREAAVWSLGVLLYNSLNGRLPFRNE--KDICTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQR 273
Cdd:cd05594 202 DY-GRAVDWWGLGVVMYEMMCGRLPFYNQdhEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDPKQR 268
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
37-283 4.66e-12

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 65.91  E-value: 4.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFG--VVYRavRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCSKVrGVIRLLDWYSIPEGFLIVMERp 114
Cdd:cd08221   8 LGRGAFGeaVLYR--KTEDNSLVVWKEVNLSRLSEKER---RDALNEIDILSLLNHD-NIITYYNHFLDGESLFIEMEY- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 115 ypCI--DMFDFIKGQGK--ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVL-RRSQY 189
Cdd:cd08221  81 --CNggNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLT-KADLVKLGDFGISKVLdSESSM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SD-FQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFR--NEKDICTAHLLGPLPFFVPV-SAEVKDLISKC 265
Cdd:cd08221 158 AEsIVGTPYYMSPELVQGVKY-NFKSDIWAVGCVLYELLTLKRTFDatNPLRLAVKIVQGEYEDIDEQySEEIIQLVHDC 236
                       250
                ....*....|....*...
gi 25143934 266 LTFDPFQRCSLEAILNHP 283
Cdd:cd08221 237 LHQDPEDRPTAEELLERP 254
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
29-285 4.81e-12

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 66.02  E-value: 4.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAV--RTCDNALVAVKFIERSNvkewariNGEQVPMEICMLAKCSKVRgVIRLLDWYSiPEG 106
Cdd:cd14112   3 GRFSFGSEIFRGRFSVIVKAVdsTTETDAHCAVKIFEVSD-------EASEAVREFESLRTLQHEN-VQRLIAAFK-PSN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLI-VMERPYPciDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTG-STKLIDFGAATVL 184
Cdd:cd14112  74 FAYlVMEKLQE--DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSwQVKLVDFGRAQKV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDI------------CTAHLLgplpfFV 252
Cdd:cd14112 152 SKLGKVPVDGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDeeetkenvifvkCRPNLI-----FV 226
                       250       260       270
                ....*....|....*....|....*....|...
gi 25143934 253 PVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14112 227 EATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
30-273 4.85e-12

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


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 65.99  E-value: 4.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNA-LVAVKFIE------RSNVKEWARINGEQVPmEICMLAKCSKVRGVIRLLDWYS 102
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKVRKKSNGQtLLALKEINmtnpafGRTEQERDKSVGDIIS-EVNIIKEQLRHPNIVRYYKTFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 103 IPEGFLIVME--RPYPCIDMFDFIKGQ-GKISEDMARFLFRQIAVTV---HEcvQNRVLHRDLKDENIVI---DLVTgst 173
Cdd:cd08528  80 ENDRLYIVMEliEGAPLGEHFSSLKEKnEHFTEDRIWNIFVQMVLALrylHK--EKQIVHRDLKPNNIMLgedDKVT--- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 174 kLIDFGAATVLRR--SQYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL-----G 246
Cdd:cd08528 155 -ITDFGLAKQKGPesSKMTSVVGTILYSCPE-IVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIveaeyE 232
                       250       260
                ....*....|....*....|....*..
gi 25143934 247 PLPFFVpVSAEVKDLISKCLTFDPFQR 273
Cdd:cd08528 233 PLPEGM-YSDDITFVIRSCLTPDPEAR 258
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
125-332 4.89e-12

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: 67.35  E-value: 4.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 125 KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRS---QYSDFQGTRLYCPP 201
Cdd:cd05623 165 KFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDM-NGHIRLADFGSCLKLMEDgtvQSSVAVGTPDYISP 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 202 EwFLHSLYLGR-----EAAVWSLGVLLYNSLNGRLPFRNEKDICT-AHLLGPLPFF------VPVSAEVKDLISK--CLT 267
Cdd:cd05623 244 E-ILQAMEDGKgkygpECDWWSLGVCMYEMLYGETPFYAESLVETyGKIMNHKERFqfptqvTDVSENAKDLIRRliCSR 322
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 268 FDPFQRCSLEAILNHPWVkqQTLSWDALTKNKVQ--KKTSESSDDHHSETLGDHSETEEDRSPPTSS 332
Cdd:cd05623 323 EHRLGQNGIEDFKNHPFF--VGIDWDNIRNCEAPyiPEVSSPTDTSNFDVDDDCLKNCETMPPPTHT 387
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
35-287 5.69e-12

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: 66.62  E-value: 5.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  35 AELGRGGFGVVYRAVRTCDNALVAVKFIERSnVKEWARingEQVPMEICMLAKCSKVRGVIRLLDWYSIPEgFLIVMERp 114
Cdd:cd06650  11 SELGAGNGGVVFKVSHKPSGLVMARKLIHLE-IKPAIR---NQIIRELQVLHECNSPYIVGFYGAFYSDGE-ISICMEH- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 115 ypcID---MFDFIKGQGKISEDmarfLFRQIAVTVHECV-----QNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR 186
Cdd:cd06650  85 ---MDggsLDQVLKKAGRIPEQ----ILGKVSIAVIKGLtylreKHKIMHRDVKPSNILVN-SRGEIKLCDFGVSGQLID 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWfLHSLYLGREAAVWSLGVLLYNSLNGRLPF--------------RNEKDiCTAHLLGPLPFFV 252
Cdd:cd06650 157 SMANSFVGTRSYMSPER-LQGTHYSVQSDIWSMGLSLVEMAVGRYPIpppdakelelmfgcQVEGD-AAETPPRPRTPGR 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 253 PVS---------------------------------AEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06650 235 PLSsygmdsrppmaifelldyivnepppklpsgvfsLEFQDFVNKCLIKNPAERADLKQLMVHAFIKR 302
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
151-287 6.28e-12

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: 65.92  E-value: 6.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 151 QNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGR 230
Cdd:cd06620 123 VHRIIHRDIKPSNILVN-SKGQIKLCDFGVSGELINSIADTFVGTSTYMSPERIQGGKY-SVKSDVWSLGLSIIELALGE 200
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25143934 231 LPF--RNEKDICTAHLLG-------------P-LPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06620 201 FPFagSNDDDDGYNGPMGildllqrivneppPrLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQ 273
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
37-283 6.29e-12

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: 65.53  E-value: 6.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIE--RSNVKEWARInGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFLIVME-R 113
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTLMAVKQVSfcRNSSSEQEEV-VEAIREEIRMMARLNHPN-IVRMLGATQHKSHFNIFVEwM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 PYPCIDMFdfIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVL--RRSQYSD 191
Cdd:cd06630  86 AGGSVASL--LSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQRLRIADFGAAARLasKGTGAGE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRL----YCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEK---------DICTAhlLGPLPFFVPVSAEV 258
Cdd:cd06630 164 FQGQLLgtiaFMAPEVLRGEQY-GRSCDVWSVGCVIIEMATAKPPWNAEKisnhlalifKIASA--TTPPPIPEHLSPGL 240
                       250       260
                ....*....|....*....|....*
gi 25143934 259 KDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd06630 241 RDVTLRCLELQPEDRPPARELLKHP 265
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
37-293 7.86e-12

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: 66.23  E-value: 7.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVyRAVRTCDNA-LVAVKFIERSNVKEWARINGEQVPMEICMLAKCSkvrGVIRLLDWYSIPEGFLIVMERpY 115
Cdd:cd05627  10 IGRGAFGEV-RLVQKKDTGhIYAMKILRKADMLEKEQVAHIRAERDILVEADGA---WVVKMFYSFQDKRNLYLIMEF-L 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSDFQ-- 193
Cdd:cd05627  85 PGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLD-AKGHVKLSDFGLCTGLKKAHRTEFYrn 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 194 -----------------------------------GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE-- 236
Cdd:cd05627 164 lthnppsdfsfqnmnskrkaetwkknrrqlaystvGTPDYIAPEVFMQTGY-NKLCDWWSLGVIMYEMLIGYPPFCSEtp 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143934 237 ----KDICTAHLLGPLPFFVPVSAEVKDLISKCLTfDPFQRC---SLEAILNHPWVkqQTLSWD 293
Cdd:cd05627 243 qetyRKVMNWKETLVFPPEVPISEKAKDLILRFCT-DAENRIgsnGVEEIKSHPFF--EGVDWE 303
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
32-282 8.68e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 65.02  E-value: 8.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAELGRGGFGVVYRAVRTcdNALVAVKFIERSNvKEWARINGEQVPMEICMLaKCSKVRGVIRLLD-WYSIPEGfliv 110
Cdd:cd14033   4 KFNIEIGRGSFKTVYRGLDT--ETTVEVAWCELQT-RKLSKGERQRFSEEVEML-KGLQHPNIVRFYDsWKSTVRG---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 merpYPCIDMFDFIKGQGKISEDMARF----------LFRQIAVTVHeCVQNR---VLHRDLKDENIVIDLVTGSTKLID 177
Cdd:cd14033  76 ----HKCIILVTELMTSGTLKTYLKRFremklkllqrWSRQILKGLH-FLHSRcppILHRDLKCDNIFITGPTGSVKIGD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 178 FGAATVLRRSQYSDFQGTRLYCPPEWFLHSLylgREAA-VWSLGVLLYNSLNGRLPF---RNEKDICTAHLLG--PLPFF 251
Cdd:cd14033 151 LGLATLKRASFAKSVIGTPEFMAPEMYEEKY---DEAVdVYAFGMCILEMATSEYPYsecQNAAQIYRKVTSGikPDSFY 227
                       250       260       270
                ....*....|....*....|....*....|.
gi 25143934 252 VPVSAEVKDLISKCLTFDPFQRCSLEAILNH 282
Cdd:cd14033 228 KVKVPELKEIIEGCIRTDKDERFTIQDLLEH 258
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
37-282 8.71e-12

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: 64.82  E-value: 8.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAvrTCDNALVAVKFIER---SNVKEWARINGEQVP--MEICMLAKCskvrgvirlldwysipegFLIVM 111
Cdd:cd14059   1 LGSGAQGAVFLG--KFRGEEVAVKKVRDekeTDIKHLRKLNHPNIIkfKGVCTQAPC------------------YCILM 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 ER-PYPciDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLR-RSQY 189
Cdd:cd14059  61 EYcPYG--QLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVT-YNDVLKISDFGTSKELSeKSTK 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFrneKDI-CTAHLLG--------PLPFFVPvsAEVKD 260
Cdd:cd14059 138 MSFAGTVAWMAPE-VIRNEPCSEKVDIWSFGVVLWELLTGEIPY---KDVdSSAIIWGvgsnslqlPVPSTCP--DGFKL 211
                       250       260
                ....*....|....*....|..
gi 25143934 261 LISKCLTFDPFQRCSLEAILNH 282
Cdd:cd14059 212 LMKQCWNSKPRNRPSFRQILMH 233
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
31-285 9.45e-12

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 65.42  E-value: 9.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringEQVPMEICMLAKCSKVRGVIRLLDWY---SIPEG- 106
Cdd:cd06638  20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDID------EEIEAEYNILKALSDHPNVVKFYGMYykkDVKNGd 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 -FLIVMERpypCI--DMFDFIKGQGKISEDMARFLfrqIAVTVHECV-------QNRVLHRDLKDENIVIDlVTGSTKLI 176
Cdd:cd06638  94 qLWLVLEL---CNggSVTDLVKGFLKRGERMEEPI---IAYILHEALmglqhlhVNKTIHRDVKGNNILLT-TEGGVKLV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAA-----TVLRRSQYSdfqGTRLYCPPEWF-----LHSLYLGReAAVWSLGVLLYNSLNGRLPFrneKDICTAHLLG 246
Cdd:cd06638 167 DFGVSaqltsTRLRRNTSV---GTPFWMAPEVIaceqqLDSTYDAR-CDVWSLGITAIELGDGDPPL---ADLHPMRALF 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 25143934 247 PLPFFVPV--------SAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06638 240 KIPRNPPPtlhqpelwSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
37-273 9.60e-12

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: 65.21  E-value: 9.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTcDNALVAVKfiersNVKEWARINGE-QVPMEICMLAKcSKVRGVIRLLDWYSIPEGFLIVME-RP 114
Cdd:cd14664   1 IGRGGAGTVYKGVMP-NGTLVAVK-----RLKGEGTQGGDhGFQAEIQTLGM-IRHRNIVRLRGYCSNPTTNLLVYEyMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 115 YPCIDMFDFIKGQGKISED------MARFLFRQIAVTVHECVQnRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQ 188
Cdd:cd14664  74 NGSLGELLHSRPESQPPLDwetrqrIALGSARGLAYLHHDCSP-LIIHRDVKSNNILLD-EEFEAHVADFGLAKLMDDKD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 ---YSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPF----------------RNEKDICTAHLLGPLP 249
Cdd:cd14664 152 shvMSSVAGSYGYIAPE-YAYTGKVSEKSDVYSYGVVLLELITGKRPFdeaflddgvdivdwvrGLLEEKKVEALVDPDL 230
                       250       260
                ....*....|....*....|....*..
gi 25143934 250 FFVPVSAEVKDLIS---KCLTFDPFQR 273
Cdd:cd14664 231 QGVYKLEEVEQVFQvalLCTQSSPMER 257
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
28-294 1.07e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 65.55  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   28 KKNYKLK-AELGRGGFGVVYRAVRTCDNALVA---VKFIERSNVKEWARINGEQVPMEICMLAKCSKVR-----GVIRLL 98
Cdd:PTZ00024   7 SERYIQKgAHLGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDRQLVGMCGIHFTTLRELKIMNeikheNIMGLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   99 DWYsIPEGFL-IVMErpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLID 177
Cdd:PTZ00024  87 DVY-VEGDFInLVMD--IMASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFIN-SKGICKIAD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  178 FGAA----------------TVLRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR--LPFRNEKDI 239
Cdd:PTZ00024 163 FGLArrygyppysdtlskdeTMQRREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKplFPGENEIDQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  240 CTA--HLLGP-----------LPFFVPVSAEVK---------------DLISKCLTFDPFQRCSLEAILNHPWVKQQTLS 291
Cdd:PTZ00024 243 LGRifELLGTpnednwpqakkLPLYTEFTPRKPkdlktifpnasddaiDLLQSLLKLNPLERISAKEALKHEYFKSDPLP 322

                 ...
gi 25143934  292 WDA 294
Cdd:PTZ00024 323 CDP 325
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
30-233 1.07e-11

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: 65.07  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAK-CSKvrgviRLLDWYSI----P 104
Cdd:cd06652   3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETSKEVNALECEIQLLKNlLHE-----RIVQYYGClrdpQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVMERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVL 184
Cdd:cd06652  78 ERTLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRD-SVGNVKLGDFGASKRL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 25143934 185 RR-----SQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF 233
Cdd:cd06652 157 QTiclsgTGMKSVTGTPYWMSPEVISGEGY-GRKADIWSVGCTVVEMLTEKPPW 209
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
29-287 1.11e-11

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: 65.79  E-value: 1.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIE---------RS--NVKEWARINGEQVpmeicmlakcSKVRGVIRL 97
Cdd:cd07849   5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpfehqtyclRTlrEIKILLRFKHENI----------IGILDIQRP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  98 LDWYSIPEGFLI--VMErpypcIDMFDFIKGQgKISEDMARFLFRQI--AV-TVHECvqnRVLHRDLKDENIVI----DL 168
Cdd:cd07849  75 PTFESFKDVYIVqeLME-----TDLYKLIKTQ-HLSNDHIQYFLYQIlrGLkYIHSA---NVLHRDLKPSNLLLntncDL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 169 vtgstKLIDFGAATVL-----RRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR--LPFRNEKDICT 241
Cdd:cd07849 146 -----KICDFGLARIAdpehdHTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRplFPGKDYLHQLN 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 242 aHLLG-----------------------PLPFFVPVS-------AEVK--DLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd07849 221 -LILGilgtpsqedlnciislkarnyikSLPFKPKVPwnklfpnADPKalDLLDKMLTFNPHKRITVEEALAHPYLEQ 297
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
37-283 1.20e-11

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: 64.64  E-value: 1.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARING-------EQVPMEICMLakcskvrGVIRLLDWYSIpegFLI 109
Cdd:cd14050   9 LGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKleeverhEKLGEHPNCV-------RFIKAWEEKGI---LYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQY 189
Cdd:cd14050  79 QTE--LCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSK-DGVCKLGDFGLVVELDKEDI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SDFQ-GTRLYCPPEwFLHSLYlGREAAVWSLGV-LLYNSLNGRLP--------FRNekdictAHLlgPLPFFVPVSAEVK 259
Cdd:cd14050 156 HDAQeGDPRYMAPE-LLQGSF-TKAADIFSLGItILELACNLELPsggdgwhqLRQ------GYL--PEEFTAGLSPELR 225
                       250       260
                ....*....|....*....|....
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd14050 226 SIIKLMMDPDPERRPTAEDLLALP 249
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
36-290 2.16e-11

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: 64.62  E-value: 2.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMeicmlaKCSKVRGVIRLLDWYSIPEGFLIVMErpy 115
Cdd:cd06659  28 KIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIM------RDYQHPNVVEMYKSYLVGEELWVLME--- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pcidmfdFIKGqGKISEDMA--RFLFRQIAVTVHECVQ-------NRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRR 186
Cdd:cd06659  99 -------YLQG-GALTDIVSqtRLNEEQIATVCEAVLQalaylhsQGVIHRDIKSDSILLTL-DGRVKLSDFGFCAQISK 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 S--QYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL--GPLPF---FVPVSAEVK 259
Cdd:cd06659 170 DvpKRKSLVGTPYWMAPEVISRCPY-GTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLrdSPPPKlknSHKASPVLR 248
                       250       260       270
                ....*....|....*....|....*....|.
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWVKQQTL 290
Cdd:cd06659 249 DFLERMLVRDPQERATAQELLDHPFLLQTGL 279
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
7-301 2.50e-11

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 64.62  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    7 LQFF-NLKLLLNGESSRGFSKFKKNyKLKAE-------LGRGGFG-VVYRAVRTCDNALVAVKFIERSNV---KEWARIN 74
Cdd:PTZ00426   1 IQFLkNLQLHKKKDSDSTKEPKRKN-KMKYEdfnfirtLGTGSFGrVILATYKNEDFPPVAIKRFEKSKIikqKQVDHVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   75 GEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMErpypcidMFDFIKGQGKISEDMARFLFRQIaVTVHECVQN-R 153
Cdd:PTZ00426  80 SERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGE-------FFTFLRRNKRFPNDVGCFYAAQI-VLIFEYLQSlN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  154 VLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSdFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF 233
Cdd:PTZ00426 152 IVYRDLKPENLLLD-KDGFIKMTDFGFAKVVDTRTYT-LCGTPEYIAPEILLNVGH-GKAADWWTLGIFIYEILVGCPPF 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25143934  234 -RNEKDICTAHLLGPLPFFVP-VSAEVKDLISKCLTFDPFQRC-----SLEAILNHPWVKQqtLSWDALTKNKVQ 301
Cdd:PTZ00426 229 yANEPLLIYQKILEGIIYFPKfLDNNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGN--IDWVSLLHKNVE 301
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
29-300 2.74e-11

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: 64.66  E-value: 2.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVpmEICMLAKCSKVRGVIRLLDWYSIPEGFL 108
Cdd:cd05617  15 QDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQT--EKHVFEQASSNPFLVGLHSCFQTTSRLF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERPYPCIDMFDfIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR-- 186
Cdd:cd05617  93 LVIEYVNGGDLMFH-MQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLD-ADGHIKLTDYGMCKEGLGpg 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 SQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF---RNEKDICTAHLLGPL----PFFVPVSAEVK 259
Cdd:cd05617 171 DTTSTFCGTPNYIAPEILRGEEY-GFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQVilekPIRIPRFLSVK 249
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 25143934 260 --DLISKCLTFDPFQR--CSLEA----ILNHPWVKqqTLSWDALTKNKV 300
Cdd:cd05617 250 asHVLKGFLNKDPKERlgCQPQTgfsdIKSHTFFR--SIDWDLLEKKQV 296
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
31-220 2.90e-11

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 64.19  E-value: 2.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARingeQVPMEICMLAKCSKVRG------VIRLLDwYSIP 104
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLK--NKPAYFR----QAMLEIAILTLLNTKYDpedkhhIVRLLD-HFMH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFL-IVMErpYPCIDMFDFIKgQGK---ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI-DLVTGSTKLIDFG 179
Cdd:cd14212  74 HGHLcIVFE--LLGVNLYELLK-QNQfrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLvNLDSPEIKLIDFG 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 25143934 180 AATVLRRSQYSDFQgTRLYCPPEWFLHSLYlgrEAAV--WSLG 220
Cdd:cd14212 151 SACFENYTLYTYIQ-SRFYRSPEVLLGLPY---STAIdmWSLG 189
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
92-285 3.26e-11

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: 63.30  E-value: 3.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  92 RGVIRLLDWYSIPEGFLIVMERPYPCIDMF--DFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlv 169
Cdd:cd14109  56 PNIVQMHDAYDDEKLAVTVIDNLASTIELVrdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQ-- 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 170 TGSTKLIDFGAATVLRRSQ-YSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLG 246
Cdd:cd14109 134 DDKLKLADFGQSRRLLRGKlTTLIYGSPEFVSPE-IVNSYPVTLATDMWSVGVLTYVLLGGISPFlgDNDRETLTNVRSG 212
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 25143934 247 PLPFFV----PVSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14109 213 KWSFDSsplgNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
37-340 3.45e-11

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: 64.27  E-value: 3.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNV---KEWARINGEqvpmeicmlakcskvRGVIrlldWYSIPEGFLIVMER 113
Cdd:cd05602  15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKAIlkkKEEKHIMSE---------------RNVL----LKNVKHPFLVGLHF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 PYPCID----MFDFIKG---------QGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG- 179
Cdd:cd05602  76 SFQTTDklyfVLDYINGgelfyhlqrERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLD-SQGHIVLTDFGl 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 -AATVLRRSQYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFVPVSA 256
Cdd:cd05602 155 cKENIEPNGTTSTFCGTPEYLAPE-VLHKQPYDRTVDWWCLGAVLYEMLYGLPPFysRNTAEMYDNILNKPLQLKPNITN 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 257 EVKDLISKCLTFDPFQRCSLE----AILNHPWVkqQTLSWDALTKNKV----QKKTSESSDDHHSetlgDHSETEEdrsP 328
Cdd:cd05602 234 SARHLLEGLLQKDRTKRLGAKddftEIKNHIFF--SPINWDDLINKKItppfNPNVSGPNDLRHF----DPEFTDE---P 304
                       330
                ....*....|..
gi 25143934 329 PTSSVSQQPGSA 340
Cdd:cd05602 305 VPNSIGQSPDSI 316
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
37-355 3.46e-11

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: 63.88  E-value: 3.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNV---KEWARINGEqvpmeicmlakcskvRGVirLLDWYSIPegFLIVMER 113
Cdd:cd05575   3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAIlkrNEVKHIMAE---------------RNV--LLKNVKHP--FLVGLHY 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 PYPCID----MFDFIKGqGKI----------SEDMARFLFRQIAVTV---HEcvqNRVLHRDLKDENIVIDlVTGSTKLI 176
Cdd:cd05575  64 SFQTKDklyfVLDYVNG-GELffhlqrerhfPEPRARFYAAEIASALgylHS---LNIIYRDLKPENILLD-SQGHVVLT 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAAT--VLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHLLGPLPFFV 252
Cdd:cd05575 139 DFGLCKegIEPSDTTSTFCGTPEYLAPEVLRKQPY-DRTVDWWCLGAVLYEMLYGLPPFysRDTAEMYDNILHKPLRLRT 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 253 PVSAEVKDLISKCLTFDPFQRC----SLEAILNHPWVKqqTLSWDALTKNKVQK----KTSESSDdhhsetlGDHSETEE 324
Cdd:cd05575 218 NVSPSARDLLEGLLQKDRTKRLgsgnDFLEIKNHSFFR--PINWDDLEAKKIPPpfnpNVSGPLD-------LRNIDPEF 288
                       330       340       350
                ....*....|....*....|....*....|.
gi 25143934 325 DRSPPTSSVSQqpgsADEGVGLSASSSNTHN 355
Cdd:cd05575 289 TREPVPASVGK----SADSVAVSASVQEADN 315
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
37-295 3.79e-11

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: 63.75  E-value: 3.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEIcmLAKCSKvRGVIRLLDWYSIPEGFLIVM----- 111
Cdd:cd05608   9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRI--LAKVHS-RFIVSLAYAFQTKTDLCLVMtimng 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 -ERPYpciDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLR--RSQ 188
Cdd:cd05608  86 gDLRY---HIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLD-DDGNVRISDLGLAVELKdgQTK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSDFQGTRLYCPPEWFLHSLYlgrEAAV--WSLGVLLYNSLNGRLPFR------NEKDICTAHLLGPLPFFVPVSAEVKD 260
Cdd:cd05608 162 TKGYAGTPGFMAPELLLGEEY---DYSVdyFTLGVTLYEMIAARGPFRargekvENKELKQRILNDSVTYSEKFSPASKS 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 25143934 261 LISKCLTFDP-----FQRCSLEAILNHPWVKQqtLSWDAL 295
Cdd:cd05608 239 ICEALLAKDPekrlgFRDGNCDGLRTHPFFRD--INWRKL 276
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
30-285 4.15e-11

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: 63.96  E-value: 4.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRA--VRTCDNALVAVKFIERSNVKEwarINGEQVPMEICMLAKCSKVRGVIRLLD----WYSI 103
Cdd:cd07857   1 RYELIKELGQGAYGIVCSArnAETSEEETVAIKKITNVFSKK---ILAKRALRELKLLRHFRGHKNITCLYDmdivFPGN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 PEGFLIVMErPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATV 183
Cdd:cd07857  78 FNELYLYEE-LMEA-DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNA-DCELKICDFGLARG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQY------SDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLnGRLPFRNEKDICTA-----HLLGP----- 247
Cdd:cd07857 155 FSENPGenagfmTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELL-GRKPVFKGKDYVDQlnqilQVLGTpdeet 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143934 248 ---------------LPFFVPV---------SAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd07857 234 lsrigspkaqnyirsLPNIPKKpfesifpnaNPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
37-293 5.15e-11

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: 63.91  E-value: 5.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVkeWARINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMERpYP 116
Cdd:cd05625   9 LGIGAFGEVCLARKVDTKALYATKTLRKKDV--LLRNQVAHVKAERDILAEADN-EWVVRLYYSFQDKDNLYFVMDY-IP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLR----------- 185
Cdd:cd05625  85 GGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR-DGHIKLTDFGLCTGFRwthdskyyqsg 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 ---RSQYSDFQ-----------GTRLYcPPEW---------FLHSL-----YLGREAAV----------WSLGVLLYNSL 227
Cdd:cd05625 164 dhlRQDSMDFSnewgdpencrcGDRLK-PLERraarqhqrcLAHSLvgtpnYIAPEVLLrtgytqlcdwWSVGVILFEML 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 228 NGRLPFRNEKDICTA------HLLGPLPFFVPVSAEVKDLISKcLTFDPFQRC---SLEAILNHPWVKQQTLSWD 293
Cdd:cd05625 243 VGQPPFLAQTPLETQmkvinwQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTIDFSSD 316
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
29-336 5.33e-11

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: 63.87  E-value: 5.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSkvrGVIRLLDWYSIPEGFL 108
Cdd:cd05622  73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSP---WVVQLFYAFQDDRYLY 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERpYPCIDMFDFIKGQgKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS- 187
Cdd:cd05622 150 MVMEY-MPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHLKLADFGTCMKMNKEg 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 --QYSDFQGTRLYCPPEwFLHSL----YLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLG------PLPFFVPVS 255
Cdd:cd05622 227 mvRCDTAVGTPDYISPE-VLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhknslTFPDDNDIS 305
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 256 AEVKDLISKCLTFDPFQ--RCSLEAILNHPWVKQQTLSWDALtKNKVQKKTSESSDDHHSETLGDHSET--EEDRSP-PT 330
Cdd:cd05622 306 KEAKNLICAFLTDREVRlgRNGVEEIKRHLFFKNDQWAWETL-RDTVAPVVPDLSSDIDTSNFDDLEEDkgEEETFPiPK 384

                ....*.
gi 25143934 331 SSVSQQ 336
Cdd:cd05622 385 AFVGNQ 390
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
31-285 5.79e-11

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: 63.57  E-value: 5.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARingeQVPMEICMLAKCSK-----VRGVIRLLDWYSIPE 105
Cdd:cd14225  45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIR--NKKRFHH----QALVEVKILDALRRkdrdnSHNVIHMKEYFYFRN 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMErpYPCIDMFDFIKGQGKISEDMArfLFRQIAVTVHECVQ----NRVLHRDLKDENIVIDLV-TGSTKLIDFGA 180
Cdd:cd14225 119 HLCITFE--LLGMNLYELIKKNNFQGFSLS--LIRRFAISLLQCLRllyrERIIHCDLKPENILLRQRgQSSIKVIDFGS 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRSQYSDFQgTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI----CTAHLLGPLP------- 249
Cdd:cd14225 195 SCYEHQRVYTYIQ-SRFYRSPEVILGLPY-SMAIDMWSLGCILAELYTGYPLFPGENEVeqlaCIMEVLGLPPpeliena 272
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 250 -----FF-----------------VPVSAEVK-----------DLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd14225 273 qrrrlFFdskgnprcitnskgkkrRPNSKDLAsalktsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
40-284 7.37e-11

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 62.63  E-value: 7.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  40 GGFGVVYRAVRTCDNALVAVKFIERSNVKEwaringeQVPM----EICMLAKCS-----KVRGVI---RLLDWYsipegf 107
Cdd:cd07843  16 GTYGVVYRARDKKTGEIVALKKLKMEKEKE-------GFPItslrEINILLKLQhpnivTVKEVVvgsNLDKIY------ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 lIVMErpypCIDM-----FDFIKGQGKISEdmARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVT--GSTKLIDFGA 180
Cdd:cd07843  83 -MVME----YVEHdlkslMETMKQPFLQSE--VKCLMLQLLSGVAHLHDNWILHRDLKTSNL---LLNnrGILKICDFGL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 AtvlRR-----SQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR--LPFRNEKD----ICTahLLG--- 246
Cdd:cd07843 153 A---REygsplKPYTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKplFPGKSEIDqlnkIFK--LLGtpt 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 247 ----PLPFFVPVSAEVK-----------------------DLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07843 228 ekiwPGFSELPGAKKKTftkypynqlrkkfpalslsdngfDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
30-284 7.85e-11

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: 62.50  E-value: 7.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersnvkewaRINGEQ-VP----MEICMLaKCSKVRGVIRLLDWYSIP 104
Cdd:cd07836   1 NFKQLEKLGEGTYATVYKGRNRTTGEIVALKEI---------HLDAEEgTPstaiREISLM-KELKHENIVRLHDVIHTE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVMErpYPCIDMFDFIK---GQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA 181
Cdd:cd07836  71 NKLMLVFE--YMDKDLKKYMDthgVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLIN-KRGELKLADFGLA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TV--LRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFR----NEKDICTAHLLGP-------- 247
Cdd:cd07836 148 RAfgIPVNTFSNEVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPgtnnEDQLLKIFRIMGTptestwpg 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 248 ---LPFFVPVSAEVK----------------DLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07836 228 isqLPEYKPTFPRYPpqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
36-283 7.99e-11

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: 62.29  E-value: 7.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFG-VVYRAvrTCDNALVAVKFIERSNVkEWARingeqvpMEICMLAKCSKVRGVIRlldWYSIPE--GFL-IVM 111
Cdd:cd13982   8 VLGYGSEGtIVFRG--TFDGRPVAVKRLLPEFF-DFAD-------REVQLLRESDEHPNVIR---YFCTEKdrQFLyIAL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 ERpypC-IDMFDFIKGQ------GKISEDMARFLfRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST----KLIDFGA 180
Cdd:cd13982  75 EL---CaASLQDLVESPresklfLRPGLEPVRLL-RQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGnvraMISDFGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRSQYSDFQ-----GTRLYCPPEWFLHSLYLGREAAV--WSLGVLLYNSL-NGRLPF----RNEKDI-----CTAH 243
Cdd:cd13982 151 CKKLDVGRSSFSRrsgvaGTSGWIAPEMLSGSTKRRQTRAVdiFSLGCVFYYVLsGGSHPFgdklEREANIlkgkySLDK 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 25143934 244 LLGPLPFFVpvsaEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd13982 231 LLSLGEHGP----EAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
37-293 8.01e-11

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: 63.49  E-value: 8.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwaRINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMERpYP 116
Cdd:cd05626   9 LGIGAFGEVCLACKVDTHALYAMKTLRKKDVLN--RNQVAHVKAERDILAEADN-EWVVKLYYSFQDKDNLYFVMDY-IP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLR---RSQY---- 189
Cdd:cd05626  85 GGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDL-DGHIKLTDFGLCTGFRwthNSKYyqkg 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 ----------SDFQ--------------------------------GTRLYCPPEWFLHSLYLgREAAVWSLGVLLYNSL 227
Cdd:cd05626 164 shirqdsmepSDLWddvsncrcgdrlktleqratkqhqrclahslvGTPNYIAPEVLLRKGYT-QLCDWWSVGVILFEML 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143934 228 NGRLPF------RNEKDICTAHLLGPLPFFVPVSAEVKDLISK--CLTFDPFQRCSLEAILNHPWVKQQTLSWD 293
Cdd:cd05626 243 VGQPPFlaptptETQLKVINWENTLHIPPQVKLSPEAVDLITKlcCSAEERLGRNGADDIKAHPFFSEVDFSSD 316
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
119-301 8.85e-11

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: 62.80  E-value: 8.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG---AATVLRRSQYSdFQGT 195
Cdd:cd05582  83 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD-EDGHIKLTDFGlskESIDHEKKAYS-FCGT 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 196 RLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPF--RNEKDICTAHL---LGpLPFFvpVSAEVKDLISKCLTFDP 270
Cdd:cd05582 161 VEYMAPE-VVNRRGHTQSADWWSFGVLMFEMLTGSLPFqgKDRKETMTMILkakLG-MPQF--LSPEAQSLLRALFKRNP 236
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 25143934 271 FQRC-----SLEAILNHPWVKqqTLSWDALTKNKVQ 301
Cdd:cd05582 237 ANRLgagpdGVEEIKRHPFFA--TIDWNKLYRKEIK 270
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
14-287 9.40e-11

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: 62.72  E-value: 9.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  14 LLLNGEssrgfsKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIER-SNVKEWARIngeqvpmEICMLAKCSKVR 92
Cdd:cd14226   4 IVKNGE------KWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNkKAFLNQAQI-------EVRLLELMNKHD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  93 G-----VIRLLDWYSIPEGFLIVMER-PYpciDMFDFIK--GQGKISEDMARFLFRQIAVTVHECVQN--RVLHRDLKDE 162
Cdd:cd14226  71 TenkyyIVRLKRHFMFRNHLCLVFELlSY---NLYDLLRntNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 163 NIVidLVT---GSTKLIDFGAATVLRRSQYSDFQgTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF--RNEK 237
Cdd:cd14226 148 NIL--LCNpkrSAIKIIDFGSSCQLGQRIYQYIQ-SRFYRSPEVLLGLPY-DLAIDMWSLGCILVEMHTGEPLFsgANEV 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 238 DICT--AHLLGPLP------------FFVPVS------------------------------------------------ 255
Cdd:cd14226 224 DQMNkiVEVLGMPPvhmldqapkarkFFEKLPdgtyylkktkdgkkykppgsrklheilgvetggpggrragepghtved 303
                       330       340       350
                ....*....|....*....|....*....|...
gi 25143934 256 -AEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd14226 304 yLKFKDLILRMLDYDPKTRITPAEALQHSFFKR 336
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
22-326 9.93e-11

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: 63.09  E-value: 9.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  22 RGFSKFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSkvrGVIRLLDWY 101
Cdd:cd05621  45 RELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSP---WVVQLFCAF 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 102 SIPEGFLIVMERpYPCIDMFDFIKGQgKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGaa 181
Cdd:cd05621 122 QDDKYLYMVMEY-MPGGDLVNLMSNY-DVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDK-YGHLKLADFG-- 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQYSDFQ-----GTRLYCPPEwFLHSL----YLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGP----- 247
Cdd:cd05621 197 TCMKMDETGMVHcdtavGTPDYISPE-VLKSQggdgYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDhknsl 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 248 -LPFFVPVSAEVKDLISKCLTFDPFQ--RCSLEAILNHPWVKQQTLSWDALTKNKVQKKTSESSDDHHSetlgDHSETEE 324
Cdd:cd05621 276 nFPDDVEISKHAKNLICAFLTDREVRlgRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTS----NFDDIED 351

                ..
gi 25143934 325 DR 326
Cdd:cd05621 352 DK 353
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
31-284 1.11e-10

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: 62.16  E-value: 1.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKfiersnvKEWARINGEQVP----MEICMLAKCSKVRGVIRLLDWYSIPEG 106
Cdd:cd07837   3 YEKLEKIGEGTYGKVYKARDKNTGKLVALK-------KTRLEMEEEGVPstalREVSLLQMLSQSIYIVRLLDVEHVEEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 ----FLIVMErpYPCIDMFDFIKGQGKISED------MARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLI 176
Cdd:cd07837  76 gkplLYLVFE--YLDTDLKKFIDSYGRGPHNplpaktIQSFMY-QLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLLKIA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFG---AATVLRRSqYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTA----HLLGP-- 247
Cdd:cd07837 153 DLGlgrAFTIPIKS-YTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLlhifRLLGTpn 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143934 248 -----------------------LPFFVP-VSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07837 232 eevwpgvsklrdwheypqwkpqdLSRAVPdLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
37-273 1.18e-10

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: 61.92  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYrAVRTCDNALVAV-KFIERSNVKEWaringEQVPMEICMLAKCSKVRGVIRLLDWY--SIPEG---FLIV 110
Cdd:cd14037  11 LAEGGFAHVY-LVKTSNGGNRAAlKRVYVNDEHDL-----NVCKREIEIMKRLSGHKNIVGYIDSSanRSGNGvyeVLLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFI--KGQGKISEDMARFLFRQIAVTV---HECvQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT-VL 184
Cdd:cd14037  85 MEY-CKGGGVIDLMnqRLQTGLTESEILKIFCDVCEAVaamHYL-KPPLIHRDLKVENVLIS-DSGNYKLCDFGSATtKI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYSD---------FQGTRL-YCPPEwfLHSLYLGRE----AAVWSLGVLLYNSLNGRLPFRNEKD--ICTAHLlgPL 248
Cdd:cd14037 162 LPPQTKQgvtyveediKKYTTLqYRAPE--MIDLYRGKPitekSDIWALGCLLYKLCFYTTPFEESGQlaILNGNF--TF 237
                       250       260
                ....*....|....*....|....*
gi 25143934 249 PFFVPVSAEVKDLISKCLTFDPFQR 273
Cdd:cd14037 238 PDNSRYSKRLHKLIRYMLEEDPEKR 262
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
37-288 1.24e-10

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: 62.70  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarINGEQVPMEICMLaKCSKVRGVIRLLDWYSIPEG------FLIV 110
Cdd:cd07851  23 VGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSA---IHAKRTYRELRLL-KHMKHENVIGLLDVFTPASSledfqdVYLV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MerPYPCIDMFDFIKGQgKISEDMARFLFRQIAVT---VHECvqnRVLHRDLKDENIVI----DLvtgstKLIDFGAATv 183
Cdd:cd07851  99 T--HLMGADLNNIVKCQ-KLSDDHIQFLVYQILRGlkyIHSA---GIIHRDLKPSNLAVnedcEL-----KILDFGLAR- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDI----CTAHLLG-P----------- 247
Cdd:cd07851 167 HTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIdqlkRIMNLVGtPdeellkkisse 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 248 --------LP---------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQ 288
Cdd:cd07851 247 sarnyiqsLPqmpkkdfkeVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEY 304
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
32-273 1.26e-10

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: 61.63  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAELGRGGFGVVYRAV---RTcdnalVAVKFIERSNVKE------WARINgeqvpmeicmlAKCSKVRGVIRLL---D 99
Cdd:cd13979   6 RLQEPLGSGGFGSVYKATykgET-----VAVKIVRRRRKNRasrqsfWAELN-----------AARLRHENIVRVLaaeT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 100 WYSIPEGFLIVME------------RPYPCIDMFDFIKgqgkISEDMA---RFLFRQiavtvhecvqnRVLHRDLKDENI 164
Cdd:cd13979  70 GTDFASLGLIIMEycgngtlqqliyEGSEPLPLAHRIL----ISLDIAralRFCHSH-----------GIVHLDVKPANI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 165 VIDlVTGSTKLIDFGAATVLRR-----SQYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDI 239
Cdd:cd13979 135 LIS-EQGVCKLCDFGCSVKLGEgnevgTPRSHIGGTYTYRAPE-LLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQH 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25143934 240 ----CTAHLLGPLPFFVPVSAE---VKDLISKCLTFDPFQR 273
Cdd:cd13979 213 vlyaVVAKDLRPDLSGLEDSEFgqrLRSLISRCWSAQPAER 253
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
8-285 1.35e-10

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: 62.74  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   8 QFFNLKLllnGESSrgFSKFKKNYKLKAeLGRGGFGVVYRAVRTCDNALVAVKFIER--SNVKEWARINGEQVpmeicmL 85
Cdd:cd07876   6 QFYSVQV---ADST--FTVLKRYQQLKP-IGSGAQGIVCAAFDTVLGINVAVKKLSRpfQNQTHAKRAYRELV------L 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  86 AKCSKVRGVIRLLDWYSiPEGFLIVMERPYPCIDMFDFIKGQ---GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDE 162
Cdd:cd07876  74 LKCVNHKNIISLLNVFT-PQKSLEEFQDVYLVMELMDANLCQvihMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 163 NIVIDlVTGSTKLIDFG-AATVLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI-- 239
Cdd:cd07876 153 NIVVK-SDCTLKILDFGlARTACTNFMMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGELVKGSVIFQGTDHIdq 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 240 ----------CTAHLLGPL-----------PFFVPVS---------------------AEVKDLISKCLTFDPFQRCSLE 277
Cdd:cd07876 231 wnkvieqlgtPSAEFMNRLqptvrnyvenrPQYPGISfeelfpdwifpseserdklktSQARDLLSKMLVIDPDKRISVD 310

                ....*...
gi 25143934 278 AILNHPWV 285
Cdd:cd07876 311 EALRHPYI 318
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
37-262 1.48e-10

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: 62.36  E-value: 1.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVyRAVRTCDNALV-AVKFIERSNVKEWARINGEQVPMEICMLAKCskvRGVIRLLDWYSIPEGFLIVMERpY 115
Cdd:cd05628   9 IGRGAFGEV-RLVQKKDTGHVyAMKILRKADMLEKEQVGHIRAERDILVEADS---LWVVKMFYSFQDKLNLYLIMEF-L 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSDFQ-- 193
Cdd:cd05628  84 PGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLD-SKGHVKLSDFGLCTGLKKAHRTEFYrn 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 194 -----------------------------------GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE-- 236
Cdd:cd05628 163 lnhslpsdftfqnmnskrkaetwkrnrrqlafstvGTPDYIAPEVFMQTGY-NKLCDWWSLGVIMYEMLIGYPPFCSEtp 241
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 237 ----KDICTAHLLGPLPFFVPVSAEVKDLI 262
Cdd:cd05628 242 qetyKKVMNWKETLIFPPEVPISEKAKDLI 271
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
37-300 1.66e-10

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: 61.90  E-value: 1.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERS---NVKEWARINGEqvpmeicmlakcskvRGVirLLDwySIPEGFLIVMER 113
Cdd:cd05604   4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKvilNRKEQKHIMAE---------------RNV--LLK--NVKHPFLVGLHY 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 114 PYPCID----MFDFIKG---------QGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGA 180
Cdd:cd05604  65 SFQTTDklyfVLDFVNGgelffhlqrERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLD-SQGHIVLTDFGL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 AT--VLRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNeKDICTAH---LLGPLPFFVPVS 255
Cdd:cd05604 144 CKegISNSDTTTTFCGTPEYLAPEVIRKQPY-DNTVDWWCLGSVLYEMLYGLPPFYC-RDTAEMYeniLHKPLVLRPGIS 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 25143934 256 AEVKDLISKCLTFDPFQRC----SLEAILNHPWVkqQTLSWDALTKNKV 300
Cdd:cd05604 222 LTAWSILEELLEKDRQLRLgakeDFLEIKNHPFF--ESINWTDLVQKKI 268
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
140-289 1.76e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 62.15  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  140 RQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLrrSQYSD----FQGTRLYCPPEW----FLHSLYLG 211
Cdd:PLN00034 175 RQILSGIAYLHRRHIVHRDIKPSNLLIN-SAKNVKIADFGVSRIL--AQTMDpcnsSVGTIAYMSPERintdLNHGAYDG 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  212 REAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVP------VSAEVKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:PLN00034 252 YAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQPpeapatASREFRHFISCCLQREPAKRWSAMQLLQHPFI 331

                 ....
gi 25143934  286 KQQT 289
Cdd:PLN00034 332 LRAQ 335
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
36-235 1.88e-10

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 61.03  E-value: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVV----YRAvrtcdNALVAVKFIERSNVKEWARINGEQVPMEICMlAKCSKVRGV-IRLLDWYSIPEgfliV 110
Cdd:cd05114  11 ELGSGLFGVVrlgkWRA-----QYKVAIKAIREGAMSEEDFIEEAKVMMKLTH-PKLVQLYGVcTQQKPIYIVTE----F 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpyPCidMFDFIK-GQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQY 189
Cdd:cd05114  81 MEN--GC--LLNYLRqRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVN-DTGVVKVSDFGMTRYVLDDQY 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SDFQGTRL---YCPPEWFLHSLYlGREAAVWSLGVLLYNSLN-GRLPFRN 235
Cdd:cd05114 156 TSSSGAKFpvkWSPPEVFNYSKF-SSKSDVWSFGVLMWEVFTeGKMPFES 204
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
28-234 1.96e-10

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: 61.89  E-value: 1.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarINGEQVPMEICMLaKCSKVRGVIRLLDWYSIPEG- 106
Cdd:cd07880  14 PDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSE---LFAKRAYRELRLL-KHMKHENVIGLLDVFTPDLSl 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 -----FLIVMerPYPCIDMFDFIKGQgKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA 181
Cdd:cd07880  90 drfhdFYLVM--PFMGTDLGKLMKHE-KLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVN-EDCELKILDFGLA 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 182 tvlrRSQYSDFQG---TRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFR 234
Cdd:cd07880 166 ----RQTDSEMTGyvvTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFK 217
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
32-284 2.03e-10

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: 61.09  E-value: 2.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAELGRGGFGVVYRAVRT---CDNALVAVKF-----IERSNVKEwaringeqvpmEICMLaKCSKVRGVIRLLD-WYS 102
Cdd:cd13983   4 KFNEVLGRGSFKTVYRAFDTeegIEVAWNEIKLrklpkAERQRFKQ-----------EIEIL-KSLKHPNIIKFYDsWES 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 103 IPEGFLI-VMErpypcidMF------DFIKGQGKISEDMARFLFRQI---AVTVHECVQNrVLHRDLKDENIVIDLVTGS 172
Cdd:cd13983  72 KSKKEVIfITE-------LMtsgtlkQYLKRFKRLKLKVIKSWCRQIlegLNYLHTRDPP-IIHRDLKCDNIFINGNTGE 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 173 TKLIDFGAATVLRRSQYSDFQGTRLYCPPEwflhsLYLGR--EAA-VWSLGVLLYNSLNGRLPFR---NEKDICTAHLLG 246
Cdd:cd13983 144 VKIGDLGLATLLRQSFAKSVIGTPEFMAPE-----MYEEHydEKVdIYAFGMCLLEMATGEYPYSectNAAQIYKKVTSG 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 25143934 247 PLP--FFVPVSAEVKDLISKCLTfDPFQRCSLEAILNHPW 284
Cdd:cd13983 219 IKPesLSKVKDPELKDFIEKCLK-PPDERPSARELLEHPF 257
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
30-285 2.71e-10

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: 60.81  E-value: 2.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFI-----ERSNVKEwarINGEQVPMEICMLAKCSkvrgviRLLDWYSI- 103
Cdd:cd06653   3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfdpdSQETSKE---VNALECEIQLLKNLRHD------RIVQYYGCl 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 --PEGFLIVMERPY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGA 180
Cdd:cd06653  74 rdPEEKKLSIFVEYmPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRD-SAGNVKLGDFGA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 A----TVLRR-SQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPF--FVP 253
Cdd:cd06653 153 SkriqTICMSgTGIKSVTGTPYWMSPEVISGEGY-GRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTkpQLP 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 254 --VSAEVKDLISKcLTFDPFQRCSLEAILNHPWV 285
Cdd:cd06653 232 dgVSDACRDFLRQ-IFVEEKRRPTAEFLLRHPFV 264
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
31-284 2.81e-10

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: 61.13  E-value: 2.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIE---------RSNVKEWA---RINGEQVP-----MEICMLAKCSKVRG 93
Cdd:cd07863   2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRvqtnedglpLSTVREVAllkRLEAFDHPnivrlMDVCATSRTDRETK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  94 VIRLLDwySIPEGFLIVMER-PYPCIDMfDFIKgqgkiseDMARFLFRQIAVtVHecvQNRVLHRDLKDENIvidLVT-- 170
Cdd:cd07863  82 VTLVFE--HVDQDLRTYLDKvPPPGLPA-ETIK-------DLMRQFLRGLDF-LH---ANCIVHRDLKPENI---LVTsg 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 171 GSTKLIDFGAATVLR-RSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGR------------------- 230
Cdd:cd07863 145 GQVKLADFGLARIYScQMALTPVVVTLWYRAPEVLLQSTY-ATPVDMWSVGCIFAEMFRRKplfcgnseadqlgkifdli 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143934 231 -LPFRNE--KDICTAHLL----GPLPF--FVP-VSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07863 224 gLPPEDDwpRDVTLPRGAfsprGPRPVqsVVPeIEESGAQLLLEMLTFNPHKRISAFRALQHPF 287
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
32-289 3.75e-10

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: 60.48  E-value: 3.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAELGRGGFGVVYRAVRT--------CDNALVAVKFIERSNVKEWAR-INGEQVPmeicmlakcskvrGVIRLLD-WY 101
Cdd:cd14032   4 KFDIELGRGSFKTVYKGLDTetwvevawCELQDRKLTKVERQRFKEEAEmLKGLQHP-------------NIVRFYDfWE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 102 SIPEGflivmerpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQ------------NRVLHRDLKDENIVIDLV 169
Cdd:cd14032  71 SCAKG--------KRCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQilkgllflhtrtPPIIHRDLKCDNIFITGP 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 170 TGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEwfLHSLYLGREAAVWSLGVLLYNSLNGRLPF---RNEKDICTAHLLG 246
Cdd:cd14032 143 TGSVKIGDLGLATLKRASFAKSVIGTPEFMAPE--MYEEHYDESVDVYAFGMCMLEMATSEYPYsecQNAAQIYRKVTCG 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 25143934 247 --PLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQT 289
Cdd:cd14032 221 ikPASFEKVTDPEIKEIIGECICKNKEERYEIKDLLSHAFFAEDT 265
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
37-281 3.92e-10

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: 60.33  E-value: 3.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNV-KEWARingEQVPMEICmLAKCSKVRGVIRLLDWYSIPEGFLIVMERpy 115
Cdd:cd14187  15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLlKPHQK---EKMSMEIA-IHRSLAHQHVVGFHGFFEDNDFVYVVLEL-- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI--DLvtgSTKLIDFGAATVLRR--SQY 189
Cdd:cd14187  89 -CRrrSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLndDM---EVKIGDFGLATKVEYdgERK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SDFQGTRLYCPPEWFL---HSLylgrEAAVWSLGVLLYNSLNGRLPF-------------RNEKDIcTAHLlgplpffVP 253
Cdd:cd14187 165 KTLCGTPNYIAPEVLSkkgHSF----EVDIWSIGCIMYTLLVGKPPFetsclketylrikKNEYSI-PKHI-------NP 232
                       250       260
                ....*....|....*....|....*...
gi 25143934 254 VSAevkDLISKCLTFDPFQRCSLEAILN 281
Cdd:cd14187 233 VAA---SLIQKMLQTDPTARPTINELLN 257
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
124-273 3.95e-10

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: 60.50  E-value: 3.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 124 IKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS---------------Q 188
Cdd:cd05609  91 LKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLIT-SMGHIKLTDFGLSKIGLMSlttnlyeghiekdtrE 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSDFQ--GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNE------KDICTAHLLGP-----LPffvpvs 255
Cdd:cd05609 170 FLDKQvcGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDtpeelfGQVISDEIEWPegddaLP------ 242
                       170
                ....*....|....*...
gi 25143934 256 AEVKDLISKCLTFDPFQR 273
Cdd:cd05609 243 DDAQDLITRLLQQNPLER 260
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
31-284 4.30e-10

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 60.63  E-value: 4.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAV-RTCDNALVAVKFIErsNV---KEWARinGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEG 106
Cdd:cd14213  14 YEIVDTLGEGAFGKVVECIdHKMGGMHVAVKIVK--NVdryREAAR--SEIQVLEHLNTTDPNSTFRCVQMLEWFDHHGH 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMErpYPCIDMFDFIKGQG--KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI------------------ 166
Cdd:cd14213  90 VCIVFE--LLGLSTYDFIKENSflPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFvqsdyvvkynpkmkrder 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 167 DLVTGSTKLIDFGAATvLRRSQYSDFQGTRLYCPPEWFLhSLYLGREAAVWSLGVLLYNSLNGRLPFRN----EKDICTA 242
Cdd:cd14213 168 TLKNPDIKVVDFGSAT-YDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFQThdskEHLAMME 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 243 HLLGPLP---------------------------------------FFVPVSAE---VKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd14213 246 RILGPLPkhmiqktrkrkyfhhdqldwdehssagryvrrrckplkeFMLSQDVDheqLFDLIQKMLEYDPAKRITLDEAL 325

                ....
gi 25143934 281 NHPW 284
Cdd:cd14213 326 KHPF 329
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
23-289 4.53e-10

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: 60.45  E-value: 4.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  23 GFSKFKKNYKLKAELGRGGFGVVYRAVRTcdNALVAVKFIERSNvKEWARINGEQVPMEICMLaKCSKVRGVIRLLD-WY 101
Cdd:cd14030  19 G*SPDGRFLKFDIEIGRGSFKTVYKGLDT--ETTVEVAWCELQD-RKLSKSERQRFKEEAGML-KGLQHPNIVRFYDsWE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 102 SIPEGflivmerpYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQ------------NRVLHRDLKDENIVIDLV 169
Cdd:cd14030  95 STVKG--------KKCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQilkglqflhtrtPPIIHRDLKCDNIFITGP 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 170 TGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSlyLGREAAVWSLGVLLYNSLNGRLPF---RNEKDICTAHLLG 246
Cdd:cd14030 167 TGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEK--YDESVDVYAFGMCMLEMATSEYPYsecQNAAQIYRRVTSG 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 25143934 247 --PLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQT 289
Cdd:cd14030 245 vkPASFDKVAIPEVKEIIEGCIRQNKDERYAIKDLLNHAFFQEET 289
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
24-284 4.97e-10

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: 60.41  E-value: 4.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  24 FSKFKKNYKLKaELGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEWARINGEQvpmEICMLaKCSKVRGVIRLLDWYSI 103
Cdd:cd07871   1 FGKLETYVKLD-KLGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAIR---EVSLL-KNLKHANIVTLHDIIHT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 PEGFLIVMErpYPCIDMFDFIKGQGKIS--EDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA 181
Cdd:cd07871  75 ERCLTLVFE--YLDSDLKQYLDNCGNLMsmHNVKIFMF-QLLRGLSYCHKRKILHRDLKPQNLLIN-EKGELKLADFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TV--LRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR-------------LPFR--------NEKD 238
Cdd:cd07871 151 RAksVPTKTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRpmfpgstvkeelhLIFRllgtpteeTWPG 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 239 IC----------TAHLLGPLPFFVP-VSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07871 231 VTsneefrsylfPQYRAQPLINHAPrLDTDGIDLLSSLLLYETKSRISAEAALRHSY 287
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
122-286 4.99e-10

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: 60.10  E-value: 4.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 122 DFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYS-----DFQGTR 196
Cdd:cd06651 100 DQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRD-SAGNVKLGDFGASKRLQTICMSgtgirSVTGTP 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 197 LYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFVP----VSAEVKDLIsKCLTFDPFQ 272
Cdd:cd06651 179 YWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQlpshISEHARDFL-GCIFVEARH 256
                       170
                ....*....|....
gi 25143934 273 RCSLEAILNHPWVK 286
Cdd:cd06651 257 RPSAEELLRHPFAQ 270
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
37-263 5.02e-10

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: 60.92  E-value: 5.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARingeQVPMEICMLAKCSK-----VRGVIRLLDWYSIPEGFLIVM 111
Cdd:cd14224  73 IGKGSFGQVVKAYDHKTHQHVALKMVR--NEKRFHR----QAAEEIRILEHLKKqdkdnTMNVIHMLESFTFRNHICMTF 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 ErpYPCIDMFDFIKG---QGkisedMARFLFRQIAVTVHECV----QNRVLHRDLKDENIVIDLVTGS-TKLIDFGAATV 183
Cdd:cd14224 147 E--LLSMNLYELIKKnkfQG-----FSLQLVRKFAHSILQCLdalhRNKIIHCDLKPENILLKQQGRSgIKVIDFGSSCY 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQYSDFQgTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGR--LPFRNEKD--ICTAHLLG-PLPFFVPVSAEV 258
Cdd:cd14224 220 EHQRIYTYIQ-SRFYRAPEVILGARY-GMPIDMWSFGCILAELLTGYplFPGEDEGDqlACMIELLGmPPQKLLETSKRA 297

                ....*
gi 25143934 259 KDLIS 263
Cdd:cd14224 298 KNFIS 302
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
126-300 5.04e-10

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: 60.06  E-value: 5.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 126 GQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSDFQ-GTRLYCPPEWF 204
Cdd:cd05605  95 GNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLD-DHGHVRISDLGLAVEIPEGETIRGRvGTVGYMAPEVV 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 205 LHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD----------ICTAhllgPLPFFVPVSAEVKDLISKCLTFDPFQR- 273
Cdd:cd05605 174 KNERY-TFSPDWWGLGCLIYEMIEGQAPFRARKEkvkreevdrrVKED----QEEYSEKFSEEAKSICSQLLQKDPKTRl 248
                       170       180       190
                ....*....|....*....|....*....|.
gi 25143934 274 -CSLEA---ILNHPWVKqqTLSWDALTKNKV 300
Cdd:cd05605 249 gCRGEGaedVKSHPFFK--SINFKRLEAGLL 277
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
29-287 5.50e-10

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: 60.69  E-value: 5.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwarINGEQVPMEICMLaKCSKVRGVIRLLDWY-SIPEG- 106
Cdd:cd07879  15 ERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSE---IFAKRAYRELTLL-KHMQHENVIGLLDVFtSAVSGd 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 ----FLIVMerPYPCIDMfDFIKGQgKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAt 182
Cdd:cd07879  91 efqdFYLVM--PYMQTDL-QKIMGH-PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVN-EDCELKILDFGLA- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 vlrRSQYSDFQG---TRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE----------------------- 236
Cdd:cd07879 165 ---RHADAEMTGyvvTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKdyldqltqilkvtgvpgpefvqk 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143934 237 -KDICTAHLLGPLP---------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd07879 242 lEDKAAKSYIKSLPkyprkdfstLFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDS 302
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
31-287 5.61e-10

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: 60.44  E-value: 5.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNvkeWARINGEQVPMEICMLaKCSKVRGVIRLLDWYSiPEGFLIV 110
Cdd:cd07877  19 YQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPF---QSIIHAKRTYRELRLL-KHMKHENVIGLLDVFT-PARSLEE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERPYPCI-----DMFDFIKGQgKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAtvlR 185
Cdd:cd07877  94 FNDVYLVThlmgaDLNNIVKCQ-KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVN-EDCELKILDFGLA---R 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RS--QYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICT------------AHLLGPLP-- 249
Cdd:cd07877 169 HTddEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQlklilrlvgtpgAELLKKISse 248
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 250 -------------------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd07877 249 sarnyiqsltqmpkmnfanVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQ 305
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
36-233 5.93e-10

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: 60.02  E-value: 5.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEWARINGEQvpmEICMLaKCSKVRGVIRLLDWYSIPEGFLIVMErpY 115
Cdd:cd07873   9 KLGEGTYATVYKGRSKLTDNLVALKEI-RLEHEEGAPCTAIR---EVSLL-KDLKHANIVTLHDIIHTEKSLTLVFE--Y 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKI--SEDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATV--LRRSQYSD 191
Cdd:cd07873  82 LDKDLKQYLDDCGNSinMHNVKLFLF-QLLRGLAYCHRRKVLHRDLKPQNLLIN-ERGELKLADFGLARAksIPTKTYSN 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 25143934 192 FQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPF 233
Cdd:cd07873 160 EVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLF 201
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
31-223 5.94e-10

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 60.49  E-value: 5.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARingeQVPMEICMLAKCSKVRGvirllDWYSIPEGFLIV 110
Cdd:cd14227  17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILK--NHPSYAR----QGQIEVSILARLSTESA-----DDYNFVRAYECF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERPYPCI-------DMFDFIKgQGKISE---DMARFLFRQIAVTVHECVQNRVLHRDLKDENIVidLVTGS-----TKL 175
Cdd:cd14227  86 QHKNHTCLvfemleqNLYDFLK-QNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIM--LVDPSrqpyrVKV 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 25143934 176 IDFGAATVLRRSQYSDFQGTRLYCPPEWFLhSLYLGREAAVWSLGVLL 223
Cdd:cd14227 163 IDFGSASHVSKAVCSTYLQSRYYRAPEIIL-GLPFCEAIDMWSLGCVI 209
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
37-287 6.27e-10

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: 60.04  E-value: 6.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewaRINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVM----- 111
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIK---KRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLtlmng 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 -ERPYPCIDMfdfikGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYS 190
Cdd:cd05630  85 gDLKFHIYHM-----GQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLD-DHGHIRISDLGLAVHVPEGQTI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 191 DFQ-GTRLYCPPEWFLHSLYLgREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLL------GPLPFFVPVSAEVKDLIS 263
Cdd:cd05630 159 KGRvGTVGYMAPEVVKNERYT-FSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVerlvkeVPEEYSEKFSPQARSLCS 237
                       250       260
                ....*....|....*....|....*....
gi 25143934 264 KCLTFDPFQR--C---SLEAILNHPWVKQ 287
Cdd:cd05630 238 MLLCKDPAERlgCrggGAREVKEHPLFKK 266
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
37-301 6.53e-10

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: 59.76  E-value: 6.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewaRINGEQVPM-EICMLAKCSKVRGVirlldwysiPegFLIVMERPY 115
Cdd:cd05606   2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIK---MKQGETLALnERIMLSLVSTGGDC---------P--FIVCMTYAF 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFI-------------KGQGKISEDMARFLFRQIAVTVhECVQNR-VLHRDLKDENIVIDlVTGSTKLIDFGAA 181
Cdd:cd05606  68 QTPDKLCFIldlmnggdlhyhlSQHGVFSEAEMRFYAAEVILGL-EHMHNRfIVYRDLKPANILLD-EHGHVRISDLGLA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK-----DICTAHLLGPLPFFVPVSA 256
Cdd:cd05606 146 CDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKtkdkhEIDRMTLTMNVELPDSFSP 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 25143934 257 EVKDLISKCLTFDPFQR--C---SLEAILNHPWVKqqTLSWDALTKNKVQ 301
Cdd:cd05606 226 ELKSLLEGLLQRDVSKRlgClgrGATEVKEHPFFK--GVDWQQVYLQKYP 273
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
29-223 7.46e-10

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 60.43  E-value: 7.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersnvkewarINGEQVPMEICMLAKCSKVRGVIRLLDWY---SIPE 105
Cdd:PTZ00036  66 KSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV----------LQDPQYKNRELLIMKNLNHINIIFLKDYYyteCFKK 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  106 G----FL-IVMErpYPCIDMFDFIKGQGKISEDMARFLFR----QIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLI 176
Cdd:PTZ00036 136 NekniFLnVVME--FIPQTVHKYMKHYARNNHALPLFLVKlysyQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLKLC 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 25143934  177 DFGAATVLRRSQYS-DFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLL 223
Cdd:PTZ00036 214 DFGSAKNLLAGQRSvSYICSRFYRAPELMLGATNYTTHIDLWSLGCII 261
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
136-233 8.31e-10

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: 59.38  E-value: 8.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 136 RFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST--KLIDFGAATVL-RRSQYSDFQGTRLYCPPEWFLHSLYlGR 212
Cdd:cd13989 105 RTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRViyKLIDLGYAKELdQGSLCTSFVGTLQYLAPELFESKKY-TC 183
                        90       100
                ....*....|....*....|.
gi 25143934 213 EAAVWSLGVLLYNSLNGRLPF 233
Cdd:cd13989 184 TVDYWSFGTLAFECITGYRPF 204
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
32-281 8.47e-10

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 59.45  E-value: 8.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAELGRGGFGVVYRAVRTCDNALVAVK-FIERSNVKEWARINgeqvpmEICMLAKCSKVRGVIRLLDWYSIPEG---- 106
Cdd:cd14036   3 RIKRVIAEGGFAFVYEAQDVGTGKEYALKrLLSNEEEKNKAIIQ------EINFMKKLSGHPNIVQFCSAASIGKEesdq 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 ----FLIVMERpypC----IDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNR--VLHRDLKDENIVIDlVTGSTKLI 176
Cdd:cd14036  77 gqaeYLLLTEL---CkgqlVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIG-NQGQIKLC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAATVL-----------RRSQYSD---FQGTRLYCPPEWF-LHSLY-LGREAAVWSLGVLLYNSLNGRLPFRNEKD-- 238
Cdd:cd14036 153 DFGSATTEahypdyswsaqKRSLVEDeitRNTTPMYRTPEMIdLYSNYpIGEKQDIWALGCILYLLCFRKHPFEDGAKlr 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 25143934 239 ICTAHLLGPlpffvPVSAEVK---DLISKCLTFDPFQRCSLEAILN 281
Cdd:cd14036 233 IINAKYTIP-----PNDTQYTvfhDLIRSTLKVNPEERLSITEIVE 273
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
31-285 8.88e-10

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: 58.99  E-value: 8.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQvpmEICMLAKCsKVRGVIRLLDWYSIPEGFL-I 109
Cdd:cd08223   2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQ---EAKLLSKL-KHPNIVSYKESFEGEDGFLyI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERpypCI--DMFDFIKGQ-GK-ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLR 185
Cdd:cd08223  78 VMGF---CEggDLYTRLKEQkGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTK-SNIIKVGDLGIARVLE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RS--QYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFrNEKDICTAH---LLGPLPfFVP--VSAEV 258
Cdd:cd08223 154 SSsdMATTLIGTPYYMSPELFSNKPY-NHKSDVWALGCCVYEMATLKHAF-NAKDMNSLVykiLEGKLP-PMPkqYSPEL 230
                       250       260
                ....*....|....*....|....*..
gi 25143934 259 KDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd08223 231 GELIKAMLHQDPEKRPSVKRILRQPYI 257
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
27-284 8.90e-10

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 60.02  E-value: 8.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGVVYRAVRTC-DNALVAVKFIErsNVKEWAringEQVPMEICMLAKCSKVRGVIRLL-----DW 100
Cdd:cd14214  11 LQERYEIVGDLGEGTFGKVVECLDHArGKSQVALKIIR--NVGKYR----EAARLEINVLKKIKEKDKENKFLcvlmsDW 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 101 YSIPEGFLIVMERPYPciDMFDFIKGQGKISEDMA--RFLFRQIAVTVHECVQNRVLHRDLKDENIVI------------ 166
Cdd:cd14214  85 FNFHGHMCIAFELLGK--NTFEFLKENNFQPYPLPhiRHMAYQLCHALKFLHENQLTHTDLKPENILFvnsefdtlynes 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 167 ------DLVTGSTKLIDFGAATvLRRSQYSDFQGTRLYCPPEWFLHsLYLGREAAVWSLGVLLYNSLNGRLPFRNEKD-- 238
Cdd:cd14214 163 ksceekSVKNTSIRVADFGSAT-FDHEHHTTIVATRHYRPPEVILE-LGWAQPCDVWSLGCILFEYYRGFTLFQTHENre 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 239 --ICTAHLLGPLP-----------FF-------------------------------VPVSAEVKDLISKCLTFDPFQRC 274
Cdd:cd14214 241 hlVMMEKILGPIPshmihrtrkqkYFykgslvwdenssdgryvsenckplmsymlgdSLEHTQLFDLLRRMLEFDPALRI 320
                       330
                ....*....|
gi 25143934 275 SLEAILNHPW 284
Cdd:cd14214 321 TLKEALLHPF 330
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
23-233 9.71e-10

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: 59.62  E-value: 9.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  23 GFSKFKKNYKLKaELGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEWARINGEQvpmEICMLaKCSKVRGVIRLLDWYS 102
Cdd:cd07872   1 GFGKMETYIKLE-KLGEGTYATVFKGRSKLTENLVALKEI-RLEHEEGAPCTAIR---EVSLL-KDLKHANIVTLHDIVH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 103 IPEGFLIVMErpYPCIDMFDFIKGQGKIS--EDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGA 180
Cdd:cd07872  75 TDKSLTLVFE--YLDKDLKQYMDDCGNIMsmHNVKIFLY-QILRGLAYCHRRKVLHRDLKPQNLLIN-ERGELKLADFGL 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 181 ATV--LRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPF 233
Cdd:cd07872 151 ARAksVPTKTYSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLF 205
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
119-286 1.01e-09

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: 59.56  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQ--GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI-----------DLVTGS---TKLIDFGAAT 182
Cdd:cd05574  87 ELFRLLQKQpgKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLhesghimltdfDLSKQSsvtPPPVRKSLRK 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 183 VLRRSQYSDFQGTRLYCPPEWFLHSL-----YL--------GREAAV--WSLGVLLYNSLNGRLPFR--NEKDICTAHLL 245
Cdd:cd05574 167 GSRRSSVKSIEKETFVAEPSARSNSFvgteeYIapevikgdGHGSAVdwWTLGILLYEMLYGTTPFKgsNRDETFSNILK 246
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 25143934 246 GPLPF--FVPVSAEVKDLISKCLTFDPFQRCSLEA----ILNHPWVK 286
Cdd:cd05574 247 KELTFpeSPPVSSEAKDLIRKLLVKDPSKRLGSKRgaseIKRHPFFR 293
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
31-284 1.19e-09

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: 58.93  E-value: 1.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersnvkewaRINGEQ-VPM----EICMLaKCSKVRGVIRLLDWYSIPE 105
Cdd:cd07844   2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEI---------RLEHEEgAPFtairEASLL-KDLKHANIVTLHDIIHTKK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMErpYPCIDMFDFIKGQGK-ISEDMAR-FLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG---A 180
Cdd:cd07844  72 TLTLVFE--YLDTDLKQYMDDCGGgLSMHNVRlFLF-QLLRGLAYCHQRRVLHRDLKPQNLLIS-ERGELKLADFGlarA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRSqYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDIC----------------TAHL 244
Cdd:cd07844 148 KSVPSKT-YSNEVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVEdqlhkifrvlgtpteeTWPG 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 245 LGPLPFFVPVS-------------------AEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07844 227 VSSNPEFKPYSfpfypprplinhaprldriPHGEELALKFLQYEPKKRISAAEAMKHPY 285
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
36-282 1.28e-09

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: 58.70  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRA-VRTCDNA--LVAVKFIersnvKEWARiNGEQVPM--EICMLakcSKVR--GVIRLLDWYSIPEGFL 108
Cdd:cd00192   2 KLGEGAFGEVYKGkLKGGDGKtvDVAVKTL-----KEDAS-ESERKDFlkEARVM---KKLGhpNVVRLLGVCTEEEPLY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVME--------------RPYPCIDMFDFIKgqgkiSEDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTK 174
Cdd:cd00192  73 LVMEymeggdlldflrksRPVFPSPEPSTLS-----LKDLLSFAI-QIAKGMEYLASKKFVHRDLAARNCLVG-EDLVVK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 175 LIDFGAATVLRRSQYSDFQ-GTRL---YCPPEWFLHSLYlGREAAVWSLGVLLYN--SLnGRLPF---RNE---KDICTA 242
Cdd:cd00192 146 ISDFGLSRDIYDDDYYRKKtGGKLpirWMAPESLKDGIF-TSKSDVWSFGVLLWEifTL-GATPYpglSNEevlEYLRKG 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 25143934 243 HLLgPLPFFVPvsAEVKDLISKCLTFDPFQRCSLEAILNH 282
Cdd:cd00192 224 YRL-PKPENCP--DELYELMLSCWQLDPEDRPTFSELVER 260
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
37-207 1.40e-09

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 58.99  E-value: 1.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALvavKFIERSNVKEwARINGEqvpMEICMLAKCSKVRG----------VIRLLDWYSIPEG 106
Cdd:cd14013   3 LGEGGFGTVYKGSLLQKDPG---GEKRRVVLKK-AKEYGE---VEIWMNERVRRACPsscaefvgafLDTTSKKFTKPSL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLI------------VMERPYP-CIDMFDFIKGQGKISEDMARFL-----FRQIAVTVHECVQNRVLHRDLKDENIVIDL 168
Cdd:cd14013  76 WLVwkyegdatladlMQGKEFPyNLEPIIFGRVLIPPRGPKRENViiksiMRQILVALRKLHSTGIVHRDVKPQNIIVSE 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 25143934 169 VTGSTKLIDFGAATVLRRS-QYS--DFQGTRLYCPPEWFLHS 207
Cdd:cd14013 156 GDGQFKIIDLGAAADLRIGiNYIpkEFLLDPRYAPPEQYIMS 197
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
37-233 1.43e-09

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: 58.82  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIErsnvKEWARINGEQVPMEICMLAKCSKVrGVIRLLDwysIPEGF--------- 107
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCR----QELSPKNRERWCLEIQIMKRLNHP-NVVAARD---VPEGLqklapndlp 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVME-------RPYpcIDMFDFIKGqgkISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVidLVTGST----KLI 176
Cdd:cd14038  74 LLAMEycqggdlRKY--LNQFENCCG---LREGAILTLLSDISSALRYLHENRIIHRDLKPENIV--LQQGEQrlihKII 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAATVLRRSQY-SDFQGTRLYCPPEWFLHSLYlgrEAAV--WSLGVLLYNSLNGRLPF 233
Cdd:cd14038 147 DLGYAKELDQGSLcTSFVGTLQYLAPELLEQQKY---TVTVdyWSFGTLAFECITGFRPF 203
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
32-280 1.55e-09

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: 58.42  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAELGRGGFGVVYRAVRTCDNAlVAVKFIERSNVKEWARINGEQVPMEICMlakcskvrgvIRLLDWYSIpegfliVM 111
Cdd:cd05112   7 TFVQEIGSGQFGLVHLGYWLNKDK-VAIKTIREGAMSEEDFIEEAEVMMKLSH----------PKLVQLYGV------CL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 ERPYPCIdMFDFIKgQGKISEDM--ARFLFRQ-----IAVTVHECV----QNRVLHRDLKDENIVIDlVTGSTKLIDFGA 180
Cdd:cd05112  70 EQAPICL-VFEFME-HGCLSDYLrtQRGLFSAetllgMCLDVCEGMayleEASVIHRDLAARNCLVG-ENQVVKVSDFGM 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRSQYSDFQGTRL---YCPPEWFLHSLYlGREAAVWSLGVLLYNSLN-GRLPFRNE------KDICTAHLLgplpf 250
Cdd:cd05112 147 TRFVLDDQYTSSTGTKFpvkWSSPEVFSFSRY-SSKSDVWSFGVLMWEVFSeGKIPYENRsnsevvEDINAGFRL----- 220
                       250       260       270
                ....*....|....*....|....*....|..
gi 25143934 251 FVP--VSAEVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd05112 221 YKPrlASTHVYEIMNHCWKERPEDRPSFSLLL 252
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
30-284 1.56e-09

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: 58.94  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIersnvkewaRINGEQ----VPMEICMLAKCSKVRGVIRLLDWYSIPE 105
Cdd:cd07869   6 SYEKLEKLGEGSYATVYKGKSKVNGKLVALKVI---------RLQEEEgtpfTAIREASLLKGLKHANIVLLHDIIHTKE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMErpYPCIDMFDFI-KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATV- 183
Cdd:cd07869  77 TLTLVFE--YVHTDLCQYMdKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLIS-DTGELKLADFGLARAk 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 -LRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTA-----HLLG----------- 246
Cdd:cd07869 154 sVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQlerifLVLGtpnedtwpgvh 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 247 PLPFFVP-------------------VSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07869 234 SLPHFKPerftlyspknlrqawnklsYVNHAEDLASKLLQCFPKNRLSAQAALSHEY 290
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
29-283 1.64e-09

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: 59.12  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVkewarING---EQVPMEICMLAkCSKVRGVIRLldWYSIPE 105
Cdd:cd05610   4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADM-----INKnmvHQVQAERDALA-LSKSPFIVHL--YYSLQS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 G--FLIVMERPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATV 183
Cdd:cd05610  76 AnnVYLVMEYLIGG-DVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLIS-NEGHIKLTDFGLSKV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 -LRRS-QYSDF------------------------------------------------QGTRLYCPPEWFLHSLYLGR- 212
Cdd:cd05610 154 tLNRElNMMDIlttpsmakpkndysrtpgqvlslisslgfntptpyrtpksvrrgaarvEGERILGTPDYLAPELLLGKp 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 213 -EAAV--WSLGVLLYNSLNGRLPFRNE-----------KDIctahllgPLPFF-VPVSAEVKDLISKCLTFDPFQRCSLE 277
Cdd:cd05610 234 hGPAVdwWALGVCLFEFLTGIPPFNDEtpqqvfqnilnRDI-------PWPEGeEELSVNAQNAIEILLTMDPTKRAGLK 306

                ....*.
gi 25143934 278 AILNHP 283
Cdd:cd05610 307 ELKQHP 312
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
127-300 1.66e-09

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: 58.97  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 127 QGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR--SQYSDFQGTRLYCPPEwF 204
Cdd:cd05588  90 QRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLD-SEGHIKLTDYGMCKEGLRpgDTTSTFCGTPNYIAPE-I 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 205 LHSLYLGREAAVWSLGVLLYNSLNGRLPF----------RNEKDICTAHLLGPlPFFVPVSAEVK--DLISKCLTFDPFQ 272
Cdd:cd05588 168 LRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnpdQNTEDYLFQVILEK-PIRIPRSLSVKaaSVLKGFLNKNPAE 246
                       170       180       190
                ....*....|....*....|....*....|....
gi 25143934 273 R--CSLEA----ILNHPWVKqqTLSWDALTKNKV 300
Cdd:cd05588 247 RlgCHPQTgfadIQSHPFFR--TIDWEQLEQKQV 278
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
37-284 1.67e-09

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: 58.92  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIerSNVKEwARINGEQVPMEICMLAKCS-----KVRGVIRLLDWYSIPEGFLI-- 109
Cdd:cd07858  13 IGRGAYGIVCSAKNSETNEKVAIKKI--ANAFD-NRIDAKRTLREIKLLRHLDhenviAIKDIMPPPHREAFNDVYIVye 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMErpypcIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI----DLvtgstKLIDFGAATVlr 185
Cdd:cd07858  90 LMD-----TDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLnancDL-----KICDFGLART-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQG----TRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLnGRLP----------------------------F 233
Cdd:cd07858 158 TSEKGDFMTeyvvTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELL-GRKPlfpgkdyvhqlklitellgspseedlgfI 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 234 RNEKDICTAHLLGPLP------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07858 237 RNEKARRYIRSLPYTPrqsfarLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPY 293
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
30-286 1.87e-09

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: 58.47  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIER-SNVKEWARI---------NGEQVPMEICMLAKCSKVRG-----V 94
Cdd:cd06639  23 TWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPiSDVDEEIEAeynilrslpNHPNVVKFYGMFYKADQYVGgqlwlV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  95 IRLLDWYSIPE---GFLIVMERpypcidmfdfikgqgkISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTG 171
Cdd:cd06639 103 LELCNGGSVTElvkGLLKCGQR----------------LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT-TEG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 172 STKLIDFG-----AATVLRRSQYSdfqGTRLYCPPEWF-----LHSLYLGReAAVWSLGVLLYNSLNGRLPFrneKDICT 241
Cdd:cd06639 166 GVKLVDFGvsaqlTSARLRRNTSV---GTPFWMAPEVIaceqqYDYSYDAR-CDVWSLGITAIELADGDPPL---FDMHP 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 25143934 242 AHLLGPLPFFVPVS--------AEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06639 239 VKALFKIPRNPPPTllnpekwcRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
30-223 2.32e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 58.56  E-value: 2.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARingeQVPMEICMLAKCSKVRGvirllDWYSIPEGFLI 109
Cdd:cd14228  16 SYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILK--NHPSYAR----QGQIEVSILSRLSSENA-----DEYNFVRSYEC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYPCI-------DMFDFIKgQGKISE---DMARFLFRQIAVTVHECVQNRVLHRDLKDENI-VIDLVTG--STKLI 176
Cdd:cd14228  85 FQHKNHTCLvfemleqNLYDFLK-QNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENImLVDPVRQpyRVKVI 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 25143934 177 DFGAATVLRRSQYSDFQGTRLYCPPEWFLhSLYLGREAAVWSLGVLL 223
Cdd:cd14228 164 DFGSASHVSKAVCSTYLQSRYYRAPEIIL-GLPFCEAIDMWSLGCVI 209
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
28-279 2.94e-09

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: 57.74  E-value: 2.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYR---------AVRTCDNALVAVK-FIERSN----------VKEWARINGEQvPMEICM--L 85
Cdd:cd05072   6 RESIKLVKKLGAGQFGEVWMgyynnstkvAVKTLKPGTMSVQaFLEEANlmktlqhdklVRLYAVVTKEE-PIYIITeyM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  86 AKCSkvrgvirLLDWYSIPEGFLIVMERpypcidMFDFikgQGKISEDMArFLFRQiavtvhecvqnRVLHRDLKDENIv 165
Cdd:cd05072  85 AKGS-------LLDFLKSDEGGKVLLPK------LIDF---SAQIAEGMA-YIERK-----------NYIHRDLRAANV- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 166 idLVTGS--TKLIDFGAATVLRRSQYSDFQGTRLycPPEWFL-HSLYLGR---EAAVWSLGVLLYNSLN-GRLPF--RNE 236
Cdd:cd05072 136 --LVSESlmCKIADFGLARVIEDNEYTAREGAKF--PIKWTApEAINFGSftiKSDVWSFGILLYEIVTyGKIPYpgMSN 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 25143934 237 KDICTAHLLG-PLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd05072 212 SDVMSALQRGyRMPRMENCPDELYDIMKTCWKEKAEERPTFDYL 255
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
37-234 2.95e-09

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: 58.27  E-value: 2.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFierSNVKEWARingeqvPMEICM-----LAKCSKvRGVIRLldwYSIPE-----G 106
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKV---FNNLSFMR------PLDVQMrefevLKKLNH-KNIVKL---FAIEEelttrH 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERpYPCIDMFDFIKGQGK---ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENI--VIDlVTGST--KLIDFG 179
Cdd:cd13988  68 KVLVMEL-CPCGSLYTVLEEPSNaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNImrVIG-EDGQSvyKLTDFG 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25143934 180 AATVLRRS-QYSDFQGTRLYCPPEWF-------LHSLYLGREAAVWSLGVLLYNSLNGRLPFR 234
Cdd:cd13988 146 AARELEDDeQFVSLYGTEEYLHPDMYeravlrkDHQKKYGATVDLWSIGVTFYHAATGSLPFR 208
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
37-287 3.05e-09

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: 58.14  E-value: 3.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNvkeWARINGEQVPMEICMLaKCSKVRGVIRLLDWY----SIPEGFLIVME 112
Cdd:cd07878  23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRPF---QSLIHARRTYRELRLL-KHMKHENVIGLLDVFtpatSIENFNEVYLV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 RPYPCIDMFDFIKGQgKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAtvlRRS--QYS 190
Cdd:cd07878  99 TNLMGADLNNIVKCQ-KLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVN-EDCELRILDFGLA---RQAddEMT 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 191 DFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE---------------------KDICTAHL----- 244
Cdd:cd07878 174 GYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNdyidqlkrimevvgtpspevlKKISSEHArkyiq 253
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 25143934 245 -LGPLP------FFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd07878 254 sLPHMPqqdlkkIFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFSQ 303
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
37-283 3.13e-09

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: 57.62  E-value: 3.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAvrTCDNALVAVKFIE----RSNVKEWARINGEQVPMEICMLAKCSkVRGVIRLLDWYSIP-------- 104
Cdd:cd14000   2 LGDGGFGSVYRA--SYKGEPVAVKIFNkhtsSNFANVPADTMLRHLRATDAMKNFRL-LRQELTVLSHLHHPsivyllgi 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 --EGFLIVME-RPYPCIDMFdfIKGQGKISEDMARFLFRQIAVTVHECVQ----NRVLHRDLKDENIVI-DLVTGS---T 173
Cdd:cd14000  79 giHPLMLVLElAPLGSLDHL--LQQDSRSFASLGRTLQQRIALQVADGLRylhsAMIIYRDLKSHNVLVwTLYPNSaiiI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 174 KLIDFGAATVLRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLP------FRNEKDIctaHLLGP 247
Cdd:cd14000 157 KIADYGISRQCCRMGAKGSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPmvghlkFPNEFDI---HGGLR 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 25143934 248 LPFFVPVSA---EVKDLISKCLTFDPFQR---CSLEAILNHP 283
Cdd:cd14000 234 PPLKQYECApwpEVEVLMKKCWKENPQQRptaVTVVSILNSP 275
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
31-282 4.37e-09

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


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 57.31  E-value: 4.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFI---ERSNVKEWARingeqvpmEICMlakCSKVR--GVIRLLDWYSIPE 105
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKIlchSKEDVKEAMR--------EIEN---YRLFNhpNILRLLDSQIVKE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GF---LIVMERPY----PCIDMFDFIKGQGK-ISEDMARFLFRQI--AV-TVHECVQNRVLHRDLKDENIVIDLvTGSTK 174
Cdd:cd13986  71 AGgkkEVYLLLPYykrgSLQDEIERRLVKGTfFPEDRILHIFLGIcrGLkAMHEPELVPYAHRDIKPGNVLLSE-DDEPI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 175 LIDFGAATVLR-----RSQYSDFQ------GTRLYCPPEWF---LHSLYLGReAAVWSLGVLLYNSLNGRLPFRNEKD-- 238
Cdd:cd13986 150 LMDLGSMNPARieiegRREALALQdwaaehCTMPYRAPELFdvkSHCTIDEK-TDIWSLGCTLYALMYGESPFERIFQkg 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 25143934 239 ------ICTAHLLGPLPFfvPVSAEVKDLISKCLTFDPFQRCSLEAILNH 282
Cdd:cd13986 229 dslalaVLSGNYSFPDNS--RYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
37-237 4.46e-09

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: 57.76  E-value: 4.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVK----EWARINgEQVPMEICMLAKCSKVrgvIRLLDWYSIPEGFLIVME 112
Cdd:cd05633  13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmkqgETLALN-ERIMLSLVSTGDCPFI---VCMTYAFHTPDKLCFILD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 RPYPCiDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSDF 192
Cdd:cd05633  89 LMNGG-DLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHVRISDLGLACDFSKKKPHAS 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 25143934 193 QGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK 237
Cdd:cd05633 167 VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHK 211
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
37-237 4.47e-09

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: 57.75  E-value: 4.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewaRINGEQVPMeicmlakcsKVRGVIRLLDWYSIPegFLIVMERPYP 116
Cdd:cd14223   8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIK---MKQGETLAL---------NERIMLSLVSTGDCP--FIVCMSYAFH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFI-------------KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATV 183
Cdd:cd14223  74 TPDKLSFIldlmnggdlhyhlSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLD-EFGHVRISDLGLACD 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 25143934 184 LRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK 237
Cdd:cd14223 153 FSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHK 206
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
29-284 5.10e-09

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: 57.35  E-value: 5.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAvRTCDNA--LVAVKFIersnvkewaRINGEQVPMEICMLAKCSKVR--------GVIRLL 98
Cdd:cd07862   1 QQYECVAEIGEGAYGKVFKA-RDLKNGgrFVALKRV---------RVQTGEEGMPLSTIREVAVLRhletfehpNVVRLF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  99 DWYSIPE-----GFLIVMERPYPCIDMF-DFIKGQGKISE---DMARFLFRQIAVtVHecvQNRVLHRDLKDENIVIDlV 169
Cdd:cd07862  71 DVCTVSRtdretKLTLVFEHVDQDLTTYlDKVPEPGVPTEtikDMMFQLLRGLDF-LH---SHRVVHRDLKPQNILVT-S 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 170 TGSTKLIDFGAATVLR-RSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI--------- 239
Cdd:cd07862 146 SGQIKLADFGLARIYSfQMALTSVVVTLWYRAPEVLLQSSY-ATPVDLWSVGCIFAEMFRRKPLFRGSSDVdqlgkildv 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 240 -------------------CTAHLLGPLPFFVPVSAEV-KDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd07862 225 iglpgeedwprdvalprqaFHSKSAQPIEKFVTDIDELgKDLLLKCLTFNPAKRISAYSALSHPY 289
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
37-253 5.23e-09

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: 56.77  E-value: 5.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAvrTCDNALVAVK------FIERSNVKEWARingeQVPMeICMLAKCSKVRGVIRLLDwysIPEGFLIV 110
Cdd:cd14064   1 IGSGSFGKVYKG--RCRNKIVAIKryrantYCSKSDVDMFCR----EVSI-LCRLNHPCVIQFVGACLD---DPSQFAIV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFIKGQGKISEDMARFLfrqIAVTV-------HECVQNrVLHRDLKDENIVIDlVTGSTKLIDFGAATV 183
Cdd:cd14064  71 TQY-VSGGSLFSLLHEQKRVIDLQSKLI---IAVDVakgmeylHNLTQP-IIHRDLNSHNILLY-EDGHAVVADFGESRF 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 184 LRRSQYSDFQ---GTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK------DICTAHLLGPLPFFVP 253
Cdd:cd14064 145 LQSLDEDNMTkqpGNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLTGEIPFAHLKpaaaaaDMAYHHIRPPIGYSIP 223
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
37-233 6.53e-09

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: 56.85  E-value: 6.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKF----IERSNVKEWARingeqvpmEICMLAKCSKVrGVIRLLDwysIPEGFLIVME 112
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKScrleLSVKNKDRWCH--------EIQIMKKLNHP-NVVKACD---VPEEMNFLVN 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 rPYPCIDMFDFIKGQGK-----------ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGST--KLIDFG 179
Cdd:cd14039  69 -DVPLLAMEYCSGGDLRkllnkpenccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIvhKIIDLG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 180 AATVLRR-SQYSDFQGTRLYCPPEWFLHSLYlgrEAAV--WSLGVLLYNSLNGRLPF 233
Cdd:cd14039 148 YAKDLDQgSLCTSFVGTLQYLAPELFENKSY---TVTVdyWSFGTMVFECIAGFRPF 201
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
36-287 1.24e-08

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: 56.18  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMeicmlaKCSKVRGVIRLLDWYSIPEGFLIVMErpy 115
Cdd:cd06657  27 KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNEVVIM------RDYQHENVVEMYNSYLVGDELWVVME--- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 pcidmfdFIKGqGKISEDMA--RFLFRQIAVTVHECVQ-------NRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRR 186
Cdd:cd06657  98 -------FLEG-GALTDIVThtRMNEEQIAAVCLAVLKalsvlhaQGVIHRDIKSDSILLTH-DGRVKLSDFGFCAQVSK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 S--QYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHL----LGP-LPFFVPVSAEVK 259
Cdd:cd06657 169 EvpRRKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMirdnLPPkLKNLHKVSPSLK 247
                       250       260
                ....*....|....*....|....*...
gi 25143934 260 DLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd06657 248 GFLDRLLVRDPAQRATAAELLKHPFLAK 275
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
119-300 1.27e-08

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: 56.58  E-value: 1.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 119 DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRR--SQYSDFQGTR 196
Cdd:cd05618 107 DLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLD-SEGHIKLTDYGMCKEGLRpgDTTSTFCGTP 185
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 197 LYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF----------RNEKDICTAHLLGPlPFFVPVSAEVK--DLISK 264
Cdd:cd05618 186 NYIAPEILRGEDY-GFSVDWWALGVLMFEMMAGRSPFdivgssdnpdQNTEDYLFQVILEK-QIRIPRSLSVKaaSVLKS 263
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 25143934 265 CLTFDPFQR------CSLEAILNHPWVKQqtLSWDALTKNKV 300
Cdd:cd05618 264 FLNKDPKERlgchpqTGFADIQGHPFFRN--VDWDLMEQKQV 303
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
37-238 1.29e-08

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: 55.77  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewaRINGEQVPM-EICMLAKCSKvRGVIRLLDWYSIPEGFLIVM---- 111
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIK---KRKGEAMALnEKRILEKVNS-RFVVSLAYAYETKDALCLVLtimn 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 --ERPYPCIDMfdfikGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQY 189
Cdd:cd05631  84 ggDLKFHIYNM-----GNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLD-DRGHIRISDLGLAVQIPEGET 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 25143934 190 SDFQ-GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKD 238
Cdd:cd05631 158 VRGRvGTVGYMAPEVINNEKY-TFSPDWWGLGCLIYEMIQGQSPFRKRKE 206
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
31-285 1.34e-08

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: 56.08  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAV-RTCDNALVAVKFIeRSNvkEWARINGEQvpmEICMLAKCSKV-----RGVIRLLDWYSIP 104
Cdd:cd14135   2 YRVYGYLGKGVFSNVVRARdLARGNQEVAIKII-RNN--ELMHKAGLK---ELEILKKLNDAdpddkKHCIRLLRHFEHK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVMErpypCIDM--FDFIKGQGK---ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFG 179
Cdd:cd14135  76 NHLCLVFE----SLSMnlREVLKKYGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTLKLCDFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVLRRSQYSDFQGTRLYCPPEWFLHSLYlgrEAA--VWSLGVLLYNSLNGRLPF----RNEKDICTAHLLGPLP---- 249
Cdd:cd14135 152 SASDIGENEITPYLVSRFYRAPEIILGLPY---DYPidMWSVGCTLYELYTGKILFpgktNNHMLKLMMDLKGKFPkkml 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 250 --------------------------------------------FFVPVS----------AEVKDLISKCLTFDPFQRCS 275
Cdd:cd14135 229 rkgqfkdqhfdenlnfiyrevdkvtkkevrrvmsdikptkdlktLLIGKQrlpdedrkklLQLKDLLDKCLMLDPEKRIT 308
                       330
                ....*....|
gi 25143934 276 LEAILNHPWV 285
Cdd:cd14135 309 PNEALQHPFI 318
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
31-283 1.43e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 56.39  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   31 YKLKAELGRGGFGVVYRAVRTCDNalvavkfiERSNVKEWARINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIV 110
Cdd:PHA03207  94 YNILSSLTPGSEGEVFVCTKHGDE--------QRKKVIVKAVTGGKTPGREIDILKTISH-RAIINLIHAYRWKSTVCMV 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  111 MeRPYPCiDMFDFIKGQGKISEDMARFLFRQIA---VTVHEcvqNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS 187
Cdd:PHA03207 165 M-PKYKC-DLFTYVDRSGPLPLEQAITIQRRLLealAYLHG---RGIIHRDVKTENIFLD-EPENAVLGDFGAACKLDAH 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  188 QYS----DFQGTRLYCPPEWFLHSLYLGReAAVWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPL--------------- 248
Cdd:PHA03207 239 PDTpqcyGWSGTLETNSPELLALDPYCAK-TDIWSAGLVLFEMSVKNVTLFGKQVKSSSSQLRSIircmqvhplefpqng 317
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934  249 -----------------PFFVP-------VSAEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:PHA03207 318 stnlckhfkqyaivlrpPYTIPpvirkygMHMDVEYLIAKMLTFDQEFRPSAQDILSLP 376
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
30-273 1.52e-08

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 55.81  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEwARINGEQVPmEICMLAKCSKvRGVIRLLDWYSIPEGFLI 109
Cdd:cd08229  25 NFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMD-AKARADCIK-EIDLLKQLNH-PNVIKYYASFIEDNELNI 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VMERPYP--CIDMFDFIKGQGK-ISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVL-- 184
Cdd:cd08229 102 VLELADAgdLSRMIKHFKKQKRlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFIT-ATGVVKLGDLGLGRFFss 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYSDFQGTRLYCPPEWfLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEK----DICTAHL---LGPLPfFVPVSAE 257
Cdd:cd08229 181 KTTAAHSLVGTPYYMSPER-IHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKmnlySLCKKIEqcdYPPLP-SDHYSEE 258
                       250
                ....*....|....*.
gi 25143934 258 VKDLISKCLTFDPFQR 273
Cdd:cd08229 259 LRQLVNMCINPDPEKR 274
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
8-285 1.76e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 55.86  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   8 QFFNLKLllnGESSrgFSKFKKNYKLKAeLGRGGFGVVYRAVRTCDNALVAVKFIER--SNVKEWARINGEQVpmeicmL 85
Cdd:cd07874   2 QFYSVEV---GDST--FTVLKRYQNLKP-IGSGAQGIVCAAYDAVLDRNVAIKKLSRpfQNQTHAKRAYRELV------L 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  86 AKCSKVRGVIRLLDWYSiPEGFLIVMERPYPCIDMFDFIKGQ---GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDE 162
Cdd:cd07874  70 MKCVNHKNIISLLNVFT-PQKSLEEFQDVYLVMELMDANLCQviqMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 163 NIVIDlVTGSTKLIDFGAATVLRRS-QYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI-- 239
Cdd:cd07874 149 NIVVK-SDCTLKILDFGLARTAGTSfMMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGEMVRHKILFPGRDYIdq 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 240 ---CTAHLLGPLPFFV-------------------------------PVSAE--------VKDLISKCLTFDPFQRCSLE 277
Cdd:cd07874 227 wnkVIEQLGTPCPEFMkklqptvrnyvenrpkyagltfpklfpdslfPADSEhnklkasqARDLLSKMLVIDPAKRISVD 306

                ....*...
gi 25143934 278 AILNHPWV 285
Cdd:cd07874 307 EALQHPYI 314
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
28-279 2.62e-08

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: 54.75  E-value: 2.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAvRTCDNALVAVKFIERSN-------VKEWARINGEQVPMEICMLAKCSKVRGVirlldw 100
Cdd:cd05148   5 REEFTLERKLGSGYFGEVWEG-LWKNRVRVAIKILKSDDllkqqdfQKEVQALKRLRHKHLISLFAVCSVGEPV------ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 101 YSIPEgfliVMERPypciDMFDFIKGQGKISEDMARFLF--RQIAVTVHECVQNRVLHRDLKDENIVI--DLVTgstKLI 176
Cdd:cd05148  78 YIITE----LMEKG----SLLAFLRSPEGQVLPVASLIDmaCQVAEGMAYLEEQNSIHRDLAARNILVgeDLVC---KVA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFGAATVLRRSQY--SDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLN-GRLPF--RNEK---DICTAHLLGPL 248
Cdd:cd05148 147 DFGLARLIKEDVYlsSDKKIPYKWTAPEAASHGTF-STKSDVWSFGILLYEMFTyGQVPYpgMNNHevyDQITAGYRMPC 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 25143934 249 PFFVPvsAEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd05148 226 PAKCP--QEIYKIMLECWAAEPEDRPSFKAL 254
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
37-179 2.97e-08

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: 52.44  E-value: 2.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKF--IERSNVKEWARingeqvpMEICMLAKCSKVR-GVIRLLDWYSIPEGFLIVME- 112
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIgdDVNNEEGEDLE-------SEMDILRRLKGLElNIPKVLVTEDVDGPNILLMEl 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 113 -RPYPCidmFDFIKGQGKISEDMARFlFRQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTKLIDFG 179
Cdd:cd13968  74 vKGGTL---IAYTQEEELDEKDVESI-MYQLAECMRLLHSFHLIHRDLNNDNILLSE-DGNVKLIDFG 136
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
36-279 3.14e-08

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: 54.58  E-value: 3.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNA--LVAVKFIERSNvkewariNGEQVPMEICMLAKcskvrgVIRLLDWYSI--------PE 105
Cdd:cd05116   2 ELGSGNFGTVKKGYYQMKKVvkTVAVKILKNEA-------NDPALKDELLREAN------VMQQLDNPYIvrmigiceAE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMER----PypcidMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVidLVTGS-TKLIDFGA 180
Cdd:cd05116  69 SWMLVMEMaelgP-----LNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVL--LVTQHyAKISDFGL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRSQ-YSDFQGTRLYcPPEWF----LHSLYLGREAAVWSLGVLLYNSLN-GRLPFRNEKDICTAHLLG-----PLP 249
Cdd:cd05116 142 SKALRADEnYYKAQTHGKW-PVKWYapecMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIEkgermECP 220
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 250 FFVPVsaEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd05116 221 AGCPP--EMYDLMKLCWTYDVDERPGFAAV 248
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
28-286 3.20e-08

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: 54.98  E-value: 3.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewaRINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGF 107
Cdd:cd05632   1 KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIK---KRKGESMALNEKQILEKVNSQFVVNLAYAYETKDAL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVM------ERPYPCIDMfdfikGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA 181
Cdd:cd05632  78 CLVLtimnggDLKFHIYNM-----GNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLD-DYGHIRISDLGLA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQYSDFQ-GTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAH------LLGPLPFFVPV 254
Cdd:cd05632 152 VKIPEGESIRGRvGTVGYMAPEVLNNQRY-TLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREevdrrvLETEEVYSAKF 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 25143934 255 SAEVKDLISKCLTFDPFQR--CSLEA---ILNHPWVK 286
Cdd:cd05632 231 SEEAKSICKMLLTKDPKQRlgCQEEGageVKRHPFFR 267
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
32-273 3.60e-08

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: 54.28  E-value: 3.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAELGRGGFGVVYRAVRTCDnalVAVKFIERSNVKEwaringEQVPM--EICMLAKCSKVRGVIRLLDWYSIPEGFLI 109
Cdd:cd14063   3 EIKEVIGKGRFGRVHRGRWHGD---VAIKLLNIDYLNE------EQLEAfkEEVAAYKNTRHDNLVLFMGACMDPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 110 VME--RPYPcidMFDFIKgQGKISEDMARFlfRQIAvtvHECVQ-------NRVLHRDLKDENIVIDLvtGSTKLIDFGA 180
Cdd:cd14063  74 VTSlcKGRT---LYSLIH-ERKEKFDFNKT--VQIA---QQICQgmgylhaKGIIHKDLKSKNIFLEN--GRVVITDFGL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLRRSQYSDFQGTrLYCPPEW-----------------FLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE--KDICT 241
Cdd:cd14063 143 FSLSGLLQPGRREDT-LVIPNGWlcylapeiiralspdldFEESLPFTKASDVYAFGTVWYELLAGRWPFKEQpaESIIW 221
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 242 AHLLGPLPFFVPVSA--EVKDLISKCLTFDPFQR 273
Cdd:cd14063 222 QVGCGKKQSLSQLDIgrEVKDILMQCWAYDPEKR 255
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
37-281 5.02e-08

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: 53.60  E-value: 5.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKEWARINGEQvPMEIcmlAKCSKVRGVIRLLDWYSIPEGFLIVMERpYP 116
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVKTC-RETLPPDLKRKFLQ-EARI---LKQYDHPNIVKLIGVCVQKQPIMIVMEL-VP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIDMFDFIKGQG---------KISEDMA---RFLfrqiavtvhecVQNRVLHRDLKDENIVIDLvTGSTKLIDFGAATVL 184
Cdd:cd05041  77 GGSLLTFLRKKGarltvkqllQMCLDAAagmEYL-----------ESKNCIHRDLAARNCLVGE-NNVLKISDFGMSREE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYSDFQGTRlYCPPEWFL-HSLYLGR---EAAVWSLGVLLYNSLN-GRLPFRNEKDICTAHLLG-----PLPFFVPv 254
Cdd:cd05041 145 EDGEYTVSDGLK-QIPIKWTApEALNYGRytsESDVWSFGILLWEIFSlGATPYPGMSNQQTREQIEsgyrmPAPELCP- 222
                       250       260
                ....*....|....*....|....*..
gi 25143934 255 sAEVKDLISKCLTFDPFQRCSLEAILN 281
Cdd:cd05041 223 -EAVYRLMLQCWAYDPENRPSFSEIYN 248
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
36-239 5.41e-08

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: 54.20  E-value: 5.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIErsnvkewarINGEQ-VPMEI---CMLAKCSKVRGVIRLLDWYSIPEGFLIVM 111
Cdd:cd07870   7 KLGEGSYATVYKGISRINGQLVALKVIS---------MKTEEgVPFTAireASLLKGLKHANIVLLHDIIHTKETLTFVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 ErpYPCIDMFDFIKGQ--GKISEDMARFLF---RQIAVTVHEcvqnRVLHRDLKDENIVIDLVtGSTKLIDFGAATV--L 184
Cdd:cd07870  78 E--YMHTDLAQYMIQHpgGLHPYNVRLFMFqllRGLAYIHGQ----HILHRDLKPQNLLISYL-GELKLADFGLARAksI 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 185 RRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDI 239
Cdd:cd07870 151 PSQTYSSEVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDV 205
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
27-249 5.83e-08

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 54.25  E-value: 5.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  27 FKKNYKLKAELGRGGFGvvyRAVRTCDN----ALVAVKFIErsNVKEWAringEQVPMEICMLAKCSKVRG-----VIRL 97
Cdd:cd14215  10 LQERYEIVSTLGEGTFG---RVVQCIDHrrggARVALKIIK--NVEKYK----EAARLEINVLEKINEKDPenknlCVQM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  98 LDWYSIPEGFLIVMErpYPCIDMFDFIKGQGKI--SEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI--------- 166
Cdd:cd14215  81 FDWFDYHGHMCISFE--LLGLSTFDFLKENNYLpyPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyelty 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 167 ---------DLVTGSTKLIDFGAATvLRRSQYSDFQGTRLYCPPEWFLHsLYLGREAAVWSLGVLLYNSLNGRLPFRN-- 235
Cdd:cd14215 159 nlekkrderSVKSTAIRVVDFGSAT-FDHEHHSTIVSTRHYRAPEVILE-LGWSQPCDVWSIGCIIFEYYVGFTLFQThd 236
                       250
                ....*....|....*.
gi 25143934 236 --EKDICTAHLLGPLP 249
Cdd:cd14215 237 nrEHLAMMERILGPIP 252
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
37-202 6.70e-08

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: 53.53  E-value: 6.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIE-RSNVKEWARINGEqvpmeICMLAKCSKvRGVIRlldWYS--IPEGFL-IVME 112
Cdd:cd14046  14 LGKGAFGQVVKVRNKLDGRYYAIKKIKlRSESKNNSRILRE-----VMLLSRLNH-QHVVR---YYQawIERANLyIQME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 rpY-PCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLR------ 185
Cdd:cd14046  85 --YcEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLD-SNGNVKIGDFGLATSNKlnvela 161
                       170       180       190
                ....*....|....*....|....*....|.
gi 25143934 186 ----RSQYSDFQ----------GTRLYCPPE 202
Cdd:cd14046 162 tqdiNKSTSAALgssgdltgnvGTALYVAPE 192
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
31-273 7.16e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 54.42  E-value: 7.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   31 YKLKAELGRGGFGVVYRAVRTCDNALVAVK-----------FIER-----SNVkewARIN----------GEQ--VPmei 82
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKvlrpdlardpeFVARfrreaQSA---ASLShpnivsvydvGEDggIP--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   83 cmlakcskvrgvirlldwYsipegflIVMErpY-PCIDMFDFIKGQGKISEDMA-RFLfRQI--AVTV-HecvQNRVLHR 157
Cdd:NF033483  83 ------------------Y-------IVME--YvDGRTLKDYIREHGPLSPEEAvEIM-IQIlsALEHaH---RNGIVHR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  158 DLKDENIVIDlVTGSTKLIDFG---AATVLRRSQYSDFQGTrlycppewfLHslYLGREAA----------VWSLGVLLY 224
Cdd:NF033483 132 DIKPQNILIT-KDGRVKVTDFGiarALSSTTMTQTNSVLGT---------VH--YLSPEQArggtvdarsdIYSLGIVLY 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143934  225 NSLNGRLPFRNEkdicTA------HLLGPLPffvPVSAEVKDL-------ISKCLTFDPFQR 273
Cdd:NF033483 200 EMLTGRPPFDGD----SPvsvaykHVQEDPP---PPSELNPGIpqsldavVLKATAKDPDDR 254
pknD PRK13184
serine/threonine-protein kinase PknD;
31-237 7.24e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 54.78  E-value: 7.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFI----------ERSNVKEwARINGEQV-PMEICMLAKCSKVRGVirlld 99
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIredlsenpllKKRFLRE-AKIAADLIhPGIVPVYSICSDGDPV----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  100 WYSIP--EGFLI--VMERPYPCidmfDFIKGQGKISEDMARFL--FRQIAVTVhECVQNR-VLHRDLKDENIVIDLVtGS 172
Cdd:PRK13184  78 YYTMPyiEGYTLksLLKSVWQK----ESLSKELAEKTSVGAFLsiFHKICATI-EYVHSKgVLHRDLKPDNILLGLF-GE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  173 TKLIDFGAAtvLRRSQYSDFQG-----------TRLYCP------PEWFLHSLYLGREAA----VWSLGVLLYNSLNGRL 231
Cdd:PRK13184 152 VVILDWGAA--IFKKLEEEDLLdidvdernicySSMTIPgkivgtPDYMAPERLLGVPASestdIYALGVILYQMLTLSF 229

                 ....*.
gi 25143934  232 PFRNEK 237
Cdd:PRK13184 230 PYRRKK 235
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
26-284 7.55e-08

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: 53.73  E-value: 7.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  26 KFKKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKfIERSnvkewARINGEQVPMEIcMLAKC--------SKVRGVIRL 97
Cdd:cd14136   7 VYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALK-VVKS-----AQHYTEAALDEI-KLLKCvreadpkdPGREHVVQL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  98 LDWYSI--PEGFLIVMERPYPCIDMFDFIKG---QGkISEDMARFLFRQIAVTVH----ECvqnRVLHRDLKDENIVIDL 168
Cdd:cd14136  80 LDDFKHtgPNGTHVCMVFEVLGPNLLKLIKRynyRG-IPLPLVKKIARQVLQGLDylhtKC---GIIHTDIKPENVLLCI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 169 VTGSTKLIDFGAATVLRRSQYSDFQgTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPF---------RNEKDI 239
Cdd:cd14136 156 SKIEVKIADLGNACWTDKHFTEDIQ-TRQYRSPEVILGAGY-GTPADIWSTACMAFELATGDYLFdphsgedysRDEDHL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 240 ctAH---LLGPLP------------FF-------------------VPV---------SAEVKDLISKCLTFDPFQRCSL 276
Cdd:cd14136 234 --ALiieLLGRIPrsiilsgkysreFFnrkgelrhisklkpwpledVLVekykwskeeAKEFASFLLPMLEYDPEKRATA 311

                ....*...
gi 25143934 277 EAILNHPW 284
Cdd:cd14136 312 AQCLQHPW 319
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
36-273 7.56e-08

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: 53.22  E-value: 7.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVV----YRAVRTcdnalVAVKFIERSNVKEWARINGEQVPMEIC------MLAKCSKVRGVirlldwysipe 105
Cdd:cd05059  11 ELGSGQFGVVhlgkWRGKID-----VAIKMIKEGSMSEDDFIEEAKVMMKLShpklvqLYGVCTKQRPI----------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 gfLIVME-RPYPCidMFDFIKGQ-GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATV 183
Cdd:cd05059  75 --FIVTEyMANGC--LLNYLRERrGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVG-EQNVVKVSDFGLARY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 184 LRRSQYSDFQGTRL---YCPPEWFLHSLYlGREAAVWSLGVLLYNSLN-GRLPFRNEKDICTA-HLLGPLPFFVPVSA-- 256
Cdd:cd05059 150 VLDDEYTSSVGTKFpvkWSPPEVFMYSKF-SSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVeHISQGYRLYRPHLApt 228
                       250
                ....*....|....*..
gi 25143934 257 EVKDLISKCLTFDPFQR 273
Cdd:cd05059 229 EVYTIMYSCWHEKPEER 245
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
28-277 8.20e-08

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: 53.53  E-value: 8.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTcDNALVAVKFIErsnvkewariNGEQVPMEICMLAKCSKVRGVIRLLDWYSIpegf 107
Cdd:cd05070   8 RESLQLIKRLGNGQFGEVWMGTWN-GNTKVAIKTLK----------PGTMSPESFLEEAQIMKKLKHDKLVQLYAV---- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 liVMERPYPCI-------DMFDFIK-GQGKISE-----DMARflfrQIAVTVHECVQNRVLHRDLKDENIVID--LVTgs 172
Cdd:cd05070  73 --VSEEPIYIVteymskgSLLDFLKdGEGRALKlpnlvDMAA----QVAAGMAYIERMNYIHRDLRSANILVGngLIC-- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 173 tKLIDFGAATVLRRSQYSDFQGTRL---YCPPEWFLHSLYLGReAAVWSLGVLLYNSLN-GRLPF--RNEKDICTAHLLG 246
Cdd:cd05070 145 -KIADFGLARLIEDNEYTARQGAKFpikWTAPEAALYGRFTIK-SDVWSFGILLTELVTkGRVPYpgMNNREVLEQVERG 222
                       250       260       270
                ....*....|....*....|....*....|....
gi 25143934 247 ---PLPFFVPVSaeVKDLISKCLTFDPFQRCSLE 277
Cdd:cd05070 223 yrmPCPQDCPIS--LHELMIHCWKKDPEERPTFE 254
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
28-233 8.64e-08

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: 53.16  E-value: 8.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNAL-----VAVKFIERSNVKEwariNGEQVPMEICMLAKCSKvRGVIRLLD--W 100
Cdd:cd05036   5 RKNLTLIRALGQGAFGEVYEGTVSGMPGDpsplqVAVKTLPELCSEQ----DEMDFLMEALIMSKFNH-PNIVRCIGvcF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 101 YSIPEgfLIVME--------------RPYP----CIDMFDFIkgqgkisedmarFLFRQIAVTVHECVQNRVLHRDLKDE 162
Cdd:cd05036  80 QRLPR--FILLElmaggdlksflrenRPRPeqpsSLTMLDLL------------QLAQDVAKGCRYLEENHFIHRDIAAR 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 163 NIvidLVTGST-----KLIDFGAATVLRRSQYSDFQGTRL----YCPPEWFLHSLYLGReAAVWSLGVLLYN--SLnGRL 231
Cdd:cd05036 146 NC---LLTCKGpgrvaKIGDFGMARDIYRADYYRKGGKAMlpvkWMPPEAFLDGIFTSK-TDVWSFGVLLWEifSL-GYM 220

                ..
gi 25143934 232 PF 233
Cdd:cd05036 221 PY 222
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
154-285 8.77e-08

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 53.73  E-value: 8.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 154 VLHRDLKDENIVI----DLvtgstKLIDFGAATVlRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNG 229
Cdd:cd07856 129 VIHRDLKPSNILVnencDL-----KICDFGLARI-QDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEG 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 230 R--LPFRNE-------------------KDICTAHLL---------GPLPF---FVPVSAEVKDLISKCLTFDPFQRCSL 276
Cdd:cd07856 203 KplFPGKDHvnqfsiitellgtppddviNTICSENTLrfvqslpkrERVPFsekFKNADPDAIDLLEKMLVFDPKKRISA 282

                ....*....
gi 25143934 277 EAILNHPWV 285
Cdd:cd07856 283 AEALAHPYL 291
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
154-286 9.18e-08

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: 53.50  E-value: 9.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 154 VLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRS--QYSDFQGTRLYCPPEwFLHSLYLGREAAVWSLGVLLYNSLNGRL 231
Cdd:cd06658 139 VIHRDIKSDSILLT-SDGRIKLSDFGFCAQVSKEvpKRKSLVGTPYWMAPE-VISRLPYGTEVDIWSLGIMVIEMIDGEP 216
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 232 PFRNEKDI-CTAHLLGPLPFFV----PVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd06658 217 PYFNEPPLqAMRRIRDNLPPRVkdshKVSSVLRGFLDLMLVREPSQRATAQELLQHPFLK 276
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
28-277 1.11e-07

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: 53.15  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTcDNALVAVKFIERSNVKEWARINGEQVpMEICMLAKCSKVRGVIRLLDWYSIPEgf 107
Cdd:cd05071   8 RESLRLEVKLGQGCFGEVWMGTWN-GTTRVAIKTLKPGTMSPEAFLQEAQV-MKKLRHEKLVQLYAVVSEEPIYIVTE-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 liVMERPypciDMFDFIKGQ-GKISE-----DMARflfrQIAVTVHECVQNRVLHRDLKDENIVI--DLVTgstKLIDFG 179
Cdd:cd05071  84 --YMSKG----SLLDFLKGEmGKYLRlpqlvDMAA----QIASGMAYVERMNYVHRDLRAANILVgeNLVC---KVADFG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVLRRSQYSDFQGTRL---YCPPEWFLHSLYLGReAAVWSLGVLLYN-SLNGRLPF-----RNEKDICTAHLLGPLPF 250
Cdd:cd05071 151 LARLIEDNEYTARQGAKFpikWTAPEAALYGRFTIK-SDVWSFGILLTElTTKGRVPYpgmvnREVLDQVERGYRMPCPP 229
                       250       260
                ....*....|....*....|....*..
gi 25143934 251 FVPVSaeVKDLISKCLTFDPFQRCSLE 277
Cdd:cd05071 230 ECPES--LHDLMCQCWRKEPEERPTFE 254
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
31-235 1.23e-07

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: 53.33  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIeRSNVKE---------WARINGEQVPMEICMLAKCSKVRGVI--RLLD 99
Cdd:cd13977   2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKI-RCNAPEnvelalrefWALSSIQRQHPNVIQLEECVLQRDGLaqRMSH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 100 WYSIPEGFL----------IVMERPYPCIDMF--DFIKGQgkiseDMARFLFR-------------QIAVTVHECVQNRV 154
Cdd:cd13977  81 GSSKSDLYLllvetslkgeRCFDPRSACYLWFvmEFCDGG-----DMNEYLLSrrpdrqtntsfmlQLSSALAFLHRNQI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 155 LHRDLKDENIVIDLVTGS--TKLIDFGAATVLR-------------RSQYSDFQGTRLYCPPE-WFLHslYLGReAAVWS 218
Cdd:cd13977 156 VHRDLKPDNILISHKRGEpiLKVADFGLSKVCSgsglnpeepanvnKHFLSSACGSDFYMAPEvWEGH--YTAK-ADIFA 232
                       250
                ....*....|....*..
gi 25143934 219 LGVLLYNSLNgRLPFRN 235
Cdd:cd13977 233 LGIIIWAMVE-RITFRD 248
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
29-284 1.33e-07

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: 53.14  E-value: 1.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQvpmEICMLAKCsKVRGVIRLLD-WYSIPEGF 107
Cdd:cd07865  12 SKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITALR---EIKILQLL-KHENVVNLIEiCRTKATPY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 livmERPYPCIDM-FDFIkgqgkiSEDMARFL---------------FRQIAVTVHECVQNRVLHRDLKDENIVIDLvTG 171
Cdd:cd07865  88 ----NRYKGSIYLvFEFC------EHDLAGLLsnknvkftlseikkvMKMLLNGLYYIHRNKILHRDMKAANILITK-DG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 172 STKLIDFGAATVL------RRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVL----------------------- 222
Cdd:cd07865 157 VLKLADFGLARAFslaknsQPNRYTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCImaemwtrspimqgnteqhqltli 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 223 -------------------LYNSLngRLPfRNEKDICTAHLlgpLPFFVPVSAevKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd07865 237 sqlcgsitpevwpgvdkleLFKKM--ELP-QGQKRKVKERL---KPYVKDPYA--LDLIDKLLVLDPAKRIDADTALNHD 308

                .
gi 25143934 284 W 284
Cdd:cd07865 309 F 309
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
31-284 2.40e-07

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: 52.29  E-value: 2.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVR--TCDNALVAVKFIERSNVKewarinGEQVPM----EICMLAKCSKvRGVIRLLdwysip 104
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKAKRknGKDGKEYAIKKFKGDKEQ------YTGISQsacrEIALLRELKH-ENVVSLV------ 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVMERpypCIDM-FDF--------IK-----GQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVT 170
Cdd:cd07842  69 EVFLEHADK---SVYLlFDYaehdlwqiIKfhrqaKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANI---LVM 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 171 ------GSTKLIDFGAATVLRRSQYSDFQG-----TRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFR-NEKD 238
Cdd:cd07842 143 gegperGVVKIGDLGLARLFNAPLKPLADLdpvvvTIWYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKgREAK 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 239 ICTA------------HLLGP-----------LPF------------FVPVS------------AEVKDLISKCLTFDPF 271
Cdd:cd07842 223 IKKSnpfqrdqlerifEVLGTptekdwpdikkMPEydtlksdtkastYPNSLlakwmhkhkkpdSQGFDLLRKLLEYDPT 302
                       330
                ....*....|...
gi 25143934 272 QRCSLEAILNHPW 284
Cdd:cd07842 303 KRITAEEALEHPY 315
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
151-232 2.74e-07

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: 52.36  E-value: 2.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 151 QNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSDFQGTRLYCPPEWfLHSLYLGREAAVWSLGVLLYNSLNGR 230
Cdd:cd06649 122 KHQIMHRDVKPSNILVN-SRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPER-LQGTHYSVQSDIWSMGLSLVELAIGR 199

                ..
gi 25143934 231 LP 232
Cdd:cd06649 200 YP 201
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
28-279 2.75e-07

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: 51.82  E-value: 2.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVV----YRAVRTCDNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVRGVIrlldwYSI 103
Cdd:cd05081   3 ERHLKYISQLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVS-----YGP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 104 PE-GFLIVMER-PYPCIDmfDFI-KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTgSTKLIDFGA 180
Cdd:cd05081  78 GRrSLRLVMEYlPSGCLR--DFLqRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEA-HVKIADFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 181 ATVLrrSQYSDF-------QGTRLYCPPEWFLHSLYlGREAAVWSLGVLLY--------------NSLNGRLPFRNEKDI 239
Cdd:cd05081 155 AKLL--PLDKDYyvvrepgQSPIFWYAPESLSDNIF-SRQSDVWSFGVVLYelftycdkscspsaEFLRMMGCERDVPAL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 25143934 240 CtaHLLG--------PLPFFVPvsAEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd05081 232 C--RLLElleegqrlPAPPACP--AEVHELMKLCWAPSPQDRPSFSAL 275
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
37-273 2.80e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 51.49  E-value: 2.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNalVAVKFIERSNV-----KEWARINGEQVPMEICMLAKCSKVRGVIRLLdwysIPEGFLivm 111
Cdd:cd14068   2 LGDGGFGSVYRAVYRGED--VAVKIFNKHTSfrllrQELVVLSHLHHPSLVALLAAGTAPRMLVMEL----APKGSL--- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 erpypcidmfDFIKGQGKISedMARFLFRQIAVTVHECVqnRVLH------RDLKDENIVI-DLVTGS---TKLIDFGAA 181
Cdd:cd14068  73 ----------DALLQQDNAS--LTRTLQHRIALHVADGL--RYLHsamiiyRDLKPHNVLLfTLYPNCaiiAKIADYGIA 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 182 TVLRRSQYSDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNG------RLPFRNEKDICTAHllGPLPffVPVS 255
Cdd:cd14068 139 QYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTCgeriveGLKFPNEFDELAIQ--GKLP--DPVK 214
                       250       260
                ....*....|....*....|....*
gi 25143934 256 -------AEVKDLISKCLTFDPFQR 273
Cdd:cd14068 215 eygcapwPGVEALIKDCLKENPQCR 239
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
31-286 2.86e-07

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: 52.09  E-value: 2.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIER--SNVKEWARINGEqvpMEICMLAKCSKVRGVIRLL---------D 99
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDvfEHVSDATRILRE---IKLLRLLRHPDIVEIKHIMlppsrrefkD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 100 WYSIPEgfliVMERpypciDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFG 179
Cdd:cd07859  79 IYVVFE----LMES-----DLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILAN-ADCKLKICDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 AATVLRRSQ-----YSDFQGTRLYCPPEwFLHSLYLGREAAV--WSLGVLLYNSLNGR--LPFRN---EKDICTaHLLG- 246
Cdd:cd07859 149 LARVAFNDTptaifWTDYVATRWYRAPE-LCGSFFSKYTPAIdiWSIGCIFAEVLTGKplFPGKNvvhQLDLIT-DLLGt 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 247 -------------------------PLPF---FVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:cd07859 227 pspetisrvrnekarrylssmrkkqPVPFsqkFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
36-273 2.89e-07

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 51.58  E-value: 2.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAV-RTCDNAL--VAVKFI----ERSNVKEWARingEQVPMeiCMLAKCSKVR--GVirlldwySIPEG 106
Cdd:cd05060   2 ELGHGNFGSVRKGVyLMKSGKEveVAVKTLkqehEKAGKKEFLR---EASVM--AQLDHPCIVRliGV-------CKGEP 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVMERPyPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVidLVT-GSTKLIDFGAATVLR 185
Cdd:cd05060  70 LMLVMELA-PLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVL--LVNrHQAKISDFGMSRALG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 --RSQYSDFQGTRLycPPEWFL-HSLYLGR---EAAVWSLGVLLYNSLN-GRLPFRNEKDICTAHLL---GPLPFFVPVS 255
Cdd:cd05060 147 agSDYYRATTAGRW--PLKWYApECINYGKfssKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLesgERLPRPEECP 224
                       250
                ....*....|....*...
gi 25143934 256 AEVKDLISKCLTFDPFQR 273
Cdd:cd05060 225 QEIYSIMLSCWKYRPEDR 242
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
152-283 2.99e-07

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: 51.59  E-value: 2.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 152 NRVLHRDLKDENIVIDLVTGST--KLIDFGAATVLRRSQYSD----FQGTRLYcPPEWFLHSLYLGREAAVWSLGVLLYN 225
Cdd:cd14012 123 NGVVHKSLHAGNVLLDRDAGTGivKLTDYSLGKTLLDMCSRGsldeFKQTYWL-PPELAQGSKSPTRKTDVWDLGLLFLQ 201
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 226 SLNGRLPFRNekdictAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd14012 202 MLFGLDVLEK------YTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
37-290 3.34e-07

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: 51.60  E-value: 3.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQvpmEICMLAKCsKVRGVIRLLDWY------SIpegFLiV 110
Cdd:cd07845  15 IGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGIPISSLR---EITLLLNL-RHPNIVELKEVVvgkhldSI---FL-V 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MErpYPCIDMFDFIKG-QGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVT--GSTKLIDFGAAtvlrrS 187
Cdd:cd07845  87 ME--YCEQDLASLLDNmPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNL---LLTdkGCLKIADFGLA-----R 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 188 QYSDFQG-------TRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGR--LPFRNEKD----ICtaHLLG-------- 246
Cdd:cd07845 157 TYGLPAKpmtpkvvTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKplLPGKSEIEqldlII--QLLGtpnesiwp 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143934 247 -----PL---------PF------FVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVKQQTL 290
Cdd:cd07845 235 gfsdlPLvgkftlpkqPYnnlkhkFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKEKPL 298
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
37-223 3.52e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 51.68  E-value: 3.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERPYP 116
Cdd:cd14211   7 LGRGTFGQVVKCWKRGTNEIVAIKILK--NHPSYARQGQIEVSILSRLSQENADEFNFVRAYECFQHKNHTCLVFEMLEQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 ciDMFDFIKgQGKISEDMARFL---FRQIAVTVHECVQNRVLHRDLKDENI-VIDLVTG--STKLIDFGAATVLRRSQYS 190
Cdd:cd14211  85 --NLYDFLK-QNKFSPLPLKYIrpiLQQVLTALLKLKSLGLIHADLKPENImLVDPVRQpyRVKVIDFGSASHVSKAVCS 161
                       170       180       190
                ....*....|....*....|....*....|...
gi 25143934 191 DFQGTRLYCPPEWFLhSLYLGREAAVWSLGVLL 223
Cdd:cd14211 162 TYLQSRYYRAPEIIL-GLPFCEAIDMWSLGCVI 193
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
141-280 3.69e-07

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: 50.09  E-value: 3.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    141 QIAVTVHECVQN-RVLHRDLKDENIVIdlvTGSTKLIDFGAatVLRRSQYSDFQgTRLYCPPEWFLHSLYlGREAAVWSL 219
Cdd:smart00750  18 EIWAVCLQCLGAlRELHRQAKSGNILL---TWDGLLKLDGS--VAFKTPEQSRP-DPYFMAPEVIQGQSY-TEKADIYSL 90
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143934    220 GVLLYNSLNGRLPFRNEKdictahllgplpffvPVSAEVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:smart00750  91 GITLYEALDYELPYNEER---------------ELSAILEILLNGMPADDPRDRSNLEGVS 136
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
120-279 5.67e-07

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: 50.69  E-value: 5.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 120 MFDFIK-GQGKISE-----DMARflfrQIAVTVHECVQNRVLHRDLKDENIVI--DLVTgstKLIDFGAATVLRRSQYSD 191
Cdd:cd14203  76 LLDFLKdGEGKYLKlpqlvDMAA----QIASGMAYIERMNYIHRDLRAANILVgdNLVC---KIADFGLARLIEDNEYTA 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 192 FQGTRLycPPEWFL--HSLYlGR---EAAVWSLGVLLYNSLN-GRLPF--RNEKDICTAHLLG---PLPFFVPVSaeVKD 260
Cdd:cd14203 149 RQGAKF--PIKWTApeAALY-GRftiKSDVWSFGILLTELVTkGRVPYpgMNNREVLEQVERGyrmPCPPGCPES--LHE 223
                       170
                ....*....|....*....
gi 25143934 261 LISKCLTFDPFQRCSLEAI 279
Cdd:cd14203 224 LMCQCWRKDPEERPTFEYL 242
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
37-283 6.45e-07

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


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 50.50  E-value: 6.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALV-AVKFIERSNVKEWARingEQVPMEICMLAKCSKV--RGVIRLLD-WYSipEGFLIVME 112
Cdd:cd14052   8 IGSGEFSQVYKVSERVPTGKVyAVKKLKPNYAGAKDR---LRRLEEVSILRELTLDghDNIVQLIDsWEY--HGHLYIQT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 RPYPCIDMFDFIKGQGKISEdMARFLFRQIAVTVHECVQ----NRVLHRDLKDENIVIDLvTGSTKLIDFGAATVLRRSQ 188
Cdd:cd14052  83 ELCENGSLDVFLSELGLLGR-LDEFRVWKILVELSLGLRfihdHHFVHLDLKPANVLITF-EGTLKIGDFGMATVWPLIR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYN-SLNGRLP--------FRNEkDICTAHLLG------------- 246
Cdd:cd14052 161 GIEREGDREYIAPEILSEHMY-DKPADIFSLGLILLEaAANVVLPdngdawqkLRSG-DLSDAPRLSstdlhsasspssn 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 25143934 247 --PLPFFVPVSAEVKD-LISKCLTFDPFQRCSLEAILNHP 283
Cdd:cd14052 239 ppPDPPNMPILSGSLDrVVRWMLSPEPDRRPTADDVLATP 278
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
36-279 7.78e-07

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: 50.31  E-value: 7.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWAringEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVMERPY 115
Cdd:cd05084   3 RIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLK----AKFLQEARILKQYSH-PNIVRLIGVCTQKQPIYIVMELVQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCiDMFDFIKGQG-KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVT--GSTKLIDFGAATVLRRSQYSDF 192
Cdd:cd05084  78 GG-DFLTFLRTEGpRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNC---LVTekNVLKISDFGMSREEEDGVYAAT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 193 QGTRlYCPPEWFL-HSLYLGR---EAAVWSLGVLLYNSLN-GRLPFRNEKDICTAHLLG-----PLPFFVPvsAEVKDLI 262
Cdd:cd05084 154 GGMK-QIPVKWTApEALNYGRyssESDVWSFGILLWETFSlGAVPYANLSNQQTREAVEqgvrlPCPENCP--DEVYRLM 230
                       250
                ....*....|....*..
gi 25143934 263 SKCLTFDPFQRCSLEAI 279
Cdd:cd05084 231 EQCWEYDPRKRPSFSTV 247
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
28-233 1.24e-06

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: 49.64  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTcDNALVAVKFIERSNVKEWARINgEQVPMEICMLAKCSKVRGVIRLLDWYSIPEgf 107
Cdd:cd05073  10 RESLKLEKKLGAGQFGEVWMATYN-KHTKVAVKTMKPGSMSVEAFLA-EANVMKTLQHDKLVKLHAVVTKEPIYIITE-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 liVMERPypciDMFDFIKGQGKISEDMARFL--FRQIAVTVHECVQNRVLHRDLKDENIVIDLVTgSTKLIDFGAATVLR 185
Cdd:cd05073  86 --FMAKG----SLLDFLKSDEGSKQPLPKLIdfSAQIAEGMAFIEQRNYIHRDLRAANILVSASL-VCKIADFGLARVIE 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 25143934 186 RSQYSDFQGTRL---YCPPEWFLHSLYLGReAAVWSLGVLLYNSLN-GRLPF 233
Cdd:cd05073 159 DNEYTAREGAKFpikWTAPEAINFGSFTIK-SDVWSFGILLMEIVTyGRIPY 209
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
9-185 1.37e-06

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 50.56  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    9 FFNLKLL--LNGESSRGFSKfkKNYKLKAELGRGGFGVVYRAVRTCDNA-----LVAVKFIERSNVKEWArinGEQVpME 81
Cdd:PLN03225 112 FVDMFVLapLEGLFRPSFKK--DDFVLGKKLGEGAFGVVYKASLVNKQSkkegkYVLKKATEYGAVEIWM---NERV-RR 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   82 ICMLAKCSKVRGVIRLLDWYSIPEGFLI-----------VM---ERPYPcIDMFDFIKGQG--KISEDMARF---LFRQI 142
Cdd:PLN03225 186 ACPNSCADFVYGFLEPVSSKKEDEYWLVwryegestladLMqskEFPYN-VEPYLLGKVQDlpKGLERENKIiqtIMRQI 264
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 25143934  143 AVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLR 185
Cdd:PLN03225 265 LFALDGLHSTGIVHRDVKPQNIIFSEGSGSFKIIDLGAAADLR 307
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
37-273 1.39e-06

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: 49.52  E-value: 1.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKewaRINGEQVPM-EICMLAKCSKVRgVIRLLDWYSIPEGFLIVMERpY 115
Cdd:cd05607  10 LGKGGFGEVCAVQVKNTGQMYACKKLDKKRLK---KKSGEKMALlEKEILEKVNSPF-IVSLAYAFETKTHLCLVMSL-M 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCIDMFDFIKGQGKISEDMARFLF--RQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQ-YSDF 192
Cdd:cd05607  85 NGGDLKYHIYNVGERGIEMERVIFysAQITCGILHLHSLKIVYRDMKPENVLLD-DNGNCRLSDLGLAVEVKEGKpITQR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 193 QGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEK------DICTAHLLGPLPFFVPV-SAEVKDLISKC 265
Cdd:cd05607 164 AGTNGYMAPEILKEESY-SYPVDWFAMGCSIYEMVAGRTPFRDHKekvskeELKRRTLEDEVKFEHQNfTEEAKDICRLF 242

                ....*...
gi 25143934 266 LTFDPFQR 273
Cdd:cd05607 243 LAKKPENR 250
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
36-280 1.65e-06

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: 49.11  E-value: 1.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVV-YRAVRTCDNalVAVKFIERSNVKEWARINGEQVPMEIC------MLAKCSKVRGVIRLLDWYSipEG-- 106
Cdd:cd05113  11 ELGTGQFGVVkYGKWRGQYD--VAIKMIKEGSMSEDEFIEEAKVMMNLSheklvqLYGVCTKQRPIFIITEYMA--NGcl 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 --FLIVMERPYPCIDMFDFIKgqgKISEDMARFLFRQIavtvhecvqnrvLHRDLKDENIVIDlVTGSTKLIDFGAATVL 184
Cdd:cd05113  87 lnYLREMRKRFQTQQLLEMCK---DVCEAMEYLESKQF------------LHRDLAARNCLVN-DQGVVKVSDFGLSRYV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 185 RRSQYSDFQGTRL---YCPPEWFLHSLYlGREAAVWSLGVLLYNSLN-GRLPF-RNEKDICTAHLLGPLPFFVP--VSAE 257
Cdd:cd05113 151 LDDEYTSSVGSKFpvrWSPPEVLMYSKF-SSKSDVWAFGVLMWEVYSlGKMPYeRFTNSETVEHVSQGLRLYRPhlASEK 229
                       250       260
                ....*....|....*....|...
gi 25143934 258 VKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd05113 230 VYTIMYSCWHEKADERPTFKILL 252
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
36-224 1.73e-06

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: 49.30  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  36 ELGRGGFGVVYR---------------AVRTC-DNALVAVKFIERSNVKEWARIngeQVPMEICMLAKCSKVRGVIRLLD 99
Cdd:cd05048  12 ELGEGAFGKVYKgellgpsseesaisvAIKTLkENASPKTQQDFRREAELMSDL---QHPNIVCLLGVCTKEQPQCMLFE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 100 WysIPEGFL---IVMERPYPCIDMFDFIKGqGKISEDMARFLF--RQIAVTVHECVQNRVLHRDLKDENIvidLVTGS-- 172
Cdd:cd05048  89 Y--MAHGDLhefLVRHSPHSDVGVSSDDDG-TASSLDQSDFLHiaIQIAAGMEYLSSHHYVHRDLAARNC---LVGDGlt 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 173 TKLIDFGAATVLRRSQYSDFQGTRL----YCPPEWFLHslylGR---EAAVWSLGVLLY 224
Cdd:cd05048 163 VKISDFGLSRDIYSSDYYRVQSKSLlpvrWMPPEAILY----GKfttESDVWSFGVVLW 217
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
28-277 1.93e-06

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: 49.11  E-value: 1.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTcDNALVAVK-----------FIERSN----------VKEWARINGEQVPMEICMLA 86
Cdd:cd05067   6 RETLKLVERLGAGQFGEVWMGYYN-GHTKVAIKslkqgsmspdaFLAEANlmkqlqhqrlVRLYAVVTQEPIYIITEYME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  87 KCSkvrgvirLLDWYSIPEGFLIVMerpYPCIDMfdfikgQGKISEDMArFLFRQiavtvhecvqnRVLHRDLKDENIVI 166
Cdd:cd05067  85 NGS-------LVDFLKTPSGIKLTI---NKLLDM------AAQIAEGMA-FIEER-----------NYIHRDLRAANILV 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 167 DlVTGSTKLIDFGAATVLRRSQYSDFQGTRL---YCPPEWFLHSLYLGReAAVWSLGVLLYNSLN-GRLPF---RNEKDI 239
Cdd:cd05067 137 S-DTLSCKIADFGLARLIEDNEYTAREGAKFpikWTAPEAINYGTFTIK-SDVWSFGILLTEIVThGRIPYpgmTNPEVI 214
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 25143934 240 CTAHLLGPLPFFVPVSAEVKDLISKCLTFDPFQRCSLE 277
Cdd:cd05067 215 QNLERGYRMPRPDNCPEELYQLMRLCWKERPEDRPTFE 252
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
80-283 2.71e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 49.10  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   80 MEICMLAKCSKvRGVIRLLDwySIPEGFLIVMERPYPCIDMFDFI-KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRD 158
Cdd:PHA03209 106 IEAMLLQNVNH-PSVIRMKD--TLVSGAITCMVLPHYSSDLYTYLtKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRD 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  159 LKDENIVIDLVTgSTKLIDFGAATV-LRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSL---------- 227
Cdd:PHA03209 183 VKTENIFINDVD-QVCIGDLGAAQFpVVAPAFLGLAGTVETNAPEVLARDKY-NSKADIWSAGIVLFEMLaypstifedp 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  228 --NGRLPFRNEK----DICTAHLLGPLPF-----------FVPVSAEVKD-------------------LISKCLTFDPF 271
Cdd:PHA03209 261 psTPEEYVKSCHshllKIISTLKVHPEEFprdpgsrlvrgFIEYASLERQpytrypcfqrvnlpidgefLVHKMLTFDAA 340
                        250
                 ....*....|..
gi 25143934  272 QRCSLEAILNHP 283
Cdd:PHA03209 341 MRPSAEEILNYP 352
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
28-279 2.96e-06

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: 48.53  E-value: 2.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTcDNALVAVKFIErsnvkewariNGEQVPMEICMLAKCSKVRGVIRLLDWYSIpegf 107
Cdd:cd05069  11 RESLRLDVKLGQGCFGEVWMGTWN-GTTKVAIKTLK----------PGTMMPEAFLQEAQIMKKLRHDKLVPLYAV---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 liVMERPYPCIDMF-------DFIK-GQGKISE-----DMARflfrQIAVTVHECVQNRVLHRDLKDENIVI--DLVTgs 172
Cdd:cd05069  76 --VSEEPIYIVTEFmgkgsllDFLKeGDGKYLKlpqlvDMAA----QIADGMAYIERMNYIHRDLRAANILVgdNLVC-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 173 tKLIDFGAATVLRRSQYSDFQGTRL---YCPPEWFLHSLYLGReAAVWSLGVLLYNSLN-GRLPF-----RNEKDICTAH 243
Cdd:cd05069 148 -KIADFGLARLIEDNEYTARQGAKFpikWTAPEAALYGRFTIK-SDVWSFGILLTELVTkGRVPYpgmvnREVLEQVERG 225
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 25143934 244 LLGPLPFFVPVSaeVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd05069 226 YRMPCPQGCPES--LHELMKLCWKKDPDERPTFEYI 259
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
37-287 3.36e-06

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: 48.95  E-value: 3.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIER--SNVKEWARINGEQVPMeicmlaKCSKVRGVIRLLDWYSiPEGFL------ 108
Cdd:cd07850   8 IGSGAQGIVCAAYDTVTGQNVAIKKLSRpfQNVTHAKRAYRELVLM------KLVNHKNIIGLLNVFT-PQKSLeefqdv 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 -IVMErpypCID--MFDFIkgQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAtvlr 185
Cdd:cd07850  81 yLVME----LMDanLCQVI--QMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVK-SDCTLKILDFGLA---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQG-----TRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI-----CTAHL----------L 245
Cdd:cd07850 150 RTAGTSFMMtpyvvTRYYRAPEVILGMGY-KENVDIWSVGCIMGEMIRGTVLFPGTDHIdqwnkIIEQLgtpsdefmsrL 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143934 246 GP--------------LPF--------FVPVS--------AEVKDLISKCLTFDPFQRCSLEAILNHPWVKQ 287
Cdd:cd07850 229 QPtvrnyvenrpkyagYSFeelfpdvlFPPDSeehnklkaSQARDLLSKMLVIDPEKRISVDDALQHPYINV 300
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
31-286 4.22e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 49.35  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934    31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARingEQVPMEICMLAKCsKVRGVIRLLDWY--SIPEGFL 108
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREK---SQLVIEVNVMREL-KHKNIVRYIDRFlnKANQKLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   109 IVME---------RPYPCIDMFdfikgqGKISEDMARFLFRQIAVTVHECVQ-------NRVLHRDLKDENIV------- 165
Cdd:PTZ00266   91 ILMEfcdagdlsrNIQKCYKMF------GKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFlstgirh 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   166 IDLVTGS---------TKLIDFG-AATVLRRSQYSDFQGTRLYCPPEWFLH-SLYLGREAAVWSLGVLLYNSLNGRLPFR 234
Cdd:PTZ00266  165 IGKITAQannlngrpiAKIGDFGlSKNIGIESMAHSCVGTPYYWSPELLLHeTKSYDDKSDMWALGCIIYELCSGKTPFH 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934   235 ---NEKDICTAHLLGP-LPfFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPWVK 286
Cdd:PTZ00266  245 kanNFSQLISELKRGPdLP-IKGKSKELNILIKNLLNLSAKERPSALQCLGYQIIK 299
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
37-279 4.95e-06

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: 47.66  E-value: 4.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAV--RTCDnalVAVKFIERSNVKEWARINGEQVpmeicMlaKCSKVRGVIRLLDWYSIPEGFLIVMErp 114
Cdd:cd05034   3 LGAGQFGEVWMGVwnGTTK---VAVKTLKPGTMSPEAFLQEAQI-----M--KKLRHDKLVQLYAVCSDEEPIYIVTE-- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 115 YPCI-DMFDFIK-GQGKISE-----DMARflfrQIAVTVHECVQNRVLHRDLKDENIVID--LVTgstKLIDFGAATVLR 185
Cdd:cd05034  71 LMSKgSLLDYLRtGEGRALRlpqliDMAA----QIASGMAYLESRNYIHRDLAARNILVGenNVC---KVADFGLARLIE 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSDFQGTRLycPPEWflhslyLGREAA----------VWSLGVLLYNSLN-GRLPF--RNEKDICTAHLLG---PLP 249
Cdd:cd05034 144 DDEYTAREGAKF--PIKW------TAPEAAlygrftiksdVWSFGILLYEIVTyGRVPYpgMTNREVLEQVERGyrmPKP 215
                       250       260       270
                ....*....|....*....|....*....|
gi 25143934 250 FFVPvsAEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd05034 216 PGCP--DELYDIMLQCWKKEPEERPTFEYL 243
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
32-275 5.75e-06

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: 47.51  E-value: 5.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  32 KLKAELGRGGFGVVYRAVRTCDNALVAVKFI--ERSNVKE---WARINGEQVpmeicmlakcSKVRGVIRLLDWysipeg 106
Cdd:cd13991   9 THQLRIGRGSFGEVHRMEDKQTGFQCAVKKVrlEVFRAEElmaCAGLTSPRV----------VPLYGAVREGPW------ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 FLIVME-RPYPCIDmfDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATVLR 185
Cdd:cd13991  73 VNIFMDlKEGGSLG--QLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAFLCDFGHAECLD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 186 RSQYSD-------FQGTRLYCPPEWFLHSlYLGREAAVWSLGVLLYNSLNGRLPFrnekdicTAHLLGPL---------- 248
Cdd:cd13991 151 PDGLGKslftgdyIPGTETHMAPEVVLGK-PCDAKVDVWSSCCMMLHMLNGCHPW-------TQYYSGPLclkianeppp 222
                       250       260       270
                ....*....|....*....|....*....|..
gi 25143934 249 -----PFFVPVSAEVkdlISKCLTFDPFQRCS 275
Cdd:cd13991 223 lreipPSCAPLTAQA---IQAGLRKEPVHRAS 251
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
28-279 7.28e-06

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: 47.48  E-value: 7.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAV-----RTCDNALVAVKFIersnvKEWARINGEQVPM-EICMLAKCSKVRGVIRLLDWY 101
Cdd:cd05055  34 RNNLSFGKTLGAGAFGKVVEATayglsKSDAVMKVAVKML-----KPTAHSSEREALMsELKIMSHLGNHENIVNLLGAC 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 102 SIPEGFLIVMErpYPCI-DMFDFIKGQGKI---SEDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVidLVTGS-TKLI 176
Cdd:cd05055 109 TIGGPILVITE--YCCYgDLLNFLRRKRESfltLEDLLSFSY-QVAKGMAFLASKNCIHRDLAARNVL--LTHGKiVKIC 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 177 DFG-AATVLRRSQYSDFQGTRL---YCPPEWFLHSLYLgREAAVWSLGVLLYN--SLNGR----LPFRNE--KDICTAHL 244
Cdd:cd05055 184 DFGlARDIMNDSNYVVKGNARLpvkWMAPESIFNCVYT-FESDVWSYGILLWEifSLGSNpypgMPVDSKfyKLIKEGYR 262
                       250       260       270
                ....*....|....*....|....*....|....*
gi 25143934 245 LGPlPFFVPvsAEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd05055 263 MAQ-PEHAP--AEIYDIMKTCWDADPLKRPTFKQI 294
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
18-285 8.04e-06

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: 47.73  E-value: 8.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  18 GESSrgFSKFKKNYKLKAeLGRGGFGVVYRAVRTCDNALVAVKFIER--SNVKEWARINGEQVpmeicmLAKCSKVRGVI 95
Cdd:cd07875  16 GDST--FTVLKRYQNLKP-IGSGAQGIVCAAYDAILERNVAIKKLSRpfQNQTHAKRAYRELV------LMKCVNHKNII 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  96 RLLDWYSiPEGFLIVMERPYPCIDMFDFIKGQ---GKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGS 172
Cdd:cd07875  87 GLLNVFT-PQKSLEEFQDVYIVMELMDANLCQviqMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVK-SDCT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 173 TKLIDFGAATVLRRS-QYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLYNSLNGRLPFRNEKDI-----CTAHLLG 246
Cdd:cd07875 165 LKILDFGLARTAGTSfMMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGEMIKGGVLFPGTDHIdqwnkVIEQLGT 243
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934 247 PLPFFV-------------------------------PVSAE--------VKDLISKCLTFDPFQRCSLEAILNHPWV 285
Cdd:cd07875 244 PCPEFMkklqptvrtyvenrpkyagysfeklfpdvlfPADSEhnklkasqARDLLSKMLVIDASKRISVDEALQHPYI 321
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
37-264 1.28e-05

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: 46.64  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNAL----VAVKFIErsnvKEWARINGEQVPMEICMLAKCSKvRGVIRLLDWYSIPEGFLIVME 112
Cdd:cd05057  15 LGSGAFGTVYKGVWIPEGEKvkipVAIKVLR----EETGPKANEEILDEAYVMASVDH-PHLVRLLGICLSSQVQLITQL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 RPYPCIDmfDFIK-GQGKI-SEDMARFLfRQIAVTVHECVQNRVLHRDLKDENIVI---DLVtgstKLIDFGAATVLRR- 186
Cdd:cd05057  90 MPLGCLL--DYVRnHRDNIgSQLLLNWC-VQIAKGMSYLEEKRLVHRDLAARNVLVktpNHV----KITDFGLAKLLDVd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 187 -SQYSdFQGTRLycPPEWF-LHSLYLGR---EAAVWSLGVLLYNSLN-GRLPFRNekdictahllgplpffVPvSAEVKD 260
Cdd:cd05057 163 eKEYH-AEGGKV--PIKWMaLESIQYRIythKSDVWSYGVTVWELMTfGAKPYEG----------------IP-AVEIPD 222

                ....
gi 25143934 261 LISK 264
Cdd:cd05057 223 LLEK 226
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
153-282 1.41e-05

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: 46.54  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 153 RVLHRDLKDENIVidLVTGSTKLIDFGAATVLRRSQY--SDFQGTRLYCPPEWFL---HSlylgREAAVWSLGVLLYNSL 227
Cdd:cd13995 116 NIIHHDIKPSNIV--FMSTKAVLVDFGLSVQMTEDVYvpKDLRGTEIYMSPEVILcrgHN----TKADIYSLGATIIHMQ 189
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143934 228 NGRLPFRNE-------KDICTAHLLGPLPFFVP--VSAEVKDLISKCLTFDPFQRCSLEAILNH 282
Cdd:cd13995 190 TGSPPWVRRyprsaypSYLYIIHKQAPPLEDIAqdCSPAMRELLEAALERNPNHRSSAAELLKH 253
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
28-202 1.86e-05

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 46.18  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINgeqvpMEICMLAKCsKVRGVIRLLDWYSIPEGF 107
Cdd:cd06646   8 QHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQ-----QEIFMVKEC-KHCNIVAYFGSYLSREKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 LIVMERpypC--IDMFDFIKGQGKISEdmarflfRQIAVTVHECVQNRV-------LHRDLKDENIVIDlVTGSTKLIDF 178
Cdd:cd06646  82 WICMEY---CggGSLQDIYHVTGPLSE-------LQIAYVCRETLQGLAylhskgkMHRDIKGANILLT-DNGDVKLADF 150
                       170       180
                ....*....|....*....|....*....
gi 25143934 179 G-----AATVLRRSQysdFQGTRLYCPPE 202
Cdd:cd06646 151 GvaakiTATIAKRKS---FIGTPYWMAPE 176
PTZ00284 PTZ00284
protein kinase; Provisional
31-249 2.01e-05

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 46.88  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934   31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsNVKEWARINGEQVP-MEICMLAKCSKVRGVIRLLDWYSIPEGFL- 108
Cdd:PTZ00284 131 FKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVR--NVPKYTRDAKIEIQfMEKVRQADPADRFPLMKIQRYFQNETGHMc 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  109 IVMERPYPCidMFDFIKGQGKISE-DMARFLFRQIAVTVHECVQNRVLHRDLKDENI-------VIDLVTGS-------- 172
Cdd:PTZ00284 209 IVMPKYGPC--LLDWIMKHGPFSHrHLAQIIFQTGVALDYFHTELHLMHTDLKPENIlmetsdtVVDPVTNRalppdpcr 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  173 TKLIDFGAATVLRRSQySDFQGTRLYCPPEWFLhSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKDICTAHL----LGPL 248
Cdd:PTZ00284 287 VRICDLGGCCDERHSR-TAIVSTRHYRSPEVVL-GLGWMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHLmektLGRL 364

                 .
gi 25143934  249 P 249
Cdd:PTZ00284 365 P 365
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
30-281 2.85e-05

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: 45.41  E-value: 2.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  30 NYKLKAELGRGGFGVVYRA----VRTCDNAL-VAVKFI-ERSNVKEwaRINgeqvpmeicMLAKCSKVRG-----VIRLL 98
Cdd:cd05032   7 KITLIRELGQGSFGMVYEGlakgVVKGEPETrVAIKTVnENASMRE--RIE---------FLNEASVMKEfnchhVVRLL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  99 DWYSIPEGFLIVME--------------RP-------YPCIDMFDFIKGQGKISEDMArflfrqiavTVHEcvqNRVLHR 157
Cdd:cd05032  76 GVVSTGQPTLVVMElmakgdlksylrsrRPeaennpgLGPPTLQKFIQMAAEIADGMA---------YLAA---KKFVHR 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 158 DLKDENIVI--DLvtgSTKLIDFGAATVLRRSQYSDFQGTRLYcPPEWF----LHSLYLGREAAVWSLGVLLYNSLN-GR 230
Cdd:cd05032 144 DLAARNCMVaeDL---TVKIGDFGMTRDIYETDYYRKGGKGLL-PVRWMapesLKDGVFTTKSDVWSFGVVLWEMATlAE 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 231 LPFR---NE---KDICTAHLLgPLPFFVPVsaEVKDLISKCLTFDPFQRCSLEAILN 281
Cdd:cd05032 220 QPYQglsNEevlKFVIDGGHL-DLPENCPD--KLLELMRMCWQYNPKMRPTFLEIVS 273
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
33-279 3.13e-05

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 45.53  E-value: 3.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  33 LKAELGRGGFGVVYRAvrTC-------DNALVAVKFIERSNVkEWARINGEQvpmEICMLAKCS-----KVRGVIRLLD- 99
Cdd:cd05049   9 LKRELGEGAFGKVFLG--ECynlepeqDKMLVAVKTLKDASS-PDARKDFER---EAELLTNLQhenivKFYGVCTEGDp 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 100 WYSIPEgfliVMERPypciDMFDFIKGQGK-----ISEDMARF---------LFRQIAVTVHECVQNRVLHRDLKDENIV 165
Cdd:cd05049  83 LLMVFE----YMEHG----DLNKFLRSHGPdaaflASEDSAPGeltlsqllhIAVQIASGMVYLASQHFVHRDLATRNCL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 166 I--DLVTgstKLIDFGAATVLRRSQYSDFQGTRL----YCPPEWFLHSLYLgREAAVWSLGVLLYNSLN-GRLPF---RN 235
Cdd:cd05049 155 VgtNLVV---KIGDFGMSRDIYSTDYYRVGGHTMlpirWMPPESILYRKFT-TESDVWSFGVVLWEIFTyGKQPWfqlSN 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 25143934 236 EKDI-C--TAHLLGPlPFFVPvsAEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd05049 231 TEVIeCitQGRLLQR-PRTCP--SEVYAVMLGCWKREPQQRLNIKDI 274
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
37-273 3.58e-05

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: 45.40  E-value: 3.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNA----LVAVKFIeRSNVKEWAriNGEQVPMEICMLAKCSKVrgVIRLLDWYSIPEGFLIVME 112
Cdd:cd05109  15 LGSGAFGTVYKGIWIPDGEnvkiPVAIKVL-RENTSPKA--NKEILDEAYVMAGVGSPY--VCRLLGICLTSTVQLVTQL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 113 RPYPCidMFDFIK-GQGKI-SEDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDLVTgSTKLIDFGAATVLRRSQyS 190
Cdd:cd05109  90 MPYGC--LLDYVReNKDRIgSQDLLNWCV-QIAKGMSYLEEVRLVHRDLAARNVLVKSPN-HVKITDFGLARLLDIDE-T 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 191 DFQGTRLYCPPEWFLHSLYLGR----EAAVWSLGVLLYNSLN-GRLPF-----RNEKDICTAHLLGPLPffvPV-SAEVK 259
Cdd:cd05109 165 EYHADGGKVPIKWMALESILHRrfthQSDVWSYGVTVWELMTfGAKPYdgipaREIPDLLEKGERLPQP---PIcTIDVY 241
                       250
                ....*....|....
gi 25143934 260 DLISKCLTFDPFQR 273
Cdd:cd05109 242 MIMVKCWMIDSECR 255
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
37-235 3.91e-05

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: 45.01  E-value: 3.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKFIERSNVKEWARINGEQVpmeicmlakCSKVRGVIRLLdwysipegFLIVMERPYP 116
Cdd:cd14150   8 IGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQV---------LRKTRHVNILL--------FMGFMTRPNF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 117 CIdMFDFIKGQG-----KISE---DMARFL--FRQIAVTVHECVQNRVLHRDLKDENIVidLVTGST-KLIDFGAATVLR 185
Cdd:cd14150  71 AI-ITQWCEGSSlyrhlHVTEtrfDTMQLIdvARQTAQGMDYLHAKNIIHRDLKSNNIF--LHEGLTvKIGDFGLATVKT 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 186 R----SQYSDFQGTRLYCPPEWFL---HSLYlGREAAVWSLGVLLYNSLNGRLPFRN 235
Cdd:cd14150 148 RwsgsQQVEQPSGSILWMAPEVIRmqdTNPY-SFQSDVYAYGVVLYELMSGTLPYSN 203
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
151-224 3.98e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 45.76  E-value: 3.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934  151 QNRVLHRDLKDENIVIDLvTGSTKLIDFGAATV---LRRSQYSDFQGTRLYCPPEWFLHSLYlGREAAVWSLGVLLY 224
Cdd:PHA03212 200 ENRIIHRDIKAENIFINH-PGDVCLGDFGAACFpvdINANKYYGWAGTIATNAPELLARDPY-GPAVDIWSAGIVLF 274
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
31-238 5.58e-05

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: 44.66  E-value: 5.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFiersnvkEWARINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd14129   2 WKVLRKIGGGGFGEIYDALDLLTRENVALKV-------ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTK---LIDFGAATVLRRS 187
Cdd:cd14129  75 MQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRkcyMLDFGLARQFTNS 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 188 --------QYSDFQGTRLYCPPEWFlHSLYLGREAAVWSLGVLLYNSLNGRLPFRNEKD 238
Cdd:cd14129 155 cgdvrpprAVAGFRGTVRYASINAH-RNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKD 212
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
140-235 6.28e-05

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: 44.67  E-value: 6.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 140 RQIAVTVHECVQNRVLHRDLKDENIVI--DLvtgSTKLIDFGAATVLRR----SQYSDFQGTRLYCPPE--WFLHSLYLG 211
Cdd:cd14151 111 RQTAQGMDYLHAKSIIHRDLKSNNIFLheDL---TVKIGDFGLATVKSRwsgsHQFEQLSGSILWMAPEviRMQDKNPYS 187
                        90       100
                ....*....|....*....|....
gi 25143934 212 REAAVWSLGVLLYNSLNGRLPFRN 235
Cdd:cd14151 188 FQSDVYAFGIVLYELMTGQLPYSN 211
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
31-301 8.60e-05

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: 44.21  E-value: 8.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFIERSNVkeWARINGEQVPME--ICMLAKCSKVRGVIRLLDWYSIPEGFL 108
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDI--IARDEVESLMCEkrIFETVNSARHPFLVNLFACFQTPEHVC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMErpYPCI-DMFDFIKgQGKISEDMARFLfrqiavtvHECV--------QNRVLHRDLKDENIVIDlVTGSTKLIDFG 179
Cdd:cd05589  79 FVME--YAAGgDLMMHIH-EDVFSEPRAVFY--------AACVvlglqflhEHKIVYRDLKLDNLLLD-TEGYVKIADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 180 aatvLRR------SQYSDFQGTRLYCPPEWFLHSLYLgREAAVWSLGVLLYNSLNGRLPF--RNEKDI--CTAHLLGPLP 249
Cdd:cd05589 147 ----LCKegmgfgDRTSTFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLIYEMLVGESPFpgDDEEEVfdSIVNDEVRYP 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 250 FFvpVSAEVKDLISKCLTFDPFQRC-----SLEAILNHPWVKqqTLSWDALTKNKVQ 301
Cdd:cd05589 222 RF--LSTEAISIMRRLLRKNPERRLgaserDAEDVKKQPFFR--NIDWEALLARKIK 274
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
37-235 1.30e-04

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: 43.54  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDnalVAVKFIersNVKEWARINGEQVPMEICMLAKCSKVRgVIRLLDWYSIP---------EG- 106
Cdd:cd14062   1 IGSGSFGTVYKGRWHGD---VAVKKL---NVTDPTPSQLQAFKNEVAVLRKTRHVN-ILLFMGYMTKPqlaivtqwcEGs 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 107 ----FLIVMERPYpciDMFDFIkgqgkiseDMARflfrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAAT 182
Cdd:cd14062  74 slykHLHVLETKF---EMLQLI--------DIAR----QTAQGMDYLHAKNIIHRDLKSNNIFLH-EDLTVKIGDFGLAT 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 183 VLRRS----QYSDFQGTRLYCPPE---------WFLHSlylgreaAVWSLGVLLYNSLNGRLPFRN 235
Cdd:cd14062 138 VKTRWsgsqQFEQPTGSILWMAPEvirmqdenpYSFQS-------DVYAFGIVLYELLTGQLPYSH 196
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
29-236 1.65e-04

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: 42.98  E-value: 1.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALVAVKFIErsnvkeWARINGEQVPMEICMLAKCSKVRgVIRLLDWYSIPEGFL 108
Cdd:cd14110   3 KTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIP------YKPEDKQLVLREYQVLRRLSHPR-IAQLHSAYLSPRHLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERpypCI--DMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIvidLVTGST--KLIDFGAATVL 184
Cdd:cd14110  76 LIEEL---CSgpELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENM---IITEKNllKIVDLGNAQPF 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 25143934 185 RRSQY--SDFQGTRLYCPPEWFLHSLYLGREAAVWSLGVLLYNSLNGRLPFRNE 236
Cdd:cd14110 150 NQGKVlmTDKKGDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSD 203
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
29-233 1.92e-04

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: 42.94  E-value: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNalVAVKFIeRSNVKEWARINgEQVPMEICMLAKCSKVRGVIrlldwysIPEGFL 108
Cdd:cd05083   6 QKLTLGEIIGEGEFGAVLQGEYMGQK--VAVKNI-KCDVTAQAFLE-ETAVMTKLQHKNLVRLLGVI-------LHNGLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 109 IVMERPYPCiDMFDFIKGQGKISEDMARFLfrQIAVTVHECVQ----NRVLHRDLKDENIVIDlVTGSTKLIDFGAATVL 184
Cdd:cd05083  75 IVMELMSKG-NLVNFLRSRGRALVPVIQLL--QFSLDVAEGMEylesKKLVHRDLAARNILVS-EDGVAKISDFGLAKVG 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 25143934 185 RRSQYSdfqgTRL---YCPPEWFLHSLYLGReAAVWSLGVLLYNSLN-GRLPF 233
Cdd:cd05083 151 SMGVDN----SRLpvkWTAPEALKNKKFSSK-SDVWSYGVLLWEVFSyGRAPY 198
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
37-280 1.96e-04

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: 43.11  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRA-VRTCDNALVAVkfIERsnVKEWARIN------GE--------QVPMEICMLAKCSKvRGVIRLLDWY 101
Cdd:cd05047   3 IGEGNFGQVLKArIKKDGLRMDAA--IKR--MKEYASKDdhrdfaGElevlcklgHHPNIINLLGACEH-RGYLYLAIEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 102 SiPEGFLIVMERPYPCIDMFD-FIKGQGKISEDMARFLFR---QIAVTVHECVQNRVLHRDLKDENIVI--DLVTgstKL 175
Cdd:cd05047  78 A-PHGNLLDFLRKSRVLETDPaFAIANSTASTLSSQQLLHfaaDVARGMDYLSQKQFIHRDLAARNILVgeNYVA---KI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 176 IDFGaatvLRRSQYSDFQGTRLYCPPEWFL-----HSLYLGReAAVWSLGVLLYNSLN-GRLPFRNekdICTAHLLGPLP 249
Cdd:cd05047 154 ADFG----LSRGQEVYVKKTMGRLPVRWMAieslnYSVYTTN-SDVWSYGVLLWEIVSlGGTPYCG---MTCAELYEKLP 225
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 25143934 250 ----FFVPVSA--EVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd05047 226 qgyrLEKPLNCddEVYDLMRQCWREKPYERPSFAQIL 262
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
149-279 2.01e-04

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: 42.87  E-value: 2.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 149 CVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSD-----FQGTRLYCPPEWFLHSLYL-GREAAVWSLGVL 222
Cdd:cd14025 110 CMKPPLLHLDLKPANILLD-AHYHVKISDFGLAKWNGLSHSHDlsrdgLRGTIAYLPPERFKEKNRCpDTKHDVYSFAIV 188
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 223 LYNSLNGRLPFRNEKDICTAHL---------LGPLPFFVPVSAE-VKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd14025 189 IWGILTQKKPFAGENNILHIMVkvvkghrpsLSPIPRQRPSECQqMICLMKRCWDQDPRKRPTFQDI 255
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
131-288 2.17e-04

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 43.35  E-value: 2.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 131 SEDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVidLVTGS-TKLIDFGAATVLRR-SQYSDFQGTRL---YCPPEWFL 205
Cdd:cd05104 213 TEDLLSFSY-QVAKGMEFLASKNCIHRDLAARNIL--LTHGRiTKICDFGLARDIRNdSNYVVKGNARLpvkWMAPESIF 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 206 HSLYLgREAAVWSLGVLLY------NSLNGRLPFRNE--KDICTAHLLGPlPFFVPvsAEVKDLISKCLTFDPFQRCSLE 277
Cdd:cd05104 290 ECVYT-FESDVWSYGILLWeifslgSSPYPGMPVDSKfyKMIKEGYRMDS-PEFAP--SEMYDIMRSCWDADPLKRPTFK 365
                       170
                ....*....|.
gi 25143934 278 AILNHpwVKQQ 288
Cdd:cd05104 366 QIVQL--IEQQ 374
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
136-279 3.83e-04

Pseudokinase domain of the unknown subfamily 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: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 42.15  E-value: 3.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 136 RFLF-RQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSDFQGTR-----LYCPPEWFLHSLY 209
Cdd:cd14045 105 RFSFaTDIARGMAYLHQHKIYHGRLKSSNCVID-DRWVCKIADYGLTTYRKEDGSENASGYQqrlmqVYLPPENHSNTDT 183
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 210 LGREAA-VWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFV--------PVSAEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd14045 184 EPTQATdVYSYAIILLEIATRNDPVPEDDYSLDEAWCPPLPELIsgktenscPCPADYVELIRRCRKNNPAQRPTFEQI 262
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
28-279 4.15e-04

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: 42.01  E-value: 4.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAVRTcDNALVAVKFIErsnvkewariNGEQVPMEICMLAKCSKVRGVIRLLDWYSI---P 104
Cdd:cd05068   7 RKSLKLLRKLGSGQFGEVWEGLWN-NTTPVAVKTLK----------PGTMDPEDFLREAQIMKKLRHPKLIQLYAVctlE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 105 EGFLIVMERpypcidM-----FDFIKGQG---KISE--DMARflfrQIAVTVHECVQNRVLHRDLKDENIVIDLvTGSTK 174
Cdd:cd05068  76 EPIYIITEL------MkhgslLEYLQGKGrslQLPQliDMAA----QVASGMAYLESQNYIHRDLAARNVLVGE-NNICK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 175 LIDFGAATVLRRSQ-YSDFQGTRLycPPEWflhslyLGREAA----------VWSLGVLLYNSLN-GRLPFRNEKDICTA 242
Cdd:cd05068 145 VADFGLARVIKVEDeYEAREGAKF--PIKW------TAPEAAnynrfsiksdVWSFGILLTEIVTyGRIPYPGMTNAEVL 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 25143934 243 HLLG-----PLPFFVPvsAEVKDLISKCLTFDPFQRCSLEAI 279
Cdd:cd05068 217 QQVErgyrmPCPPNCP--PQLYDIMLECWKADPMERPTFETL 256
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
151-281 4.19e-04

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 42.10  E-value: 4.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 151 QNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQYSDFQ---------------GTRLYCPPEwFLHSLYL--GRE 213
Cdd:cd14027 108 GKGVIHKDLKPENILVD-NDFHIKIADLGLASFKMWSKLTKEEhneqrevdgtakknaGTLYYMAPE-HLNDVNAkpTEK 185
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25143934 214 AAVWSLGVLLYNSLNGRLPF---RNEKDICTAHLLGPLPFFVPVS----AEVKDLISKCLTFDPFQRCSLEAILN 281
Cdd:cd14027 186 SDVYSFAIVLWAIFANKEPYenaINEDQIIMCIKSGNRPDVDDITeycpREIIDLMKLCWEANPEARPTFPGIEE 260
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
33-224 9.48e-04

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: 40.87  E-value: 9.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  33 LKAELGRGGFGVVYRAVRTCDNALVAVKFI--ERSNVKEWARingeqvpmEICMLaKCSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd05052  10 MKHKLGGGQYGEVYEGVWKKYNLTVAVKTLkeDTMEVEEFLK--------EAAVM-KEIKHPNLVQLLGVCTREPPFYII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERpYPCIDMFDFIKGQGKISEDMARFLF--RQIAVTVHECVQNRVLHRDLKDENIVI---DLVtgstKLIDFGAATVLR 185
Cdd:cd05052  81 TEF-MPYGNLLDYLRECNREELNAVVLLYmaTQIASAMEYLEKKNFIHRDLAARNCLVgenHLV----KVADFGLSRLMT 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 25143934 186 RSQYSDFQGTRL---YCPPEWFLHSLYlGREAAVWSLGVLLY 224
Cdd:cd05052 156 GDTYTAHAGAKFpikWTAPESLAYNKF-SIKSDVWAFGVLLW 196
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
37-253 1.00e-03

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: 40.92  E-value: 1.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNAL---VAVKFIER-SNVKEWARINGEQVPMeicmlaKCSKVRGVIRLLDWYSIPEGF-LIVM 111
Cdd:cd05058   3 IGKGHFGCVYHGTLIDSDGQkihCAVKSLNRiTDIEEVEQFLKEGIIM------KDFSHPNVLSLLGICLPSEGSpLVVL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 112 erPYPCI-DMFDFIKGQGK--ISEDMARFLFrQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA-TVLRRS 187
Cdd:cd05058  77 --PYMKHgDLRNFIRSETHnpTVKDLIGFGL-QVAKGMEYLASKKFVHRDLAARNCMLD-ESFTVKVADFGLArDIYDKE 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25143934 188 QYSDFQGTRLYCPPEWF-LHSLYLGR---EAAVWSLGVLLYNSLN-GRLPFR--NEKDICTAHLLG---PLPFFVP 253
Cdd:cd05058 153 YYSVHNHTGAKLPVKWMaLESLQTQKfttKSDVWSFGVLLWELMTrGAPPYPdvDSFDITVYLLQGrrlLQPEYCP 228
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
125-284 1.16e-03

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


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 40.61  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 125 KGQGKISEDMA-RFLFRQIAVTVHECVQN---------RVLH------RDLKDENIVIDlVTGSTKLIDFGAATVLRRSQ 188
Cdd:cd05576  89 KEIHQLFADLDeRLAAASRFYIPEECIQRwaaemvvalDALHregivcRDLNPNNILLN-DRGHIQLTYFSRWSEVEDSC 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 189 YSDfQGTRLYCPPEwfLHSLYLGREAA-VWSLGVLLYNSLNGRLPFRNEKDICTAHLLGPLPFFvpVSAEVKDLISKCLT 267
Cdd:cd05576 168 DSD-AIENMYCAPE--VGGISEETEACdWWSLGALLFELLTGKALVECHPAGINTHTTLNIPEW--VSEEARSLLQQLLQ 242
                       170       180
                ....*....|....*....|..
gi 25143934 268 FDPFQR-----CSLEAILNHPW 284
Cdd:cd05576 243 FNPTERlgagvAGVEDIKSHPF 264
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
31-237 1.51e-03

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 40.17  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFiersnvkEWARINGEQVPME---ICMLAKCSKVRGVirlldWYSIPEGF 107
Cdd:cd14127   2 YKVGKKIGEGSFGVIFEGTNLLNGQQVAIKF-------EPRKSDAPQLRDEyrtYKLLAGCPGIPNV-----YYFGQEGL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 108 --LIVMERPYPCI-DMFDFIKgqGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI----DLVTGSTKLIDFGA 180
Cdd:cd14127  70 hnILVIDLLGPSLeDLFDLCG--RKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIgrpgTKNANVIHVVDFGM 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25143934 181 AtvlrrSQYSDFQgTRLYCP----------PEWFLHSLYLGREAA----VWSLGVLLYNSLNGRLPFRNEK 237
Cdd:cd14127 148 A-----KQYRDPK-TKQHIPyrekkslsgtARYMSINTHLGREQSrrddLEALGHVFMYFLRGSLPWQGLK 212
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
28-281 1.63e-03

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 40.41  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  28 KKNYKLKAELGRGGFGVVYRAvrTC-------DNALVAVKFIERSNVKEWARINGEQVPMEICMLAKCSKVRGVirlldw 100
Cdd:cd05093   4 RHNIVLKRELGEGAFGKVFLA--ECynlcpeqDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGV------ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 101 ySIPEGFLIVMERPYPCIDMFDFIKGQG-------------KISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVI- 166
Cdd:cd05093  76 -CVEGDPLIMVFEYMKHGDLNKFLRAHGpdavlmaegnrpaELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVg 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 167 -DLVTgstKLIDFGAATVLRRSQYSDFQGTRL----YCPPEWFLHSLYLgREAAVWSLGVLLYNSLN-GRLPF----RNE 236
Cdd:cd05093 155 eNLLV---KIGDFGMSRDVYSTDYYRVGGHTMlpirWMPPESIMYRKFT-TESDVWSLGVVLWEIFTyGKQPWyqlsNNE 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 25143934 237 KDIC-TAHLLGPLPFFVPvsAEVKDLISKCLTFDPFQRCSLEAILN 281
Cdd:cd05093 231 VIECiTQGRVLQRPRTCP--KEVYDLMLGCWQREPHMRLNIKEIHS 274
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
140-280 1.69e-03

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 40.28  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 140 RQIAVTVHECVQNRVLHRDLKDENIVI---DLVTGST---KLIDFGAA-TVLRRSQYSDfqgtRL-YCPPEWFLHSLYLG 211
Cdd:cd05076 123 RQLASALSYLENKNLVHGNVCAKNILLarlGLEEGTSpfiKLSDPGVGlGVLSREERVE----RIpWIAPECVPGGNSLS 198
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25143934 212 REAAVWSLG-VLLYNSLNGRLPFRN----EKDICTAHLLGpLPffVPVSAEVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd05076 199 TAADKWGFGaTLLEICFNGEAPLQSrtpsEKERFYQRQHR-LP--EPSCPELATLISQCLTYEPTQRPSFRTIL 269
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
149-280 1.88e-03

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 39.92  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 149 CVQNRVLHRDlkdeniVIDLVTGS-TKLIDFGAA-TVLRRSQYSDfqgtRL-YCPPEWFLHSLYLGREAAVWSLGVLLYN 225
Cdd:cd05077 136 CTKNILLARE------GIDGECGPfIKLSDPGIPiTVLSRQECVE----RIpWIAPECVEDSKNLSIAADKWSFGTTLWE 205
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143934 226 -SLNGRLPFRNEKDICTAHLL-GPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAIL 280
Cdd:cd05077 206 iCYNGEIPLKDKTLAEKERFYeGQCMLVTPSCKELADLMTHCMNYDPNQRPFFRAIM 262
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
114-181 2.01e-03

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 40.44  E-value: 2.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25143934  114 PYP-CIDmfDFIKGQGKISEDMA---------RFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAA 181
Cdd:PLN03224 282 PFPgCLE--EFMMAGKKIPDNMPqdkrdinviKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVT-VDGQVKIIDFGAA 356
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
29-273 2.29e-03

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: 39.98  E-value: 2.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  29 KNYKLKAELGRGGFGVVYRAVRTCDNALV--AVKFIersnvKEWARINGEQ-VPMEICMLAKCSKVRGVIRLLDWYSiPE 105
Cdd:cd05089   2 EDIKFEDVIGEGNFGQVIKAMIKKDGLKMnaAIKML-----KEFASENDHRdFAGELEVLCKLGHHPNIINLLGACE-NR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 106 GFLIVMERPYPCIDMFDFI-------------KGQGKISEDMARFLFR---QIAVTVHECVQNRVLHRDLKDENIVI--D 167
Cdd:cd05089  76 GYLYIAIEYAPYGNLLDFLrksrvletdpafaKEHGTASTLTSQQLLQfasDVAKGMQYLSEKQFIHRDLAARNVLVgeN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 168 LVTgstKLIDFGaatvLRRSQYSDFQGTRLYCPPEWFL-----HSLYLGReAAVWSLGVLLYNSLN-GRLPFRNekdICT 241
Cdd:cd05089 156 LVS---KIADFG----LSRGEEVYVKKTMGRLPVRWMAieslnYSVYTTK-SDVWSFGVLLWEIVSlGGTPYCG---MTC 224
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 25143934 242 AHLLGPLPFFVPVSA------EVKDLISKCLTFDPFQR 273
Cdd:cd05089 225 AELYEKLPQGYRMEKprncddEVYELMRQCWRDRPYER 262
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
31-238 2.40e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; 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. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 39.62  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  31 YKLKAELGRGGFGVVYRAVRTCDNALVAVKFiersnvkEWARINGEQVPMEICMLAKCSKVRGVIRLLDWYSIPEGFLIV 110
Cdd:cd14130   2 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-------ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 111 MERPYPCIDMFDFIKGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTK---LIDFGAA------ 181
Cdd:cd14130  75 MQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRkcyMLDFGLArqytnt 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25143934 182 --TVLRRSQYSDFQGTRLYCPPEWFLHSlYLGREAAVWSLGVLLYNSLNGRLPFRNEKD 238
Cdd:cd14130 155 tgEVRPPRNVAGFRGTVRYASVNAHKNR-EMGRHDDLWSLFYMLVEFAVGQLPWRKIKD 212
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
37-273 2.80e-03

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: 39.66  E-value: 2.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934  37 LGRGGFGVVYRAVRTCDNALVAVKF-IERSNVKEWARINGEQvpMEICMLAKCSKVRGVIRLLDWYSIPEGFLIVMERPY 115
Cdd:cd05110  15 LGSGAFGTVYKGIWVPEGETVKIPVaIKILNETTGPKANVEF--MDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPH 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 116 PCidMFDFI-KGQGKISEDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDlVTGSTKLIDFGAATVLRRSQySDFQG 194
Cdd:cd05110  93 GC--LLDYVhEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVK-SPNHVKITDFGLARLLEGDE-KEYNA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 195 TRLYCPPEWF----LHSLYLGREAAVWSLGVLLYN--SLNGR----LPFRNEKDICTAHLLGPLPffvPV-SAEVKDLIS 263
Cdd:cd05110 169 DGGKMPIKWMalecIHYRKFTHQSDVWSYGVTIWElmTFGGKpydgIPTREIPDLLEKGERLPQP---PIcTIDVYMVMV 245
                       250
                ....*....|
gi 25143934 264 KCLTFDPFQR 273
Cdd:cd05110 246 KCWMIDADSR 255
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
132-183 3.06e-03

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 39.02  E-value: 3.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 25143934   132 EDMARFLFRQIAVTVHECVQNRVLHRDLKDENIVIDLVTGSTKLIDFGAATV 183
Cdd:pfam01636 147 EELEERLLAALLALLPAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGL 198
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
153-284 5.12e-03

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: 38.84  E-value: 5.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 153 RVLHRDLKDENIVIDlVTGSTKLIDFG------AATVLRRSQYSDFQGTRL-------YCPPEWFLHSLYlGREAAVWSL 219
Cdd:cd14011 135 KLVHGNICPESVVIN-SNGEWKLAGFDfcisseQATDQFPYFREYDPNLPPlaqpnlnYLAPEYILSKTC-DPASDMFSL 212
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143934 220 GVLLYNSLN-GRLPFRNEKDICTA------HLLGPLPFFVPVSAEVKDLISKCLTFDPFQRCSLEAILNHPW 284
Cdd:cd14011 213 GVLIYAIYNkGKPLFDCVNNLLSYkknsnqLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPF 284
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
140-238 5.18e-03

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: 38.47  E-value: 5.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143934 140 RQIAVTVHECVQNRVLHRDLKDENIVidLVTGST-KLIDFGAATVLRR----SQYSDFQGTRLYCPPE--WFLHSLYLGR 212
Cdd:cd14149 115 RQTAQGMDYLHAKNIIHRDMKSNNIF--LHEGLTvKIGDFGLATVKSRwsgsQQVEQPTGSILWMAPEviRMQDNNPFSF 192
                        90       100
                ....*....|....*....|....*.
gi 25143934 213 EAAVWSLGVLLYNSLNGRLPFRNEKD 238
Cdd:cd14149 193 QSDVYSYGIVLYELMTGELPYSHINN 218
 
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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