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Conserved domains on  [gi|15218425|ref|NP_177374|]
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Leucine-rich receptor-like protein kinase family protein [Arabidopsis thaliana]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1000136)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00113 super family cl33413
leucine-rich repeat receptor-like protein kinase; Provisional
33-1076 1.87e-105

leucine-rich repeat receptor-like protein kinase; Provisional


The actual alignment was detected with superfamily member PLN00113:

Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 353.38  E-value: 1.87e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    33 VLSISVFFLTVSEAVCNLQDRDSLLWFSGNVSSPVSPL-HWNSSIDCCSWEGISCDKSpeNRVTSIILSSRGLSGNLPSS 111
Cdd:PLN00113   11 YLIFMLFFLFLNFSMLHAEELELLLSFKSSINDPLKYLsNWNSSADVCLWQGITCNNS--SRVVSIDLSGKNISGKISSA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   112 VLDLQRLSRLDLSHNRLSGPLPPGFLSALDQLLVLDLSYNSFKGELPlqqsfgNGSngIFPIQTVDLSSNLLEGEILSSS 191
Cdd:PLN00113   89 IFRLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFTGSIP------RGS--IPNLETLDLSNNMLSGEIPNDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   192 VFLqgaFNLTSFNVSNNSFTGSIP---------SFMCTASPQLTK--------------LDFSYNDFSGDLSQELSRCSR 248
Cdd:PLN00113  161 GSF---SSLKVLDLGGNVLVGKIPnsltnltslEFLTLASNQLVGqiprelgqmkslkwIYLGYNNLSGEIPYEIGGLTS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   249 LSVLRAGFNNLSGEIPKEIYNLPELEQLFLPVNRLSGKIDNGITRLTKLTLLELYSNHIEGEIPKDIGKLSKLSSLQLHV 328
Cdd:PLN00113  238 LNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   329 NNLMGSIPVSLANCTKLVKLNLRVNQLGGTLSAiDFSRFQSLSILDLGNNSFTGEFPSTVYSCKMMTAMRFAGNKLTGQI 408
Cdd:PLN00113  318 NNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPK-NLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   409 SPQVLELESLSFFTFSDNkmtNLTGALSilQGCKKLStLIMAKNFYDETVPSNKDFLRSDgFPSLQIFGIGACRLTGEIP 488
Cdd:PLN00113  397 PKSLGACRSLRRVRLQDN---SFSGELP--SEFTKLP-LVYFLDISNNNLQGRINSRKWD-MPSLQMLSLARNKFFGGLP 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   489 AwLIKLQRVEVMDLSMNRFVGTIPGWLGTLPDLFYLDLSDNFLTGELPKELFQLRALMSqkaydaternylelpvfvnpn 568
Cdd:PLN00113  470 D-SFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVS--------------------- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   569 nvttnqqynqlsslpptiyikrnnltgtipvevgqlkvlhiLELLGNNFSGSIPDELSNLTNLERLDLSNNNLSGRIPWS 648
Cdd:PLN00113  528 -----------------------------------------LDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKN 566
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   649 LTGLHFLSYFNVANNTLSGPIPTGTQFDTFPKANFEGNPLLCGGVLLTSCDPTQhsttkmgkgKVNRTLVLGLVLGLFFG 728
Cdd:PLN00113  567 LGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPCK---------RVRKTPSWWFYITCTLG 637
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   729 VSLILVLLALLVLSKRRVNPGDSENAEleiNSNGSYSevppgsdkdislvLLFGNSRYeVKDLTIFELLKATdnfSQANI 808
Cdd:PLN00113  638 AFLVLALVAFGFVFIRGRNNLELKRVE---NEDGTWE-------------LQFFDSKV-SKSITINDILSSL---KEENV 697
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   809 IGCGGFGLVYKA-TLDNGTKLAVKKlTGDYGMMEKEFKAEvevLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:PLN00113  698 ISRGKKGASYKGkSIKNGMQFVVKE-INDVNSIPSSEIAD---MGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEV 773
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   888 LHenpegpaQLDWPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVadfglsRLILPYRTHVTTELVG 967
Cdd:PLN00113  774 LR-------NLSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHL------RLSLPGLLCTDTKCFI 840
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   968 TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVfRPKMSRELVAWVHTMKRDGKPEEVFDTLLRE--SGNEEA 1045
Cdd:PLN00113  841 SSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADA-EFGVHGSIVEWARYCYSDCHLDMWIDPSIRGdvSVNQNE 919
                        1050      1060      1070
                  ....*....|....*....|....*....|.
gi 15218425  1046 MLRVLDIACMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:PLN00113  920 IVEVMNLALHCTATDPTARPCANDVLKTLES 950
 
Name Accession Description Interval E-value
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
33-1076 1.87e-105

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 353.38  E-value: 1.87e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    33 VLSISVFFLTVSEAVCNLQDRDSLLWFSGNVSSPVSPL-HWNSSIDCCSWEGISCDKSpeNRVTSIILSSRGLSGNLPSS 111
Cdd:PLN00113   11 YLIFMLFFLFLNFSMLHAEELELLLSFKSSINDPLKYLsNWNSSADVCLWQGITCNNS--SRVVSIDLSGKNISGKISSA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   112 VLDLQRLSRLDLSHNRLSGPLPPGFLSALDQLLVLDLSYNSFKGELPlqqsfgNGSngIFPIQTVDLSSNLLEGEILSSS 191
Cdd:PLN00113   89 IFRLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFTGSIP------RGS--IPNLETLDLSNNMLSGEIPNDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   192 VFLqgaFNLTSFNVSNNSFTGSIP---------SFMCTASPQLTK--------------LDFSYNDFSGDLSQELSRCSR 248
Cdd:PLN00113  161 GSF---SSLKVLDLGGNVLVGKIPnsltnltslEFLTLASNQLVGqiprelgqmkslkwIYLGYNNLSGEIPYEIGGLTS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   249 LSVLRAGFNNLSGEIPKEIYNLPELEQLFLPVNRLSGKIDNGITRLTKLTLLELYSNHIEGEIPKDIGKLSKLSSLQLHV 328
Cdd:PLN00113  238 LNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   329 NNLMGSIPVSLANCTKLVKLNLRVNQLGGTLSAiDFSRFQSLSILDLGNNSFTGEFPSTVYSCKMMTAMRFAGNKLTGQI 408
Cdd:PLN00113  318 NNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPK-NLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   409 SPQVLELESLSFFTFSDNkmtNLTGALSilQGCKKLStLIMAKNFYDETVPSNKDFLRSDgFPSLQIFGIGACRLTGEIP 488
Cdd:PLN00113  397 PKSLGACRSLRRVRLQDN---SFSGELP--SEFTKLP-LVYFLDISNNNLQGRINSRKWD-MPSLQMLSLARNKFFGGLP 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   489 AwLIKLQRVEVMDLSMNRFVGTIPGWLGTLPDLFYLDLSDNFLTGELPKELFQLRALMSqkaydaternylelpvfvnpn 568
Cdd:PLN00113  470 D-SFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVS--------------------- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   569 nvttnqqynqlsslpptiyikrnnltgtipvevgqlkvlhiLELLGNNFSGSIPDELSNLTNLERLDLSNNNLSGRIPWS 648
Cdd:PLN00113  528 -----------------------------------------LDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKN 566
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   649 LTGLHFLSYFNVANNTLSGPIPTGTQFDTFPKANFEGNPLLCGGVLLTSCDPTQhsttkmgkgKVNRTLVLGLVLGLFFG 728
Cdd:PLN00113  567 LGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPCK---------RVRKTPSWWFYITCTLG 637
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   729 VSLILVLLALLVLSKRRVNPGDSENAEleiNSNGSYSevppgsdkdislvLLFGNSRYeVKDLTIFELLKATdnfSQANI 808
Cdd:PLN00113  638 AFLVLALVAFGFVFIRGRNNLELKRVE---NEDGTWE-------------LQFFDSKV-SKSITINDILSSL---KEENV 697
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   809 IGCGGFGLVYKA-TLDNGTKLAVKKlTGDYGMMEKEFKAEvevLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:PLN00113  698 ISRGKKGASYKGkSIKNGMQFVVKE-INDVNSIPSSEIAD---MGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEV 773
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   888 LHenpegpaQLDWPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVadfglsRLILPYRTHVTTELVG 967
Cdd:PLN00113  774 LR-------NLSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHL------RLSLPGLLCTDTKCFI 840
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   968 TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVfRPKMSRELVAWVHTMKRDGKPEEVFDTLLRE--SGNEEA 1045
Cdd:PLN00113  841 SSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADA-EFGVHGSIVEWARYCYSDCHLDMWIDPSIRGdvSVNQNE 919
                        1050      1060      1070
                  ....*....|....*....|....*....|.
gi 15218425  1046 MLRVLDIACMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:PLN00113  920 IVEVMNLALHCTATDPTARPCANDVLKTLES 950
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
809-1077 3.16e-91

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: 293.25  E-value: 3.16e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGD-YGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14664    1 IGRGGAGTVYKGVMPNGTLVAVKRLKGEgTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEGPAQLDWPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVG 967
Cdd:cd14664   81 LHSRPESQPPLDWETRQRIALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMSSVAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  968 TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAWVHTMKRDGKPEEVFDTLLRESGNEEAML 1047
Cdd:cd14664  161 SYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDGVDIVDWVRGLLEEKKVEALVDPDLQGVYKLEEVE 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 15218425 1048 RVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14664  241 QVFQVALLCTQSSPMERPTMREVVRMLEGD 270
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
807-1070 1.60e-44

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 161.93  E-value: 1.60e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     807 NIIGCGGFGLVYKAT-LDNGTKLAVKKL-TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:smart00220    5 EKLGEGSFGKVYLARdKKTGKLVAIKVIkKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDL 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     885 DYWLHEN---PEGPAQldwpkrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPyrTHV 961
Cdd:smart00220   85 FDLLKKRgrlSEDEAR-------FYLRQILSALEYLHSK---GIVHRDLKPENILLDEDGHVKLADFGLARQLDP--GEK 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     962 TTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRPmevFRPKMSRELvawvhTMKRDGKPEEVFDT 1035
Cdd:smart00220  153 LTTFVGTPEYMAPEvllgkgYGKAV------DIWSLGVILYELLTGKPP---FPGDDQLLE-----LFKKIGKPKPPFPP 218
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 15218425    1036 LLRESGNEeamlrVLDIACMCVNQNPMKRPNIQQV 1070
Cdd:smart00220  219 PEWDISPE-----AKDLIRKLLVKDPEKRLTAEEA 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
809-1023 3.05e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.80  E-value: 3.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKE---FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:COG0515   15 LGRGGMGVVYLARdLRLGRPVALKVLRPELAADPEArerFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHEnpEGPaqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTE 964
Cdd:COG0515   95 ADLLRR--RGP--LPPAEALRILAQLAEALAAAHAA---GIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTGT 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  965 LVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME--------------------VFRPKMSRELVAWVHTM 1023
Cdd:COG0515  168 VVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDgdspaellrahlrepppppsELRPDLPPALDAIVLRA 246
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
809-1071 3.93e-42

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: 154.96  E-value: 3.93e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    809 IGCGGFGLVYKATL-----DNGTKLAVKKLTGDYGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:pfam07714    7 LGEGAFGEVYKGTLkgegeNTKIKVAVKTLKEGADEEEREdFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    883 SLDYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP-YRTHV 961
Cdd:pfam07714   87 DLLDFLRKHKR---KLTLKDLLSMALQIAKGMEYLESK---NFVHRDLAARNCLVSENLVVKISDFGLSRDIYDdDYYRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    962 TTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKR----DGKPEEVFDTL 1036
Cdd:pfam07714  161 RGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQP---YPGMSNEEVLEFLEDGYRlpqpENCPDELYDLM 237
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 15218425   1037 LResgneeamlrvldiacmCVNQNPMKRPNIQQVV 1071
Cdd:pfam07714  238 KQ-----------------CWAYDPEDRPTFSELV 255
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
783-1004 1.88e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 90.24  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   783 NSRYEVKDLtifellkatdnfsqaniIGCGGFGLVYKAtLDN--GTKLAVKKLTGDY----GMMEKeFKAEVEVLSRAKH 856
Cdd:NF033483    6 GGRYEIGER-----------------IGRGGMAEVYLA-KDTrlDRDVAVKVLRPDLardpEFVAR-FRREAQSAASLSH 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   857 ENLVAlqgycvhdsarilIYSFMENGSLDY-------------WLHENpeGPaqLDWPKRLNIMRGASSGLAYMHQiceP 923
Cdd:NF033483   67 PNIVS-------------VYDVGEDGGIPYivmeyvdgrtlkdYIREH--GP--LSPEEAVEIMIQILSALEHAHR---N 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   924 HIVHRDIKSSNILL--DGNFKayVADFGLSRLILPYRTHVTTELVGTLGYIPPEygQAW--VATLRGDVYSFGVVMLELL 999
Cdd:NF033483  127 GIVHRDIKPQNILItkDGRVK--VTDFGIARALSSTTMTQTNSVLGTVHYLSPE--QARggTVDARSDIYSLGIVLYEML 202

                  ....*
gi 15218425  1000 TGKRP 1004
Cdd:NF033483  203 TGRPP 207
 
Name Accession Description Interval E-value
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
33-1076 1.87e-105

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 353.38  E-value: 1.87e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    33 VLSISVFFLTVSEAVCNLQDRDSLLWFSGNVSSPVSPL-HWNSSIDCCSWEGISCDKSpeNRVTSIILSSRGLSGNLPSS 111
Cdd:PLN00113   11 YLIFMLFFLFLNFSMLHAEELELLLSFKSSINDPLKYLsNWNSSADVCLWQGITCNNS--SRVVSIDLSGKNISGKISSA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   112 VLDLQRLSRLDLSHNRLSGPLPPGFLSALDQLLVLDLSYNSFKGELPlqqsfgNGSngIFPIQTVDLSSNLLEGEILSSS 191
Cdd:PLN00113   89 IFRLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFTGSIP------RGS--IPNLETLDLSNNMLSGEIPNDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   192 VFLqgaFNLTSFNVSNNSFTGSIP---------SFMCTASPQLTK--------------LDFSYNDFSGDLSQELSRCSR 248
Cdd:PLN00113  161 GSF---SSLKVLDLGGNVLVGKIPnsltnltslEFLTLASNQLVGqiprelgqmkslkwIYLGYNNLSGEIPYEIGGLTS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   249 LSVLRAGFNNLSGEIPKEIYNLPELEQLFLPVNRLSGKIDNGITRLTKLTLLELYSNHIEGEIPKDIGKLSKLSSLQLHV 328
Cdd:PLN00113  238 LNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   329 NNLMGSIPVSLANCTKLVKLNLRVNQLGGTLSAiDFSRFQSLSILDLGNNSFTGEFPSTVYSCKMMTAMRFAGNKLTGQI 408
Cdd:PLN00113  318 NNFTGKIPVALTSLPRLQVLQLWSNKFSGEIPK-NLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   409 SPQVLELESLSFFTFSDNkmtNLTGALSilQGCKKLStLIMAKNFYDETVPSNKDFLRSDgFPSLQIFGIGACRLTGEIP 488
Cdd:PLN00113  397 PKSLGACRSLRRVRLQDN---SFSGELP--SEFTKLP-LVYFLDISNNNLQGRINSRKWD-MPSLQMLSLARNKFFGGLP 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   489 AwLIKLQRVEVMDLSMNRFVGTIPGWLGTLPDLFYLDLSDNFLTGELPKELFQLRALMSqkaydaternylelpvfvnpn 568
Cdd:PLN00113  470 D-SFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVS--------------------- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   569 nvttnqqynqlsslpptiyikrnnltgtipvevgqlkvlhiLELLGNNFSGSIPDELSNLTNLERLDLSNNNLSGRIPWS 648
Cdd:PLN00113  528 -----------------------------------------LDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKN 566
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   649 LTGLHFLSYFNVANNTLSGPIPTGTQFDTFPKANFEGNPLLCGGVLLTSCDPTQhsttkmgkgKVNRTLVLGLVLGLFFG 728
Cdd:PLN00113  567 LGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDLCGGDTTSGLPPCK---------RVRKTPSWWFYITCTLG 637
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   729 VSLILVLLALLVLSKRRVNPGDSENAEleiNSNGSYSevppgsdkdislvLLFGNSRYeVKDLTIFELLKATdnfSQANI 808
Cdd:PLN00113  638 AFLVLALVAFGFVFIRGRNNLELKRVE---NEDGTWE-------------LQFFDSKV-SKSITINDILSSL---KEENV 697
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   809 IGCGGFGLVYKA-TLDNGTKLAVKKlTGDYGMMEKEFKAEvevLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:PLN00113  698 ISRGKKGASYKGkSIKNGMQFVVKE-INDVNSIPSSEIAD---MGKLQHPNIVKLIGLCRSEKGAYLIHEYIEGKNLSEV 773
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   888 LHenpegpaQLDWPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVadfglsRLILPYRTHVTTELVG 967
Cdd:PLN00113  774 LR-------NLSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHL------RLSLPGLLCTDTKCFI 840
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   968 TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVfRPKMSRELVAWVHTMKRDGKPEEVFDTLLRE--SGNEEA 1045
Cdd:PLN00113  841 SSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADA-EFGVHGSIVEWARYCYSDCHLDMWIDPSIRGdvSVNQNE 919
                        1050      1060      1070
                  ....*....|....*....|....*....|.
gi 15218425  1046 MLRVLDIACMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:PLN00113  920 IVEVMNLALHCTATDPTARPCANDVLKTLES 950
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
809-1077 3.16e-91

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: 293.25  E-value: 3.16e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGD-YGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14664    1 IGRGGAGTVYKGVMPNGTLVAVKRLKGEgTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEGPAQLDWPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVG 967
Cdd:cd14664   81 LHSRPESQPPLDWETRQRIALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMSSVAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  968 TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAWVHTMKRDGKPEEVFDTLLRESGNEEAML 1047
Cdd:cd14664  161 SYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDGVDIVDWVRGLLEEKKVEALVDPDLQGVYKLEEVE 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 15218425 1048 RVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14664  241 QVFQVALLCTQSSPMERPTMREVVRMLEGD 270
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
809-1077 1.26e-89

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: 288.79  E-value: 1.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKL-TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14066    1 IGSGGFGTVYKGVLENGTVVAVKRLnEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEGPAqLDWPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYR-THVTTELV 966
Cdd:cd14066   81 LHCHKGSPP-LPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSEsVSKTSAVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  967 GTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSR-ELVAWVHtMKRDGKPEEVFD-TLLRESGN-E 1043
Cdd:cd14066  160 GTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRkDLVEWVE-SKGKEELEDILDkRLVDDDGVeE 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15218425 1044 EAMLRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14066  239 EEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
809-1074 1.66e-60

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: 207.00  E-value: 1.66e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLdNGTKLAVKKLT--GDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDY 886
Cdd:cd13999    1 IGSGSFGEVYKGKW-RGTDVAIKKLKveDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlILPYRTHVTTELV 966
Cdd:cd13999   80 LLHKKKI---PLSWSLRLKIALDIARGMNYLHS---PPIIHRDLKSLNILLDENFTVKIADFGLSR-IKNSTTEKMTGVV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  967 GTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVawVHTMKR----DGKPEEVFDTLLResgn 1042
Cdd:cd13999  153 GTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAV--VQKGLRppipPDCPPELSKLIKR---- 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 15218425 1043 eeamlrvldiacmCVNQNPMKRPNIQQVVDWL 1074
Cdd:cd13999  227 -------------CWNEDPEKRPSFSEIVKRL 245
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
809-1077 2.56e-57

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 200.05  E-value: 2.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNgTKLAVKKLTG----DYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd14159    1 IGEGGFGCVYQAVMRN-TEYAVKRLKEdselDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHENPEGPAqLDWPKRLNIMRGASSGLAYMHQiCEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTE 964
Cdd:cd14159   80 EDRLHCQVSCPC-LSWSQRLHVLLGTARAIQYLHS-DSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPKQPGMSS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LV-------GTLGYIPPEY---GQAWVATlrgDVYSFGVVMLELLTGKRPMEV---FRPKMSRELV---------AWVHT 1022
Cdd:cd14159  158 TLartqtvrGTLAYLPEEYvktGTLSVEI---DVYSFGVVLLELLTGRRAMEVdscSPTKYLKDLVkeeeeaqhtPTTMT 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425 1023 MKRDGKPEEVFDTLLRESGNEEAM-------LRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14159  235 HSAEAQAAQLATSICQKHLDPQAGpcppelgIEISQLACRCLHRRAKKRPPMTEVFQELERL 296
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
795-1077 3.56e-47

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 170.76  E-value: 3.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  795 ELLKATDNF------SQANIIGCGGFGLVYKATLdNGTKLAVKKLT----GDYGMMEKEFKAEVEVLSRAKHENLVALQG 864
Cdd:cd14158    3 ELKNMTNNFderpisVGGNKLGEGGFGVVFKGYI-NDKNVAVKKLAamvdISTEDLTKQFEQEIQVMAKCQHENLVELLG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  865 YCVHDSARILIYSFMENGSLDYWLHENPEGPAqLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAY 944
Cdd:cd14158   82 YSCDGPQLCLVYTYMPNGSLLDRLACLNDTPP-LSWHMRCKIAQGTANGINYLH---ENNHIHRDIKSANILLDETFVPK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  945 VADFGLSRLILPYRTHVTTE-LVGTLGYIPPEYGQAWVaTLRGDVYSFGVVMLELLTGKRPMEVFRPKmsrelvAWVHTM 1023
Cdd:cd14158  158 ISDFGLARASEKFSQTIMTErIVGTTAYMAPEALRGEI-TPKSDIFSFGVVLLEIITGLPPVDENRDP------QLLLDI 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425 1024 KRDGKPEE--VFDTLLRESGN--EEAMLRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14158  231 KEEIEDEEktIEDYVDKKMGDwdSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
807-1070 1.60e-44

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 161.93  E-value: 1.60e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     807 NIIGCGGFGLVYKAT-LDNGTKLAVKKL-TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:smart00220    5 EKLGEGSFGKVYLARdKKTGKLVAIKVIkKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDL 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     885 DYWLHEN---PEGPAQldwpkrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPyrTHV 961
Cdd:smart00220   85 FDLLKKRgrlSEDEAR-------FYLRQILSALEYLHSK---GIVHRDLKPENILLDEDGHVKLADFGLARQLDP--GEK 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     962 TTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRPmevFRPKMSRELvawvhTMKRDGKPEEVFDT 1035
Cdd:smart00220  153 LTTFVGTPEYMAPEvllgkgYGKAV------DIWSLGVILYELLTGKPP---FPGDDQLLE-----LFKKIGKPKPPFPP 218
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 15218425    1036 LLRESGNEeamlrVLDIACMCVNQNPMKRPNIQQV 1070
Cdd:smart00220  219 PEWDISPE-----AKDLIRKLLVKDPEKRLTAEEA 248
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
808-1074 6.01e-44

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: 160.41  E-value: 6.01e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     808 IIGCGGFGLVYKATLDNGTKL-----AVKKLTGDYGM-MEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:smart00221    6 KLGEGAFGEVYKGTLKGKGDGkevevAVKTLKEDASEqQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     882 GSLDYWLHENpeGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHV 961
Cdd:smart00221   86 GDLLDYLRKN--RPKELSLSDLLSFALQIARGMEYLESK---NFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYK 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     962 TTELVGTLGYIPPE---YGQAWVATlrgDVYSFGVVMLELLT-GKRPmevfRPKMS-RELVAWVHTMKRDGKPEEVFDtl 1036
Cdd:smart00221  161 VKGGKLPIRWMAPEslkEGKFTSKS---DVWSFGVLLWEIFTlGEEP----YPGMSnAEVLEYLKKGYRLPKPPNCPP-- 231
                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 15218425    1037 lresgneeamlRVLDIACMCVNQNPMKRPNIQQVVDWL 1074
Cdd:smart00221  232 -----------ELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
808-1074 7.97e-44

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 160.00  E-value: 7.97e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     808 IIGCGGFGLVYKATL-----DNGTKLAVKKLTGDYGM-MEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:smart00219    6 KLGEGAFGEVYKGKLkgkggKKKVEVAVKTLKEDASEqQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYMEG 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     882 GSLDYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHV 961
Cdd:smart00219   86 GDLLSYLRKNRP---KLSLSDLLSFALQIARGMEYLESK---NFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYR 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425     962 TTELVGTLGYIPPE---YGQAWVATlrgDVYSFGVVMLELLT-GKRPmevfRPKMS-RELVAWVHTMKR----DGKPEEV 1032
Cdd:smart00219  160 KRGGKLPIRWMAPEslkEGKFTSKS---DVWSFGVLLWEIFTlGEQP----YPGMSnEEVLEYLKNGYRlpqpPNCPPEL 232
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 15218425    1033 FdtllresgneeamlrvlDIACMCVNQNPMKRPNIQQVVDWL 1074
Cdd:smart00219  233 Y-----------------DLMLQCWAEDPEDRPTFSELVEIL 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
809-1023 3.05e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 164.80  E-value: 3.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKE---FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:COG0515   15 LGRGGMGVVYLARdLRLGRPVALKVLRPELAADPEArerFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGESL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHEnpEGPaqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTE 964
Cdd:COG0515   95 ADLLRR--RGP--LPPAEALRILAQLAEALAAAHAA---GIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQTGT 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  965 LVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME--------------------VFRPKMSRELVAWVHTM 1023
Cdd:COG0515  168 VVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDgdspaellrahlrepppppsELRPDLPPALDAIVLRA 246
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
809-1004 5.50e-43

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: 157.75  E-value: 5.50e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMME---KEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd14014    8 LGRGGMGEVYRARdTLLGRPVAIKVLRPELAEDEefrERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHENpeGPaqLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLI-LPYRTHvTT 963
Cdd:cd14014   88 ADLLRER--GP--LPPREALRILAQIADALAAAHR---AGIVHRDIKPANILLTEDGRVKLTDFGIARALgDSGLTQ-TG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15218425  964 ELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14014  160 SVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPP 200
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
809-1071 3.93e-42

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: 154.96  E-value: 3.93e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    809 IGCGGFGLVYKATL-----DNGTKLAVKKLTGDYGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:pfam07714    7 LGEGAFGEVYKGTLkgegeNTKIKVAVKTLKEGADEEEREdFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    883 SLDYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP-YRTHV 961
Cdd:pfam07714   87 DLLDFLRKHKR---KLTLKDLLSMALQIAKGMEYLESK---NFVHRDLAARNCLVSENLVVKISDFGLSRDIYDdDYYRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    962 TTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKR----DGKPEEVFDTL 1036
Cdd:pfam07714  161 RGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQP---YPGMSNEEVLEFLEDGYRlpqpENCPDELYDLM 237
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 15218425   1037 LResgneeamlrvldiacmCVNQNPMKRPNIQQVV 1071
Cdd:pfam07714  238 KQ-----------------CWAYDPEDRPTFSELV 255
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
807-1075 6.37e-40

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 148.84  E-value: 6.37e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLDNG----TKLAVKKLTGDYGMME-KEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGdgktVDVAVKTLKEDASESErKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHEN-----PEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP 956
Cdd:cd00192   81 GDLLDFLRKSrpvfpSPEPSTLSLKDLLSFAIQIAKGMEYLASK---KFVHRDLAARNCLVGEDLVVKISDFGLSRDIYD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  957 YRTHVTTelvgTLGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMS-RELVAWVHTMKRDGKP 1029
Cdd:cd00192  158 DDYYRKK----TGGKLPirwmaPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPY----PGLSnEEVLEYLRKGYRLPKP 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15218425 1030 EEVFDTLlresgneeamlrvLDIACMCVNQNPMKRPNIQQVVDWLK 1075
Cdd:cd00192  230 ENCPDEL-------------YELMLSCWQLDPEDRPTFSELVERLE 262
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
809-998 8.59e-39

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: 143.95  E-value: 8.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLT-GDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDY 886
Cdd:cd00180    1 LGKGSFGKVYKARdKETGKKVAVKVIPkEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENPEGpaqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELV 966
Cdd:cd00180   81 LLKENKGP---LSEEEALSILRQLLSALEYLHSN---GIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGG 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15218425  967 GTLGYIPPE-------YGQAwvatlrGDVYSFGVVMLEL 998
Cdd:cd00180  155 TTPPYYAPPellggryYGPK------VDIWSLGVILYEL 187
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
809-1066 2.41e-38

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: 144.13  E-value: 2.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMME--KEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd13978    1 LGSGGFGTVSKArHVSWFGMVAIKCLHSSPNCIEerKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHENPEGPAqldWPKRLNIMRGASSGLAYMHQIcEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL----ILPYRTHV 961
Cdd:cd13978   81 SLLEREIQDVP---WSLRFRIIHEIALGMNFLHNM-DPPLLHHDLKPENILLDNHFHVKISDFGLSKLgmksISANRRRG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  962 TTELVGTLGYIPPEY---GQAwVATLRGDVYSFGVVMLELLTGKRPMEvfrpkmSRELVAWVHTMKRDGKPEEVFDtlLR 1038
Cdd:cd13978  157 TENLGGTPIYMAPEAfddFNK-KPTSKSDVYSFAIVIWAVLTRKEPFE------NAINPLLIMQIVSKGDRPSLDD--IG 227
                        250       260
                 ....*....|....*....|....*...
gi 15218425 1039 ESGNEEAMLRVLDIACMCVNQNPMKRPN 1066
Cdd:cd13978  228 RLKQIENVQELISLMIRCWDGNPDARPT 255
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
808-1069 4.89e-34

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: 131.49  E-value: 4.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVK--KLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSArilIYSFME---N 881
Cdd:cd06606    7 LLGKGSFGSVYLALnLDTGELMAVKevELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENT---LNIFLEyvpG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHEN---PEgpaqldwpkrlNIMRGAS----SGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd06606   84 GSLASLLKKFgklPE-----------PVVRKYTrqilEGLEYLH---SNGIVHRDIKGANILVDSDGVVKLADFGCAKRL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 LPYRT-HVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEvfrpkmsrELVAWVHTMKRDGKPEEVf 1033
Cdd:cd06606  150 AEIATgEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWS--------ELGNPVAALFKIGSSGEP- 220
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 15218425 1034 dTLLRESGNEEAmlrvLDIACMCVNQNPMKRPNIQQ 1069
Cdd:cd06606  221 -PPIPEHLSEEA----KDFLRKCLQRDPKKRPTADE 251
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
812-1066 6.69e-32

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 126.19  E-value: 6.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  812 GGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14026    8 GAFGTVSRARhADWRVTVAIKCLKLDSPVGDSERNcllKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSLNEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEGPAqLDWPKRLNIMRGASSGLAYMHQICEPhIVHRDIKSSNILLDGNFKAYVADFGLSRL----ILPYRTHVTT 963
Cdd:cd14026   88 LHEKDIYPD-VAWPLRLRILYEIALGVNYLHNMSPP-LLHHDLKTQNILLDGEFHVKIADFGLSKWrqlsISQSRSSKSA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  964 ELVGTLGYIPPEY---GQAWVATLRGDVYSFGVVMLELLTGKRPME-VFRPkmsrelVAWVHTMKRDGKPEEVFDTLLRE 1039
Cdd:cd14026  166 PEGGTIIYMPPEEyepSQKRRASVKHDIYSYAIIMWEVLSRKIPFEeVTNP------LQIMYSVSQGHRPDTGEDSLPVD 239
                        250       260
                 ....*....|....*....|....*..
gi 15218425 1040 SGNEEAMLRVLDIACMcvnQNPMKRPN 1066
Cdd:cd14026  240 IPHRATLINLIESGWA---QNPDERPS 263
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
809-1077 1.91e-29

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: 118.31  E-value: 1.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTkLAVKKLtgDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL 888
Cdd:cd14058    1 VGRGSFGVVCKARWRNQI-VAVKII--ESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HeNPEGPAQLDWPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILL-DGNFKAYVADFGLSRLIlpyRTHVTTElVG 967
Cdd:cd14058   78 H-GKEPKPIYTAAHAMSWALQCAKGVAYLHSMKPKALIHRDLKPPNLLLtNGGTVLKICDFGTACDI---STHMTNN-KG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  968 TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVaWVHTMKR----DGKPEEVfdtllresgnE 1043
Cdd:cd14058  153 SAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMW-AVHNGERppliKNCPKPI----------E 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15218425 1044 EAMLRvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14058  222 SLMTR-------CWSKDPEKRPSMKEIVKIMSHL 248
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
793-1069 2.15e-29

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: 118.07  E-value: 2.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  793 IFELLKAtdnfsqaniIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSA 871
Cdd:cd05122    1 LFEILEK---------IGKGGFGVVYKARhKKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  872 RILIYSFMENGSLDYWLHEnpegpaqldWPKRLN------IMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYV 945
Cdd:cd05122   72 LWIVMEFCSGGSLKDLLKN---------TNKTLTeqqiayVCKEVLKGLEYLHSH---GIIHRDIKAANILLTSDGEVKL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  946 ADFGLSRLILPyrTHVTTELVGTLGYIPPE------YGQAwvatlrGDVYSFGVVMLELLTGKRPMEVFRPkmSRELVaw 1019
Cdd:cd05122  140 IDFGLSAQLSD--GKTRNTFVGTPYWMAPEviqgkpYGFK------ADIWSLGITAIEMAEGKPPYSELPP--MKALF-- 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425 1020 vhTMKRDGKPEevfdtlLRESGNEEAMLRvlDIACMCVNQNPMKRPNIQQ 1069
Cdd:cd05122  208 --LIATNGPPG------LRNPKKWSKEFK--DFLKKCLQKDPEKRPTAEQ 247
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
808-1077 8.98e-29

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 116.34  E-value: 8.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDnGTKLAVKKL----TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd14061    1 VIGVGGFGKVYRGIWR-GEEVAVKAArqdpDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENPEGPAQL-DWPkrLNIMRGassgLAYMHQICEPHIVHRDIKSSNILLD--------GNFKAYVADFGLSRLI 954
Cdd:cd14061   80 LNRVLAGRKIPPHVLvDWA--IQIARG----MNYLHNEAPVPIIHRDLKSSNILILeaienedlENKTLKITDFGLAREW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 lpyrtHVTTEL--VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMsrelVAWVHTMKRDGKP--- 1029
Cdd:cd14061  154 -----HKTTRMsaAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLA----VAYGVAVNKLTLPips 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425 1030 --EEVFDTLLREsgneeamlrvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14061  225 tcPEPFAQLMKD----------------CWQPDPHDRPSFADILKQLENI 258
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
809-1075 1.24e-28

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: 116.03  E-value: 1.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTG----DYGMmEKEFKAEVEVLSRAKHENLVALQGYcVHDSARI-LIYSFMENG 882
Cdd:cd14007    8 LGKGKFGNVYLAReKKSGFIVALKVISKsqlqKSGL-EHQLRREIEIQSHLRHPNILRLYGY-FEDKKRIyLILEYAPNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLdyWLHENPEGPaqLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHvt 962
Cdd:cd14007   86 EL--YKELKKQKR--FDEKEAAKYIYQLALALDYLH---SKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSNRRK-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  963 tELVGTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRPmevFRPKMSRElvawvhTMKRDGKPEEVFDtl 1036
Cdd:cd14007  157 -TFCGTLDYLPPEmvegkeYDY------KVDIWSLGVLCYELLVGKPP---FESKSHQE------TYKRIQNVDIKFP-- 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 15218425 1037 lrESGNEEAMlrvlDIACMCVNQNPMKRPNIQQVVD--WLK 1075
Cdd:cd14007  219 --SSVSPEAK----DLISKLLQKDPSKRLSLEQVLNhpWIK 253
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
809-1017 1.63e-28

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 116.14  E-value: 1.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGT---KLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd14160    1 IGEGEIFEVYRVRIGNRSyavKLFKQEKKMQWKKHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHENpEGPAQLDWPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLilpyRTH----- 960
Cdd:cd14160   81 DRLQCH-GVTKPLSWHERINILIGIAKAIHYLHNSQPCTVICGNISSANILLDDQMQPKLTDFALAHF----RPHledqs 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  961 ----VTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKR-----PMEVFRPKMSRELV 1017
Cdd:cd14160  156 ctinMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCKvvlddPKHLQLRDLLHELM 221
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
809-1070 2.52e-28

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: 114.92  E-value: 2.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVK-----KLTGDygmMEKEFKAEVEVLSRAKHENLVALqgYCVHDSARIlIYSFME-- 880
Cdd:cd14003    8 LGEGSFGKVKLARhKLTGEKVAIKiidksKLKEE---IEEKIKREIEIMKLLNHPNIIKL--YEVIETENK-IYLVMEya 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 -NGSL-DYwLHEN---PEGPAQldwpkrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL 955
Cdd:cd14003   82 sGGELfDY-IVNNgrlSEDEAR-------RFFQQLISAVDYCHSN---GIVHRDLKLENILLDKNGNLKIIDFGLSNEFR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 PYRTHVTTelVGTLGYIPPEygqawvaTLRG--------DVYSFGVVMLELLTGKRP------MEVFRPKMSRELVAWVH 1021
Cdd:cd14003  151 GGSLLKTF--CGTPAYAAPE-------VLLGrkydgpkaDVWSLGVILYAMLTGYLPfdddndSKLFRKILKGKYPIPSH 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425 1022 tmkrdgKPEEVFDTLLResgneeaMLRVldiacmcvnqNPMKRPNIQQV 1070
Cdd:cd14003  222 ------LSPDARDLIRR-------MLVV----------DPSKRITIEEI 247
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
809-1065 4.17e-28

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: 114.30  E-value: 4.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGdyGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL-DY 886
Cdd:cd05034    3 LGAGQFGEVWMGVWNGTTKVAVKTLKP--GTMSPEaFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLlDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WlhENPEGPAqLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP--YRTHVTTE 964
Cdd:cd05034   81 L--RTGEGRA-LRLPQLIDMAAQIASGMAYLE---SRNYIHRDLAARNILVGENNVCKVADFGLARLIEDdeYTAREGAK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LvgTLGYIPPE---YGqawVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMS-RELVAWVHTMKRDGKPEEVFDTLlre 1039
Cdd:cd05034  155 F--PIKWTAPEaalYG---RFTIKSDVWSFGILLYEIVTyGRVPY----PGMTnREVLEQVERGYRMPKPPGCPDEL--- 222
                        250       260
                 ....*....|....*....|....*.
gi 15218425 1040 sgneeamlrvLDIACMCVNQNPMKRP 1065
Cdd:cd05034  223 ----------YDIMLQCWKKEPEERP 238
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
807-1004 5.08e-28

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 114.39  E-value: 5.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLDNGTK----LAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd05033   10 KVIGGGEFGEVCSGSLKLPGKkeidVAIKTLKSGYSDKQRlDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMEN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHV 961
Cdd:cd05033   90 GSLDKFLRENDG---KFTVTQLVGMLRGIASGMKYLSEMN---YVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEATY 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425  962 TTElvGtlGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRP 1004
Cdd:cd05033  164 TTK--G--GKIPirwtaPEAIAYRKFTSASDVWSFGIVMWEVMSyGERP 208
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
809-1074 1.41e-27

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 112.97  E-value: 1.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGmmEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14065    1 LGKGFFGEVYKVThRETGKVMVMKELKRFDE--QRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEgpaQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL---DGNFKAYVADFGLSRLILPYRTHVTTE 964
Cdd:cd14065   79 LKSMDE---QLPWSQRVSLAKDIASGMAYLHSK---NIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKTKKPDR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 -----LVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELL--TGKRPMEVFRPKMSRELVAWVHTMKRDGKPEEVFDTLL 1037
Cdd:cd14065  153 kkrltVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIgrVPADPDYLPRTMDFGLDVRAFRTLYVPDCPPSFLPLAI 232
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15218425 1038 ResgneeamlrvldiacmCVNQNPMKRPNIQQVVDWL 1074
Cdd:cd14065  233 R-----------------CCQLDPEKRPSFVELEHHL 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
807-1070 2.02e-27

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: 112.57  E-value: 2.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKAT-LDNGTKLAVKKL--TGDYGMMEKEFKAEVEVLSRAKHENLVALqgYCVHDSaRILIYSFME--- 880
Cdd:cd05117    6 KVLGRGSFGVVRLAVhKKTGEEYAVKIIdkKKLKSEDEEMLRREIEILKRLDHPNIVKL--YEVFED-DKNLYLVMElct 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHEN---PEGPAQldwpkrlNIMRGASSGLAYMHQICephIVHRDIKSSNILL---DGNFKAYVADFGLSRLI 954
Cdd:cd05117   83 GGELFDRIVKKgsfSEREAA-------KIMKQILSAVAYLHSQG---IVHRDLKPENILLaskDPDSPIKIIDFGLAKIF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 LPyrTHVTTELVGTLGYIPPE------YGQAwvatlrGDVYSFGVVMLELLTGKRPmevFRPKMSRELVawvhTMKRDGK 1028
Cdd:cd05117  153 EE--GEKLKTVCGTPYYVAPEvlkgkgYGKK------CDIWSLGVILYILLCGYPP---FYGETEQELF----EKILKGK 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15218425 1029 ---PEEVFDTLlresgNEEAMLRVLDiaCMCVnqNPMKRPNIQQV 1070
Cdd:cd05117  218 ysfDSPEWKNV-----SEEAKDLIKR--LLVV--DPKKRLTAAEA 253
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
809-1039 3.20e-27

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: 111.97  E-value: 3.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTgDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL 888
Cdd:cd05112   12 IGSGQFGLVHLGYWLNKDKVAIKTIR-EGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENpegPAQLDWPKRLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVGT 968
Cdd:cd05112   91 RTQ---RGLFSAETLLGMCLDVCEGMAYLEEAS---VIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTGTKFP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  969 LGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPME----------------VFRPKMSR----ELVAWVHTMKRDG 1027
Cdd:cd05112  165 VKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYEnrsnsevvedinagfrLYKPRLASthvyEIMNHCWKERPED 244
                        250
                 ....*....|..
gi 15218425 1028 KPEevFDTLLRE 1039
Cdd:cd05112  245 RPS--FSLLLRQ 254
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
805-1004 3.58e-27

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: 112.01  E-value: 3.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  805 QANIIGCGGFGLVYKA-TLDNGTKLAVKKLT---GDYGMMeKEFKAEVEVLSRAKHENLVALQGYCVHdsaRILIYSFME 880
Cdd:cd06626    4 RGNKIGEGTFGKVYTAvNLDTGELMAMKEIRfqdNDPKTI-KEIADEMKVLEGLDHPNLVRYYGVEVH---REEVYIFME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 ---NGSLDYWLHENPEGPAQLdwpkrlnIMRGAS---SGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd06626   80 ycqEGTLEELLRHGRILDEAV-------IRVYTLqllEGLAYLH---ENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  955 LPYRTHVT----TELVGTLGYIPPEY--GQAWVATLRG-DVYSFGVVMLELLTGKRP 1004
Cdd:cd06626  150 KNNTTTMApgevNSLVGTPAYMAPEVitGNKGEGHGRAaDIWSLGCVVLEMATGKRP 206
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
809-1022 4.61e-27

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: 111.47  E-value: 4.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTkLAVKKLTGDYGMMEKE---FKAEVEVLSRAKHENLVALQGYCVHDSARILIYS-FMENGSL 884
Cdd:cd14064    1 IGSGSFGKVYKGRCRNKI-VAIKRYRANTYCSKSDvdmFCREVSILCRLNHPCVIQFVGACLDDPSQFAIVTqYVSGGSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQICEPhIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTE 964
Cdd:cd14064   80 FSLLHEQKR---VIDLQSKLIIAVDVAKGMEYLHNLTQP-IIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  965 LVGTLGYIPPE-YGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAWVHT 1022
Cdd:cd14064  156 QPGNLRWMAPEvFTQCTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYHHI 214
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
809-1077 4.92e-27

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 111.29  E-value: 4.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLdNGTKLAVKKLTgDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL-DYW 887
Cdd:cd05039   14 IGKGEFGDVMLGDY-RGQKVAVKCLK-DDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSLvDYL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 lheNPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRlilpyrtHVTTELVG 967
Cdd:cd05039   92 ---RSRGRAVITRKDQLGFALDVCEGMEYLE---SKKFVHRDLAARNVLVSEDNVAKVSDFGLAK-------EASSNQDG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  968 tlGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMS-RELVAWVHTMKR----DGKPEEVFDTL 1036
Cdd:cd05039  159 --GKLPikwtaPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY----PRIPlKDVVPHVEKGYRmeapEGCPPEVYKVM 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 15218425 1037 LresgneeamlrvldiacMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05039  233 K-----------------NCWELDPAKRPTFKQLREKLEHI 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
802-1004 1.20e-26

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: 110.01  E-value: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKA-TLDNGTKLAVK--KLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGyCVHDSARI-LIYS 877
Cdd:cd06627    1 NYQLGDLIGRGAFGSVYKGlNLNTGEFVAIKqiSLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIG-SVKTKDSLyIILE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYWLHENpeGPaqldWPKRLNIMRGAS--SGLAYMHqicEPHIVHRDIKSSNILL--DGNFKayVADFGLSrL 953
Cdd:cd06627   80 YVENGSLASIIKKF--GK----FPESLVAVYIYQvlEGLAYLH---EQGVIHRDIKGANILTtkDGLVK--LADFGVA-T 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  954 ILPYRTHVTTELVGTLGYIPPEygqawVATLRG-----DVYSFGVVMLELLTGKRP 1004
Cdd:cd06627  148 KLNEVEKDENSVVGTPYWMAPE-----VIEMSGvttasDIWSVGCTVIELLTGNPP 198
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
808-1000 1.36e-26

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 110.88  E-value: 1.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTkLAVKKltgdygMMEKEFK---AEVEV--LSRAKHENLvaLQGYC---VHDSARI---LIY 876
Cdd:cd14053    2 IKARGRFGAVWKAQYLNRL-VAVKI------FPLQEKQswlTEREIysLPGMKHENI--LQFIGaekHGESLEAeywLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHENpegpaQLDWPKRLNIMRGASSGLAYMH-------QICEPHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd14053   73 EFHERGSLCDYLKGN-----VISWNELCKIAESMARGLAYLHedipatnGGHKPSIAHRDFKSKNVLLKSDLTACIADFG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  950 LSRLILPYR----THvttELVGTLGYIPPEYGQAWV-----ATLRGDVYSFGVVMLELLT 1000
Cdd:cd14053  148 LALKFEPGKscgdTH---GQVGTRRYMAPEVLEGAInftrdAFLRIDMYAMGLVLWELLS 204
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
809-1070 1.39e-26

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: 109.86  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKK--LTGdygMMEKEFKA---EVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd08215    8 IGKGSFGSAYLVRrKSDGKLYVLKEidLSN---MSEKEREEalnEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRlILPYRTHVT 962
Cdd:cd08215   85 DLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSR---KILHRDLKTQNIFLTKDGVVKLGDFGISK-VLESTTDLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  963 TELVGTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRPmevFRPKMSRELVAWVhtMKRDGKP-EEVFDT 1035
Cdd:cd08215  161 KTVVGTPYYLSPElcenkpYNY------KSDIWALGCVLYELCTLKHP---FEANNLPALVYKI--VKGQYPPiPSQYSS 229
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15218425 1036 LLResgneeamlrvlDIACMCVNQNPMKRPNIQQV 1070
Cdd:cd08215  230 ELR------------DLVNSMLQKDPEKRPSANEI 252
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
808-1002 4.14e-26

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


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 109.58  E-value: 4.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYgmmEKE-----FKAEVEVLSRAKHENLVALQGYCV-HDSARI-----LI 875
Cdd:cd07840    6 QIGEGTYGQVYKArNKKTGELVALKKIRMEN---EKEgfpitAIREIKLLQKLDHPNVVRLKEIVTsKGSAKYkgsiyMV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFME---NGsldywLHENPEgpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd07840   83 FEYMDhdlTG-----LLDNPE--VKFTESQIKCYMKQLLEGLQYLHSN---GILHRDIKGSNILINNDGVLKLADFGLAR 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  953 LILPYRTHVTTELVGTLGYIPPE-------YGQAwVatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd07840  153 PYTKENNADYTNRVITLWYRPPElllgatrYGPE-V-----DMWSVGCILAELFTGK 203
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
104-448 5.67e-26

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 111.95  E-value: 5.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  104 LSGNLPSSVLDLQRLSRLDLSHNRLSGPLPPGFLSALDQLLVLDLSYNSFKGELPLQQSFGNGSNGIFPIQTVDLSSNLL 183
Cdd:COG4886    2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  184 EGEILSSSVFLQGAFNLTSFNVSNNSFTGSIPsfmctaspQLTKLDFSYNDFSgDLSQELSRCSRLSVLRAGFNNLSgEI 263
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGNEELSNLT--------NLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  264 PKEIYNLPELEQLFLPVNRLSGkIDNGITRLTKLTLLELYSNHIEgEIPKDIGKLSKLSSLQLHVNNLmGSIPVSLANCT 343
Cdd:COG4886  152 PEPLGNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQL-TDLPEPLANLT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  344 KLVKLNLRVNQLGgtlSAIDFSRFQSLSILDLGNNSFTGEFPSTvySCKMMTAMRFAGNKLTGqispqvLELESLSFFTF 423
Cdd:COG4886  229 NLETLDLSNNQLT---DLPELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTD------LKLKELELLLG 297
                        330       340
                 ....*....|....*....|....*
gi 15218425  424 SDNKMTNLTGALSILQGCKKLSTLI 448
Cdd:COG4886  298 LNSLLLLLLLLNLLELLILLLLLTT 322
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
812-1009 9.17e-26

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 108.77  E-value: 9.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  812 GGFGLVYKATLDNgTKLAVKKLTGDYGM----MEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14157    4 GTFADIYKGYRHG-KQYVIKRLKETECEspksTERFFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQDR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENpEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLsRLiLPYRTHV------ 961
Cdd:cd14157   83 LQQQ-GGSHPLPWEQRLSISLGLLKAVQHLHNF---GILHGNIKSSNVLLDGNLLPKLGHSGL-RL-CPVDKKSvytmmk 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425  962 TTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFR 1009
Cdd:cd14157  157 TKVLQISLAYLPEDFVRHGQLTEKVDIFSCGVVLAEILTGIKAMDEFR 204
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
811-1077 1.60e-25

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: 106.58  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  811 CGG--FGLVYKAT-LDNGTKLAVKKLTgdygmmekEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL-DY 886
Cdd:cd14060    1 CGGgsFGSVYRAIwVSQDKEVAVKKLL--------KIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLfDY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLIlPYRTHVTteLV 966
Cdd:cd14060   73 LNSNESE---EMDMDQIMTWATDIAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFH-SHTTHMS--LV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  967 GTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMsrelVAW--VHTMKRDGKPEEV---FDTLLREsg 1041
Cdd:cd14060  147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQ----VAWlvVEKNERPTIPSSCprsFAELMRR-- 220
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 15218425 1042 neeamlrvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14060  221 --------------CWEADVKERPSFKQIIGILESM 242
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
809-1079 2.85e-25

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: 106.52  E-value: 2.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLD-NGTKLAVKKLTG-DYGMMEKEFKAEVEVLSRAKHENLVALQGyCVHDSARI-LIYSFMENGSLD 885
Cdd:cd06623    9 LGQGSSGVVYKVRHKpTGKIYALKKIHVdGDEEFRKQLLRELKTLRSCESPYVVKCYG-AFYKEGEIsIVLEYMDGGSLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHENPEgpaqldWPKRL--NIMRGASSGLAYMHQicEPHIVHRDIKSSNILL--DGNFKayVADFGLSRlILPYRTHV 961
Cdd:cd06623   88 DLLKKVGK------IPEPVlaYIARQILKGLDYLHT--KRHIIHRDIKPSNLLInsKGEVK--IADFGISK-VLENTLDQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  962 TTELVGTLGYIPPE------YGQAwvatlrGDVYSFGVVMLELLTGKRPMEvfrpkmSRELVAWVHTMKR--DGKPEEVf 1033
Cdd:cd06623  157 CNTFVGTVTYMSPEriqgesYSYA------ADIWSLGLTLLECALGKFPFL------PPGQPSFFELMQAicDGPPPSL- 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425 1034 dtllrESGNEEAMLRvlDIACMCVNQNPMKRPNIQQVVD--WLKNIEA 1079
Cdd:cd06623  224 -----PAEEFSPEFR--DFISACLQKDPKKRPSAAELLQhpFIKKADN 264
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
803-1077 3.09e-25

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: 106.36  E-value: 3.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLhENPEGPAqLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP--YRTH 960
Cdd:cd05148   88 SLLAFL-RSPEGQV-LPVASLIDMACQVAEGMAYLE---EQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEdvYLSS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTTelvgtlgyIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELVAWVHTMKRDGK-PEEVF 1033
Cdd:cd05148  163 DKK--------IPykwtaPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAGYRMPCPAKcPQEIY 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15218425 1034 DTLLresgneeamlrvldiACMCVnqNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05148  235 KIML---------------ECWAA--EPEDRPSFKALREELDNI 261
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
809-1070 3.39e-25

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: 106.42  E-value: 3.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN-GTKLAVK---KLTGDygmmEKEFK---AEVEVLSRAKHENLVALQGYCVHDSAriLIYSFMEN 881
Cdd:cd14025    4 VGSGGFGQVYKVRHKHwKTWLAIKcppSLHVD----DSERMellEEAKKMEMAKFRHILPVYGICSEPVG--LVMEYMET 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENPegpaqLDWPKRLNIMRGASSGLAYMHQIcEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHV 961
Cdd:cd14025   78 GSLEKLLASEP-----LPWELRFRIIHETAVGMNFLHCM-KPPLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHSHD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  962 TTE--LVGTLGYIPPE--YGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMsrelvawvHTMKRDGKPEEVFDTLL 1037
Cdd:cd14025  152 LSRdgLRGTIAYLPPErfKEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNIL--------HIMVKVVKGHRPSLSPI 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 15218425 1038 RESGNEEAMlRVLDIACMCVNQNPMKRPNIQQV 1070
Cdd:cd14025  224 PRQRPSECQ-QMICLMKRCWDQDPRKRPTFQDI 255
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
808-1075 4.00e-25

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: 106.16  E-value: 4.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLdNGTKLAVKKL---------------------TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYC 866
Cdd:cd14000    1 LLGDGGFGSVYRASY-KGEPVAVKIFnkhtssnfanvpadtmlrhlrATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  867 VHdsARILIYSFMENGSLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILL-----DGNF 941
Cdd:cd14000   80 IH--PLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHS---AMIIYRDLKSHNVLVwtlypNSAI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  942 KAYVADFGLSRLILPYRThVTTElvGTLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLTGKRPMEvfrPKMSRELVAWV 1020
Cdd:cd14000  155 IIKIADYGISRQCCRMGA-KGSE--GTPGFRAPEIARGNVIyNEKVDVFSFGMLLYEILSGGAPMV---GHLKFPNEFDI 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425 1021 HTMKRD--GKPEEVFDTllresgneeamlRVLDIACMCVNQNPMKRPNIQQVVDWLK 1075
Cdd:cd14000  229 HGGLRPplKQYECAPWP------------EVEVLMKKCWKENPQQRPTAVTVVSILN 273
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
809-1067 5.12e-25

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: 105.54  E-value: 5.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLdNGTKLAVKKL--TGDYGMMEKEFKAEVEVLsRAKHENLV---ALQGYCVHDSARILIYSFMENGS 883
Cdd:cd13979   11 LGSGGFGSVYKATY-KGETVAVKIVrrRRKNRASRQSFWAELNAA-RLRHENIVrvlAAETGTDFASLGLIIMEYCGNGT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHEnpeGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRT--HV 961
Cdd:cd13979   89 LQQLIYE---GSEPLPLAHRILISLDIARALRFCHS---HGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGNEvgTP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  962 TTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvHTMKRDGKPEEVFDTLLResg 1041
Cdd:cd13979  163 RSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVA--KDLRPDLSGLEDSEFGQR--- 237
                        250       260
                 ....*....|....*....|....*.
gi 15218425 1042 neeamLRVLdIACmCVNQNPMKRPNI 1067
Cdd:cd13979  238 -----LRSL-ISR-CWSAQPAERPNA 256
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
809-1065 6.01e-25

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: 105.57  E-value: 6.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDyGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL 888
Cdd:cd05068   16 LGSGQFGEVWEGLWNNTTPVAVKTLKPG-TMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEYL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENPEgpaQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP---YRTHVTTEL 965
Cdd:cd05068   95 QGKGR---SLQLPQLIDMAAQVASGMAYLES---QNYIHRDLAARNVLVGENNICKVADFGLARVIKVedeYEAREGAKF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  966 vgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMS-RELVAWVHTMKR----DGKPEEVFDTLLRe 1039
Cdd:cd05068  169 --PIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPY----PGMTnAEVLQQVERGYRmpcpPNCPPQLYDIMLE- 241
                        250       260
                 ....*....|....*....|....*.
gi 15218425 1040 sgneeamlrvldiacmCVNQNPMKRP 1065
Cdd:cd05068  242 ----------------CWKADPMERP 251
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
808-1004 9.55e-25

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: 105.12  E-value: 9.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLdNGTKLAVKKLTGD----YGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd14146    1 IIGVGGFGKVYRATW-KGQEVAVKAARQDpdedIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENPEGPAQ-----------LDWPkrLNIMRGassgLAYMHQICEPHIVHRDIKSSNILL--------DGNFKAY 944
Cdd:cd14146   80 LNRALAAANAAPGPrrarripphilVNWA--VQIARG----MLYLHEEAVVPILHRDLKSSNILLlekiehddICNKTLK 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  945 VADFGLSRlilpyRTHVTTEL--VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14146  154 ITDFGLAR-----EWHRTTKMsaAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVP 210
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
808-1004 1.13e-24

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 104.95  E-value: 1.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTK----LAVKKLTGDYGMME-KEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd05065   11 VIGAGEFGEVCRGRLKLPGKreifVAIKTLKSGYTEKQrRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENpEG---PAQLdwpkrLNIMRGASSGLAYMhqiCEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRT 959
Cdd:cd05065   91 ALDSFLRQN-DGqftVIQL-----VGMLRGIAAGMKYL---SEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTS 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  960 HVT-TELVGtlGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRP 1004
Cdd:cd05065  162 DPTyTSSLG--GKIPirwtaPEAIAYRKFTSASDVWSYGIVMWEVMSyGERP 211
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
804-1004 1.89e-24

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 104.29  E-value: 1.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  804 SQANIIGCGGFGLVYKATLDNGTK----LAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd05063    8 TKQKVIGAGEFGEVFRGILKMPGRkevaVAIKTLKPGYTEKQRqDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWL--HENPEGPAQLdwpkrLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLI-- 954
Cdd:cd05063   88 MENGALDKYLrdHDGEFSSYQL-----VGMLRGIAAGMKYLSDM---NYVHRDLAARNILVNSNLECKVSDFGLSRVLed 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  955 LPYRTHVTTElvgtlGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRP 1004
Cdd:cd05063  160 DPEGTYTTSG-----GKIPirwtaPEAIAYRKFTSASDVWSFGIVMWEVMSfGERP 210
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
809-1072 4.49e-24

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: 102.63  E-value: 4.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVK----KLTGDYGMMEKeFKAEVEVLSRAKHENLVALQGyCVHDSARIliYSFME--- 880
Cdd:cd14099    9 LGKGGFAKCYEVTdMSTGKVYAGKvvpkSSLTKPKQREK-LKSEIKIHRSLKHPNIVKFHD-CFEDEENV--YILLElcs 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSL-DYW-----LHEnPEgpAQLdwpkrlnIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFGLS-RL 953
Cdd:cd14099   85 NGSLmELLkrrkaLTE-PE--VRY-------FMRQILSGVKYLHSNR---IIHRDLKLGNLFLDENMNVKIGDFGLAaRL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  954 ILPYRTHVTteLVGTLGYIPPEYgqawVATLRG-----DVYSFGVVMLELLTGKRPMEvfrpkmSRELVAwvhTMKRDGK 1028
Cdd:cd14099  152 EYDGERKKT--LCGTPNYIAPEV----LEKKKGhsfevDIWSLGVILYTLLVGKPPFE------TSDVKE---TYKRIKK 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15218425 1029 PEEVFDTLLRESgNEEAMLrvldIACMcVNQNPMKRPNIQQVVD 1072
Cdd:cd14099  217 NEYSFPSHLSIS-DEAKDL----IRSM-LQPDPTKRPSLDEILS 254
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
809-1076 8.46e-24

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: 101.92  E-value: 8.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGdyGMMEKE-FKAEVEVLSRAKHENLVALqgYCVHDSARILIYS-FMENGSLDY 886
Cdd:cd14203    3 LGQGCFGEVWMGTWNGTTKVAIKTLKP--GTMSPEaFLEEAQIMKKLRHDKLVQL--YAVVSEEPIYIVTeFMSKGSLLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLhENPEGPAqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELV 966
Cdd:cd14203   79 FL-KDGEGKY-LKLPQLVDMAAQIASGMAYIERM---NYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  967 GTLGYIPPE---YGQawvATLRGDVYSFGVVMLELLTGKRpmeVFRPKMS-RELVAWVHTMKRDGKPEEVFDTLlresgn 1042
Cdd:cd14203  154 FPIKWTAPEaalYGR---FTIKSDVWSFGILLTELVTKGR---VPYPGMNnREVLEQVERGYRMPCPPGCPESL------ 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15218425 1043 EEAMlrvldiaCMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd14203  222 HELM-------CQCWRKDPEERPTFEYLQSFLED 248
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
809-1065 8.50e-24

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: 101.76  E-value: 8.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTgDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL 888
Cdd:cd05059   12 LGSGQFGVVHLGKWRGKIDVAIKMIK-EGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLLNYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENPE--GPAQLdwpkrLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFGLSRLIL--PYRTHVTTE 964
Cdd:cd05059   91 RERRGkfQTEQL-----LEMCKDVCEAMEYLESNG---FIHRDLAARNCLVGEQNVVKVSDFGLARYVLddEYTSSVGTK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRpkmSRELVAWVHTMKRDGKPeevfdtllresgnE 1043
Cdd:cd05059  163 F--PVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFS---NSEVVEHISQGYRLYRP-------------H 224
                        250       260
                 ....*....|....*....|..
gi 15218425 1044 EAMLRVLDIACMCVNQNPMKRP 1065
Cdd:cd05059  225 LAPTEVYTIMYSCWHEKPEERP 246
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
809-1072 8.72e-24

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: 102.52  E-value: 8.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKK-LTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILI-YSFMENGSLD 885
Cdd:cd06620   13 LGAGNGGSVSKVLhIPTGTIMAKKViHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENNNIIIcMEYMDCGSLD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHENpeGPAQLDWPKRlnIMRGASSGLAYMHQicEPHIVHRDIKSSNILLDGNFKAYVADFGLSR-LIlpyrTHVTTE 964
Cdd:cd06620   93 KILKKK--GPFPEEVLGK--IAVAVLEGLTYLYN--VHRIIHRDIKPSNILVNSKGQIKLCDFGVSGeLI----NSIADT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMevfrpkmsrelvaWVHTMKRDGK--PEEVFDtLLRESGN 1042
Cdd:cd06620  163 FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF-------------AGSNDDDDGYngPMGILD-LLQRIVN 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 15218425 1043 EEA------------MLRVLDIacmCVNQNPMKRPNIQQVVD 1072
Cdd:cd06620  229 EPPprlpkdrifpkdLRDFVDR---CLLKDPRERPSPQLLLD 267
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
803-1002 1.06e-23

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: 102.18  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYgmmEKE-FKA----EVEVLSRAKHENLVALQGYCVHDSARILIY 876
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKdKKTGEIVALKKIRLDN---EEEgIPStalrEISLLKELKHPNIVKLLDVIHTENKLYLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENgSLDYWLHENPeGPAQLDWPKrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL--DGNFKayVADFGLSRLI 954
Cdd:cd07829   78 EYCDQ-DLKKYLDKRP-GPLPPNLIK--SIMYQLLRGLAYCHSH---RILHRDLKPQNLLInrDGVLK--LADFGLARAF 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  955 -LPYRTHvTTELVgTLGYIPPE-------YGQAwVatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd07829  149 gIPLRTY-THEVV-TLWYRAPEillgskhYSTA-V-----DIWSVGCIFAELITGK 196
Pkinase pfam00069
Protein kinase domain;
808-1074 1.39e-23

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 100.01  E-value: 1.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    808 IIGCGGFGLVYKATL-DNGTKLAVKKL--TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:pfam00069    6 KLGSGSFGTVYKAKHrDTGKIVAIKKIkkEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    885 DYWLHEN---PEGPAQLdwpkrlnimrgassglaYMHQICEphivhrdikssnilldgnfkayvadfGLsrlilpYRTHV 961
Cdd:pfam00069   86 FDLLSEKgafSEREAKF-----------------IMKQILE--------------------------GL------ESGSS 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    962 TTELVGTLGYIPPE------YGQAwvatlrGDVYSFGVVMLELLTGKRPmevFRPKMSRELVAwvHTMKRDGKPEEVFDT 1035
Cdd:pfam00069  117 LTTFVGTPWYMAPEvlggnpYGPK------VDVWSLGCILYELLTGKPP---FPGINGNEIYE--LIIDQPYAFPELPSN 185
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 15218425   1036 LlresgNEEAmlrvLDIACMCVNQNPMKRPNIQQVV--DWL 1074
Cdd:pfam00069  186 L-----SEEA----KDLLKKLLKKDPSKRLTATQALqhPWF 217
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
807-1072 2.12e-23

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: 100.94  E-value: 2.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKA-TLDNGTKLAVKK-LTGDYGMMEKE----FKAEVEVLSRAKHENLVALQGYCVHDSArilIYSFME 880
Cdd:cd06632    6 QLLGSGSFGSVYEGfNGDTGDFFAVKEvSLVDDDKKSREsvkqLEQEIALLSKLRHPNIVQYYGTEREEDN---LYIFLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 ---NGSLDYWLHENpeGPaqLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPY 957
Cdd:cd06632   83 yvpGGSIHKLLQRY--GA--FEEPVIRLYTRQILSGLAYLH---SRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  958 RThvTTELVGTLGYIPPEY--GQAWVATLRGDVYSFGVVMLELLTGKRPMEVFrpkmsrELVAWVHTMKRDGKPEEVFDT 1035
Cdd:cd06632  156 SF--AKSFKGSPYWMAPEVimQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQY------EGVAAIFKIGNSGELPPIPDH 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15218425 1036 LLRESGneeamlrvlDIACMCVNQNPMKRPNIQQVVD 1072
Cdd:cd06632  228 LSPDAK---------DFIRLCLQRDPEDRPTASQLLE 255
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
799-1072 2.96e-23

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 102.59  E-value: 2.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   799 ATDNFSQ---ANIIGCGGFGLVYKATLDNGTKL-AVKKLTGDY-GMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARI 873
Cdd:PLN00034   69 AAKSLSElerVNRIGSGAGGTVYKVIHRPTGRLyALKVIYGNHeDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQ 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   874 LIYSFMENGSLdywlhenpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRl 953
Cdd:PLN00034  149 VLLEFMDGGSL--------EGTHIADEQFLADVARQILSGIAYLHR---RHIVHRDIKPSNLLINSAKNVKIADFGVSR- 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   954 ILPYRTHVTTELVGTLGYIPPE-----YGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKmsrelvAWVHTMKR--D 1026
Cdd:PLN00034  217 ILAQTMDPCNSSVGTIAYMSPErintdLNHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQG------DWASLMCAicM 290
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 15218425  1027 GKPEEVFDTLLRESGNEeamlrvldIACmCVNQNPMKRPNIQQVVD 1072
Cdd:PLN00034  291 SQPPEAPATASREFRHF--------ISC-CLQREPAKRWSAMQLLQ 327
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
808-1077 3.56e-23

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: 100.50  E-value: 3.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLdNGTKLAVKKL----TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd14145   13 IIGIGGFGKVYRAIW-IGDEVAVKAArhdpDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENPEGPAQL-DWPKRLnimrgaSSGLAYMHQICEPHIVHRDIKSSNILL-----DGNFKAY---VADFGLSRli 954
Cdd:cd14145   92 LNRVLSGKRIPPDILvNWAVQI------ARGMNYLHCEAIVPVIHRDLKSSNILIlekveNGDLSNKilkITDFGLAR-- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 lpyRTHVTTEL--VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPmevFRpKMSRELVAWVHTMKRDGKP--- 1029
Cdd:cd14145  164 ---EWHRTTKMsaAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVP---FR-GIDGLAVAYGVAMNKLSLPips 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425 1030 --EEVFDTLLREsgneeamlrvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14145  237 tcPEPFARLMED----------------CWNPDPHSRPPFTNILDQLTAI 270
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
783-1070 1.12e-22

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: 99.29  E-value: 1.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  783 NSRYEvkdltifellkatDNFSQANIIGCGGFGLVYKAT--LDnGTKLAVKK--LTGDYGMMEKEFKaEVEVLSRAKHEN 858
Cdd:cd13996    1 NSRYL-------------NDFEEIELLGSGGFGSVYKVRnkVD-GVTYAIKKirLTEKSSASEKVLR-EVKALAKLNHPN 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  859 LValqGYcvHDS--ARILIYSFME---NGSLDYWLHEnPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSS 933
Cdd:cd13996   66 IV---RY--YTAwvEEPPLYIQMElceGGTLRDWIDR-RNSSSKNDRKLALELFKQILKGVSYIH---SKGIVHRDLKPS 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  934 NILLDGNFK-AYVADFGLSRLI-------------LPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELL 999
Cdd:cd13996  137 NIFLDNDDLqVKIGDFGLATSIgnqkrelnnlnnnNNGNTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425 1000 TgkrpmeVFRPKMSRelvawVHTMK--RDGK-PEEvfdtlLRESGNEEAMLrvldIACMcVNQNPMKRPNIQQV 1070
Cdd:cd13996  217 H------PFKTAMER-----STILTdlRNGIlPES-----FKAKHPKEADL----IQSL-LSKNPEERPSAEQL 269
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
809-1004 1.16e-22

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: 99.08  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTK------LAVKKLT-GDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd05049   13 LGEGAFGKVFLGECYNLEPeqdkmlVAVKTLKdASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFEYMEH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLH----------ENPEGPAQLDWPKRLNIMRGASSGLAYMhqiCEPHIVHRDIKSSNILLDGNFKAYVADFGLS 951
Cdd:cd05049   93 GDLNKFLRshgpdaaflaSEDSAPGELTLSQLLHIAVQIASGMVYL---ASQHFVHRDLATRNCLVGTNLVVKIGDFGMS 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  952 RLILP---YRTHVTTELvgTLGYIPPE---YGQawvATLRGDVYSFGVVMLELLT-GKRP 1004
Cdd:cd05049  170 RDIYStdyYRVGGHTML--PIRWMPPEsilYRK---FTTESDVWSFGVVLWEIFTyGKQP 224
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
808-1077 2.68e-22

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: 97.75  E-value: 2.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAtLDNGTKLAVKKL----TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd14148    1 IIGVGGFGKVYKG-LWRGEEVAVKAArqdpDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENPEGPAQL-DWPKRLnimrgaSSGLAYMHQICEPHIVHRDIKSSNILL----------DGNFKayVADFGLSR 952
Cdd:cd14148   80 LNRALAGKKVPPHVLvNWAVQI------ARGMNYLHNEAIVPIIHRDLKSSNILIlepienddlsGKTLK--ITDFGLAR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  953 lilpyRTHVTTEL--VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMevfrpkmsREL----VAWVHTMKRd 1026
Cdd:cd14148  152 -----EWHKTTKMsaAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY--------REIdalaVAYGVAMNK- 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425 1027 gkpeevfDTLLRESGNEEAMLRVLDiACMCvnQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14148  218 -------LTLPIPSTCPEPFARLLE-ECWD--PDPHGRPDFGSILKRLEDI 258
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
808-998 3.49e-22

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


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 97.89  E-value: 3.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTkLAVKKLtgDYGMmEKEFKAEVEVLSRA--KHENLVALQGYCVHDSAR----ILIYSFMEN 881
Cdd:cd13998    2 VIGKGRFGEVWKASLKNEP-VAVKIF--SSRD-KQSWFREKEIYRTPmlKHENILQFIAADERDTALrtelWLVTAFHPN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENpegpaQLDWPKRLNIMRGASSGLAYMHQ---ICE---PHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL 955
Cdd:cd13998   78 GSL*DYLSLH-----TIDWVSLCRLALSVARGLAHLHSeipGCTqgkPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  956 PYRTHV---TTELVGTLGYIPPEYGQAWV------ATLRGDVYSFGVVMLEL 998
Cdd:cd13998  153 PSTGEEdnaNNGQVGTKRYMAPEVLEGAInlrdfeSFKRVDIYAMGLVLWEM 204
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
808-1004 4.21e-22

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 97.24  E-value: 4.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTK----LAVKKLTGDYgmMEKE---FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFME 880
Cdd:cd05066   11 VIGAGEFGEVCSGRLKLPGKreipVAIKTLKAGY--TEKQrrdFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHENPegpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL--PYR 958
Cdd:cd05066   89 NGSLDAFLRKHD---GQFTVIQLVGMLRGIASGMKYLSDM---GYVHRDLAARNILVNSNLVCKVSDFGLSRVLEddPEA 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  959 THVTTElvgtlGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRP 1004
Cdd:cd05066  163 AYTTRG-----GKIPirwtaPEAIAYRKFTSASDVWSYGIVMWEVMSyGERP 209
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
809-1004 4.26e-22

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: 96.82  E-value: 4.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL-DNGTKLAVKKLTGDYGMMEKEF---KAEVEVLSRAKHENLVALQgYCVHDSARI-LIYSFMENGS 883
Cdd:cd05123    1 LGKGSFGKVLLVRKkDTGKLYAMKVLRKKEIIKRKEVehtLNERNILERVNHPFIVKLH-YAFQTEEKLyLVLDYVPGGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHEN---PEGPAQLdwpkrlnimRGA--SSGLAYMHQIcepHIVHRDIKSSNILLD--GNFKayVADFGLSRlILP 956
Cdd:cd05123   80 LFSHLSKEgrfPEERARF---------YAAeiVLALEYLHSL---GIIYRDLKPENILLDsdGHIK--LTDFGLAK-ELS 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425  957 YRTHVTTELVGTLGYIPPE------YGQAwVatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05123  145 SDGDRTYTFCGTPEYLAPEvllgkgYGKA-V-----DWWSLGVLLYEMLTGKPP 192
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
809-1038 5.08e-22

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: 97.02  E-value: 5.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGdyGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARIlIYSFMENGSLDYW 887
Cdd:cd05073   19 LGAGQFGEVWMATYNKHTKVAVKTMKP--GSMSVEaFLAEANVMKTLQHDKLVKLHAVVTKEPIYI-ITEFMAKGSLLDF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEGPAQLdwPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVG 967
Cdd:cd05073   96 LKSDEGSKQPL--PKLIDFSAQIAEGMAFIEQ---RNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKF 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  968 TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPME-VFRPKMSRELVAWVHTMKRDGKPEEVFDTLLR 1038
Cdd:cd05073  171 PIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPgMSNPEVIRALERGYRMPRPENCPEELYNIMMR 243
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
809-1076 5.50e-22

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: 97.07  E-value: 5.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGdyGMMEKE-FKAEVEVLSRAKHENLVALQGyCVHDSARILIYSFMENGSLDYW 887
Cdd:cd05071   17 LGQGCFGEVWMGTWNGTTRVAIKTLKP--GTMSPEaFLQEAQVMKKLRHEKLVQLYA-VVSEEPIYIVTEYMSKGSLLDF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LheNPEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVG 967
Cdd:cd05071   94 L--KGEMGKYLRLPQLVDMAAQIASGMAYVERM---NYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  968 TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRpmeVFRPKM-SRELVAWVHTMKRDGKPEEVFDTLlresgneeam 1046
Cdd:cd05071  169 PIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGR---VPYPGMvNREVLDQVERGYRMPCPPECPESL---------- 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 15218425 1047 lrvLDIACMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd05071  236 ---HDLMCQCWRKEPEERPTFEYLQAFLED 262
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
802-1072 6.00e-22

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: 96.71  E-value: 6.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT-LDNGTKLAVKK--LTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVrKVDGRVYALKQidISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENPEGPAQLDWPKRLNIMrgASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlILPYR 958
Cdd:cd08529   81 AENGDLHSLIKSQRGRPLPEDQIWKFFIQ--TLLGLSHLHS---KKILHRDIKSMNIFLDKGDNVKIGDLGVAK-ILSDT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  959 THVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVfrpkmsRELVAWVHTMKRdGKPEEVfdtllr 1038
Cdd:cd08529  155 TNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEA------QNQGALILKIVR-GKYPPI------ 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15218425 1039 ESGNEEAMLRVLDiacMCVNQNPMKRPNIQQVVD 1072
Cdd:cd08529  222 SASYSQDLSQLID---SCLTKDYRQRPDTTELLR 252
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
807-1077 6.56e-22

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 97.07  E-value: 6.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLDN-----GTKLAVKKLTGDYGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARI--LIYSF 878
Cdd:cd05038   10 KQLGEGHFGSVELCRYDPlgdntGEQVAVKSLQPSGEEQHMSdFKREIEILRTLDHEYIVKYKGVCESPGRRSlrLIMEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYR 958
Cdd:cd05038   90 LPSGSLRDYLQRHRD---QIDLKRLLLFASQICKGMEYLG---SQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  959 THVTtelVGTLGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT----GKRPMEVFRPKMSRELVAWVHT-----MK 1024
Cdd:cd05038  164 EYYY---VKEPGESPifwyaPECLRESRFSSASDVWSFGVTLYELFTygdpSQSPPALFLRMIGIAQGQMIVTrllelLK 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425 1025 RDGK-------PEEVFDtLLREsgneeamlrvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05038  241 SGERlprppscPDEVYD-LMKE----------------CWEYEPQDRPSFSDLILIIDRL 283
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
799-1074 6.67e-22

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: 96.56  E-value: 6.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  799 ATDNFSQANIIGCGGFGLVYKATlDNGTK--LAVK---KLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYcVHDSARI 873
Cdd:cd14116    3 ALEDFEIGRPLGKGKFGNVYLAR-EKQSKfiLALKvlfKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGY-FHDATRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 -LIYSFMENGSLDYWLHEnpegPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd14116   81 yLILEYAPLGTVYRELQK----LSKFDEQRTATYITELANALSYCHS---KRVIHRDIKPENLLLGSAGELKIADFGWSV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  953 LILPYRThvtTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPmevFRPKMSRElvawvhTMKRDGKPEEV 1032
Cdd:cd14116  154 HAPSSRR---TTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPP---FEANTYQE------TYKRISRVEFT 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15218425 1033 FDTLLRESGNeeamlrvlDIACMCVNQNPMKRPNIQQVVD--WL 1074
Cdd:cd14116  222 FPDFVTEGAR--------DLISRLLKHNPSQRPMLREVLEhpWI 257
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
809-1072 6.69e-22

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: 97.03  E-value: 6.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGdyGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd05072   15 LGAGQFGEVWMGYYNNSTKVAVKTLKP--GTMSVQaFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLLDF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEGPAQLdwPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVG 967
Cdd:cd05072   93 LKSDEGGKVLL--PKLIDFSAQIAEGMAYIER---KNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  968 TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMSR-ELVAWVHTMKRDGKPEEVFDTLlresgneea 1045
Cdd:cd05072  168 PIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPY----PGMSNsDVMSALQRGYRMPRMENCPDEL--------- 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 15218425 1046 mlrvLDIACMCVNQNPMKRPN---IQQVVD 1072
Cdd:cd05072  235 ----YDIMKTCWKEKAEERPTfdyLQSVLD 260
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
809-1004 6.75e-22

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: 96.02  E-value: 6.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLdNGTKLAVKKLtgdygmmEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL 888
Cdd:cd14059    1 LGSGAQGAVFLGKF-RGEEVAVKKV-------RDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENPEGPAQL--DWPKRLnimrgaSSGLAYMHQicepH-IVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTteL 965
Cdd:cd14059   73 RAGREITPSLlvDWSKQI------ASGMNYLHL----HkIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMS--F 140
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15218425  966 VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14059  141 AGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIP 179
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
809-1004 7.66e-22

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 96.96  E-value: 7.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN------GTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd05092   13 LGEGAFGKVFLAECHNllpeqdKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRHG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLH---------ENPEG--PAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLS 951
Cdd:cd05092   93 DLNRFLRshgpdakilDGGEGqaPGQLTLGQMLQIASQIASGMVYLASL---HFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  952 RLILP---YRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRP 1004
Cdd:cd05092  170 RDIYStdyYRVGGRTML--PIRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQP 224
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
807-999 8.16e-22

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 96.96  E-value: 8.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLdNGTKLAVKKLtgdYGMMEKEFKAEVE----VLSRakHENL---VALQGYCVHDSAR-ILIYSF 878
Cdd:cd14056    1 KTIGKGRYGEVWLGKY-RGEKVAVKIF---SSRDEDSWFRETEiyqtVMLR--HENIlgfIAADIKSTGSWTQlWLITEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENpegpaQLDWPKRLNIMRGASSGLAYMH-QIC----EPHIVHRDIKSSNILLDGNFKAYVADFGLSrl 953
Cdd:cd14056   75 HEHGSLYDYLQRN-----TLDTEEALRLAYSAASGLAHLHtEIVgtqgKPAIAHRDLKSKNILVKRDGTCCIADLGLA-- 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  954 ILPYRTHVTTEL-----VGTLGYIPPE-------------YGQAwvatlrgDVYSFGVVMLELL 999
Cdd:cd14056  148 VRYDSDTNTIDIppnprVGTKRYMAPEvlddsinpksfesFKMA-------DIYSFGLVLWEIA 204
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
802-1010 1.02e-21

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: 95.89  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT-LDNGTKLAVKK--LTGDYGMMEKEFKA---EVEVLSRAKHENLVALQGyCVHDSARILI 875
Cdd:cd06625    1 NWKQGKLLGQGAFGQVYLCYdADTGRELAVKQveIDPINTEASKEVKAlecEIQLLKNLQHERIVQYYG-CLQDEKSLSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 Y-SFMENGSLdywlHENPEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd06625   80 FmEYMPGGSV----KDEIKAYGALTENVTRKYTRQILEGLAYLHSN---MIVHRDIKGANILRDSNGNVKLGDFGASKRL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  955 LPYRTHVTTELV-GTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRPMEVFRP 1010
Cdd:cd06625  153 QTICSSTGMKSVtGTPYWMSPEvingegYGR------KADIWSVGCTVVEMLTTKPPWAEFEP 209
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
809-1077 1.25e-21

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: 96.65  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTK------LAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd05093   13 LGEGAFGKVFLAECYNLCPeqdkilVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHEN-PEG--------PAQLDWPKRLNIMRGASSGLAYMhqiCEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd05093   93 DLNKFLRAHgPDAvlmaegnrPAELTQSQMLHIAQQIAAGMVYL---ASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  954 ILP---YRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELVAWVHTMKRDGK- 1028
Cdd:cd05093  170 VYStdyYRVGGHTML--PIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVLQRPRTc 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425 1029 PEEVFDTLLResgneeamlrvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05093  248 PKEVYDLMLG-----------------CWQREPHMRLNIKEIHSLLQNL 279
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
807-1069 1.33e-21

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: 95.69  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKA-TLDNGTKLAVKKLtgDYGMM-EKEFK---AEVEVLSRAKHENLValqGYC--VHDSARILIYSFM 879
Cdd:cd08217    6 ETIGKGSFGTVRKVrRKSDGKILVWKEI--DYGKMsEKEKQqlvSEVNILRELKHPNIV---RYYdrIVDRANTTLYIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 E---NGSLdywlhenpegpAQL-----------DWPKRLNIMRGASSGLAYMH--QICEPHIVHRDIKSSNILLDGNFKA 943
Cdd:cd08217   81 EyceGGDL-----------AQLikkckkenqyiPEEFIWKIFTQLLLALYECHnrSVGGGKILHRDLKPANIFLDSDNNV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  944 YVADFGLSRlILPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPmevFRPKMSRELVAWVhtm 1023
Cdd:cd08217  150 KLGDFGLAR-VLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPP---FQAANQLELAKKI--- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15218425 1024 kRDGKpeevFDTLlrESGNEEAMLRVLDiacMCVNQNPMKRPNIQQ 1069
Cdd:cd08217  223 -KEGK----FPRI--PSRYSSELNEVIK---SMLNVDPDKRPSVEE 258
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
807-1000 1.40e-21

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 96.66  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLDNgTKLAVKKLTG---DYGMMEKEFKAevevLSRAKHENLVALQGYCVHDSAR-----ILIYSF 878
Cdd:cd14054    1 QLIGQGRYGTVWKGSLDE-RPVAVKVFPArhrQNFQNEKDIYE----LPLMEHSNILRFIGADERPTADgrmeyLLVLEY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENpegpaQLDWPKRLNIMRGASSGLAYMHQ------ICEPHIVHRDIKSSNILLDGNFKAYVADFGLSr 952
Cdd:cd14054   76 APKGSLCSYLREN-----TLDWMSSCRMALSLTRGLAYLHTdlrrgdQYKPAIAHRDLNSRNVLVKADGSCVICDFGLA- 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  953 LILPYRTHVTTEL----------VGTLGYIPPEYGQAWV-------ATLRGDVYSFGVVMLELLT 1000
Cdd:cd14054  150 MVLRGSSLVRGRPgaaenasiseVGTLRYMAPEVLEGAVnlrdcesALKQVDVYALGLVLWEIAM 214
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
809-1070 1.62e-21

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: 95.15  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLdNGTkLAVKKL--TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARIlIYSFMENGSLDY 886
Cdd:cd14062    1 IGSGSFGTVYKGRW-HGD-VAVKKLnvTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAI-VTQWCEGSSLYK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLH--ENpegpaQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlilpyrthVTTE 964
Cdd:cd14062   78 HLHvlET-----KFEMLQLIDIARQTAQGMDYLHA---KNIIHRDLKSNNIFLHEDLTVKIGDFGLAT--------VKTR 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LVGTLGYIPPEYGQAWVA------------TLRGDVYSFGVVMLELLTGKRPMEvfrpkmsrelvawvHTMKRDGKPEEV 1032
Cdd:cd14062  142 WSGSQQFEQPTGSILWMApevirmqdenpySFQSDVYAFGIVLYELLTGQLPYS--------------HINNRDQILFMV 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15218425 1033 FDTLLR------ESGNEEAMLRVLDiacMCVNQNPMKRPNIQQV 1070
Cdd:cd14062  208 GRGYLRpdlskvRSDTPKALRRLME---DCIKFQRDERPLFPQI 248
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
807-1076 1.77e-21

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 95.56  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKAT----LDNG---TKLAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd05044    1 KFLGSGAFGEVFEGTakdiLGDGsgeTKVAVKTLRKGATDQEKaEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHEN-PE--GPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL---DGNFKAY-VADFGLS 951
Cdd:cd05044   81 MEGGDLLSYLRAArPTafTPPLLTLKDLLSICVDVAKGCVYLEDM---HFVHRDLAARNCLVsskDYRERVVkIGDFGLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  952 RLI-------------LPYRthvttelvgtlgYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELV 1017
Cdd:cd05044  158 RDIykndyyrkegeglLPVR------------WMAPESLVDGVFTTQSDVWAFGVLMWEILTlGQQP---YPARNNLEVL 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425 1018 AWVHTMKRDGKPEEVFDTLLresgneEAMLRvldiacmCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd05044  223 HFVRAGGRLDQPDNCPDDLY------ELMLR-------CWSTDPEERPSFARILEQLQN 268
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
809-1004 2.58e-21

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: 94.93  E-value: 2.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVK---------------KLTGDYGMMEKeFKAEVEVLSRAKHENLVALqgYCVHDSAR 872
Cdd:cd14008    1 LGRGSFGKVKLALdTETGQLYAIKifnksrlrkrregknDRGKIKNALDD-VRREIAIMKKLDHPNIVRL--YEVIDDPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 I----LIYSFMENGSLDYWlhENPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADF 948
Cdd:cd14008   78 SdklyLVLEYCEGGPVMEL--DSGDRVPPLPEETARKYFRDLVLGLEYLH---ENGIVHRDIKPENLLLTADGTVKISDF 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  949 GLSRlILPYRTHVTTELVGTLGYIPPEYGQAWVATLRG---DVYSFGVVMLELLTGKRP 1004
Cdd:cd14008  153 GVSE-MFEDGNDTLQKTAGTPAFLAPELCDGDSKTYSGkaaDIWALGVTLYCLVFGRLP 210
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
808-1004 2.74e-21

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: 94.60  E-value: 2.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAtLDNGTKLAVK----KLtGDYGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSAR--ILIYSFME 880
Cdd:cd13983    8 VLGRGSFKTVYRA-FDTEEGIEVAwneiKL-RKLPKAERQrFKQEIEILKSLKHPNIIKFYDSWESKSKKevIFITELMT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWL--HENPEGPAQLDWPKRlnIMRGassgLAYMHQiCEPHIVHRDIKSSNILLDGN---FKayVADFGLSRLIl 955
Cdd:cd13983   86 SGTLKQYLkrFKRLKLKVIKSWCRQ--ILEG----LNYLHT-RDPPIIHRDLKCDNIFINGNtgeVK--IGDLGLATLL- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425  956 pyRTHVTTELVGTLGYIPPE-----YGQawvatlRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd13983  156 --RQSFAKSVIGTPEFMAPEmyeehYDE------KVDIYAFGMCLLEMATGEYP 201
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
809-1074 2.76e-21

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: 94.56  E-value: 2.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT---LDNGTKLAVK-----KLTGDYgmMEKEFKAEVEVLSRAKHENLValqgyCVHDsarIL-----I 875
Cdd:cd14080    8 IGEGSYSKVKLAEytkSGLKEKVACKiidkkKAPKDF--LEKFLPRELEILRKLRHPNII-----QVYS---IFergskV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFM---ENGSLDYWLHEN---PEGPAQLdwpkrlnIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd14080   78 FIFMeyaEHGDLLEYIQKRgalSESQARI-------WFRQLALAVQYLHSLD---IAHRDLKCENILLDSNNNVKLSDFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  950 LSRLILPYRTHVTTE-LVGTLGYIPPEygqawvaTLRG--------DVYSFGVVMLELLTGKRPMEVFRPKmsrelvawv 1020
Cdd:cd14080  148 FARLCPDDDGDVLSKtFCGSAAYAAPE-------ILQGipydpkkyDIWSLGVILYIMLCGSMPFDDSNIK--------- 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425 1021 hTMKRDGKPEEVFDTLLRESGNEEAMLRVLDIacmcVNQNPMKRPNIQQVV--DWL 1074
Cdd:cd14080  212 -KMLKDQQNRKVRFPSSVKKLSPECKDLIDQL----LEPDPTKRATIEEILnhPWL 262
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
809-1077 2.77e-21

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: 94.95  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGdyGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARIlIYSFMENGSLDYW 887
Cdd:cd05067   15 LGAGQFGEVWMGYYNGHTKVAIKSLKQ--GSMSPDaFLAEANLMKQLQHQRLVRLYAVVTQEPIYI-ITEYMENGSLVDF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LhENPEGpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIlpyrthVTTELVG 967
Cdd:cd05067   92 L-KTPSG-IKLTINKLLDMAAQIAEGMAFIEE---RNYIHRDLRAANILVSDTLSCKIADFGLARLI------EDNEYTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  968 TLG------YIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFR-PKMSRELVAWVHTMKRDGKPEEVFDTLLRe 1039
Cdd:cd05067  161 REGakfpikWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTnPEVIQNLERGYRMPRPDNCPEELYQLMRL- 239
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15218425 1040 sgneeamlrvldiacmCVNQNPMKRPNIqqvvDWLKNI 1077
Cdd:cd05067  240 ----------------CWKERPEDRPTF----EYLRSV 257
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
807-1069 3.47e-21

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: 94.73  E-value: 3.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKA-TLDNGTKLAVKKLTgdygmMEK------EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFM 879
Cdd:cd06610    7 EVIGSGATAVVYAAyCLPKKEKVAIKRID-----LEKcqtsmdELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGS-LDYWLHENPEGpaQLDWPKRLNIMRGASSGLAYMHQicEPHIvHRDIKSSNILLDGNFKAYVADFGLSRLILPY- 957
Cdd:cd06610   82 SGGSlLDIMKSSYPRG--GLDEAIIATVLKEVLKGLEYLHS--NGQI-HRDVKAGNILLGEDGSVKIADFGVSASLATGg 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  958 -RTH-VTTELVGTLGYIPPE-------YGQawvatlRGDVYSFGVVMLELLTGK------RPMEVFrpkmsrelvawVHT 1022
Cdd:cd06610  157 dRTRkVRKTFVGTPCWMAPEvmeqvrgYDF------KADIWSFGITAIELATGAapyskyPPMKVL-----------MLT 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425 1023 MKRD------GKPEEVFDTLLREsgneeaMLRvldiacMCVNQNPMKRPNIQQ 1069
Cdd:cd06610  220 LQNDppsletGADYKKYSKSFRK------MIS------LCLQKDPSKRPTAEE 260
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
809-1004 3.99e-21

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: 94.75  E-value: 3.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL------DNGTKLAVKKLTGDYGM-MEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd05048   13 LGEGAFGKVYKGELlgpsseESAISVAIKTLKENASPkTQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYMAH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWL-----HENP-------EGPAQLDWPKRLNIMRGASSGLAYM--HqicepHIVHRDIKSSNILLDGNFKAYVAD 947
Cdd:cd05048   93 GDLHEFLvrhspHSDVgvssdddGTASSLDQSDFLHIAIQIAAGMEYLssH-----HYVHRDLAARNCLVGDGLTVKISD 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  948 FGLSRLILP---YRTHVTTELvgTLGYIPPE---YGQawvATLRGDVYSFGVVMLELLT-GKRP 1004
Cdd:cd05048  168 FGLSRDIYSsdyYRVQSKSLL--PVRWMPPEailYGK---FTTESDVWSFGVVLWEIFSyGLQP 226
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
809-1077 4.06e-21

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 94.50  E-value: 4.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14154    1 LGKGFFGQAIKVThRETGEVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEgpaQLDWPKRLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTEL-- 965
Cdd:cd14154   81 LKDMAR---PLPWAQRVRFAKDIASGMAYLHSMN---IIHRDLNSHNCLVREDKTVVVADFGLARLIVEERLPSGNMSps 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  966 -----------------VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKmsrelvawvhtmKRD-G 1027
Cdd:cd14154  155 etlrhlkspdrkkrytvVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEADPDYLPR------------TKDfG 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425 1028 KPEEVFdtllRESGNEEAMLRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14154  223 LNVDSF----REKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
808-1074 4.57e-21

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 94.34  E-value: 4.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNgtKLAVKKLTGDYGMMEK--EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd14063    7 VIGKGRFGRVHRGRWHG--DVAIKLLNIDYLNEEQleAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCKGRTLY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNfKAYVADFGL---SRLILPYRTHVT 962
Cdd:cd14063   85 SLIHERKE---KFDFNKTVQIAQQICQGMGYLHA---KGIIHKDLKSKNIFLENG-RVVITDFGLfslSGLLQPGRREDT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  963 TELV-GTLGYIPPEYGQAWVATLR----------GDVYSFGVVMLELLTGKRPmevFRpKMSRELVAWvhtMKRDGKPEe 1031
Cdd:cd14063  158 LVIPnGWLCYLAPEIIRALSPDLDfeeslpftkaSDVYAFGTVWYELLAGRWP---FK-EQPAESIIW---QVGCGKKQ- 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 15218425 1032 vfdTLLRESGNEEamlrVLDIACMCVNQNPMKRPNIQQVVDWL 1074
Cdd:cd14063  230 ---SLSQLDIGRE----VKDILMQCWAYDPEKRPTFSDLLRML 265
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
809-1070 5.34e-21

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 94.69  E-value: 5.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN--GTK----LAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd05094   13 LGEGAFGKVFLAECYNlsPTKdkmlVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMKHG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENpeGP--------------AQLDWPKRLNIMRGASSGLAYMhqiCEPHIVHRDIKSSNILLDGNFKAYVADF 948
Cdd:cd05094   93 DLNKFLRAH--GPdamilvdgqprqakGELGLSQMLHIATQIASGMVYL---ASQHFVHRDLATRNCLVGANLLVKIGDF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  949 GLSRLILP---YRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELVAWVHTMK 1024
Cdd:cd05094  168 GMSRDVYStdyYRVGGHTML--PIRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPWFQLSNTEVIECITQGRVLE 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425 1025 RDGK-PEEVFDTLLResgneeamlrvldiacmCVNQNPMKRPNIQQV 1070
Cdd:cd05094  246 RPRVcPKEVYDIMLG-----------------CWQREPQQRLNIKEI 275
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
809-1076 5.84e-21

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: 93.98  E-value: 5.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGdyGMMEKE-FKAEVEVLSRAKHENLVALqgYCVHDSARILIYS-FMENGSLDY 886
Cdd:cd05070   17 LGNGQFGEVWMGTWNGNTKVAIKTLKP--GTMSPEsFLEEAQIMKKLKHDKLVQL--YAVVSEEPIYIVTeYMSKGSLLD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENpEGPAqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELV 966
Cdd:cd05070   93 FLKDG-EGRA-LKLPNLVDMAAQVAAGMAYIERM---NYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  967 GTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRpmeVFRPKM-SRELVAWVHTMKRDGKPEEVFDTLlresgnEEA 1045
Cdd:cd05070  168 FPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR---VPYPGMnNREVLEQVERGYRMPCPQDCPISL------HEL 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 15218425 1046 MLRvldiacmCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd05070  239 MIH-------CWKKDPEERPTFEYLQGFLED 262
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
809-1071 6.52e-21

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: 93.41  E-value: 6.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKkLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL 888
Cdd:cd05113   12 LGTGQFGVVKYGKWRGQYDVAIK-MIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENPEG--PAQLdwpkrLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL--PYRTHVTTE 964
Cdd:cd05113   91 REMRKRfqTQQL-----LEMCKDVCEAMEYLES---KQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLddEYTSSVGSK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELVAWVHTMKRDGKPEEvfdtllresgne 1043
Cdd:cd05113  163 F--PVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQGLRLYRPHLASE------------ 228
                        250       260
                 ....*....|....*....|....*...
gi 15218425 1044 eamlRVLDIACMCVNQNPMKRPNIQQVV 1071
Cdd:cd05113  229 ----KVYTIMYSCWHEKADERPTFKILL 252
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
809-1065 7.43e-21

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 94.13  E-value: 7.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL------DNGTKLAVKKLTGDYGM-MEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd05050   13 IGQGAFGRVFQARApgllpyEPFTMVAVKMLKEEASAdMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYMAY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHEN------------------PEGPAQLDWPKRLNIMRGASSGLAYMhqiCEPHIVHRDIKSSNILLDGNFKA 943
Cdd:cd05050   93 GDLNEFLRHRspraqcslshstssarkcGLNPLPLSCTEQLCIAKQVAAGMAYL---SERKFVHRDLATRNCLVGENMVV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  944 YVADFGLSRLILP--YRTHVTTELVgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWV 1020
Cdd:cd05050  170 KIADFGLSRNIYSadYYKASENDAI-PIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQP---YYGMAHEEVIYYV 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425 1021 htmkRDGK--------PEEVFDtLLResgneeamlrvldiacMCVNQNPMKRP 1065
Cdd:cd05050  246 ----RDGNvlscpdncPLELYN-LMR----------------LCWSKLPSDRP 277
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
809-1076 9.63e-21

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: 93.60  E-value: 9.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDyGMMEKEFKAEVEVLSRAKHENLVALQGyCVHDSARILIYSFMENGSLDYWL 888
Cdd:cd05069   20 LGQGCFGEVWMGTWNGTTKVAIKTLKPG-TMMPEAFLQEAQIMKKLRHDKLVPLYA-VVSEEPIYIVTEFMGKGSLLDFL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENpEGpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVGT 968
Cdd:cd05069   98 KEG-DG-KYLKLPQLVDMAAQIADGMAYIERM---NYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  969 LGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRpmeVFRPKM-SRELVAWVHTMKRDGKPEevfdtllresGNEEAML 1047
Cdd:cd05069  173 IKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR---VPYPGMvNREVLEQVERGYRMPCPQ----------GCPESLH 239
                        250       260
                 ....*....|....*....|....*....
gi 15218425 1048 RVLDiacMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd05069  240 ELMK---LCWKKDPDERPTFEYIQSFLED 265
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
809-1077 1.20e-20

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: 92.80  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL--DNGT--KLAVKKLT-GDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSArILIYSFMENGS 883
Cdd:cd05060    3 LGHGNFGSVRKGVYlmKSGKevEVAVKTLKqEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEPL-MLVMELAPLGP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENPEGPAQldwpKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTT 963
Cdd:cd05060   82 LLKYLKKRREIPVS----DLKELAHQVAMGMAYLE---SKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  964 ELVGT--LGYIPPE---YGQawvATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKRDGKPEEVFDTll 1037
Cdd:cd05060  155 TTAGRwpLKWYAPEcinYGK---FSSKSDVWSYGVTLWEAFSyGAKP---YGEMKGPEVIAMLESGERLPRPEECPQE-- 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 15218425 1038 resgneeamlrVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05060  227 -----------IYSIMLSCWKYRPEDRPTFSELESTFRRD 255
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
801-1006 1.30e-20

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: 92.62  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKAT-----LDNGTKLAVKKLTGDYGMMEKeFKAEVEVLSRAKHENLVALQGYCVHDSARILI 875
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYRARslhtgLEVAIKMIDKKAMQKAGMVQR-VRNEVEIHCQLKHPSILELYNYFEDSNYVYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLhENPEGPAQLDWPKrlNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGL-SRLI 954
Cdd:cd14186   80 LEMCHNGEMSRYL-KNRKKPFTEDEAR--HFMHQIVTGMLYLHS---HGILHRDLTLSNLLLTRNMNIKIADFGLaTQLK 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  955 LPYRTHVTteLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14186  154 MPHEKHFT--MCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFD 203
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
809-1070 1.39e-20

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 93.16  E-value: 1.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLV----YKATLDN-GTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSAR--ILIYSFMEN 881
Cdd:cd14205   12 LGKGNFGSVemcrYDPLQDNtGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRnlRLIMEYLPY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMhqiCEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHV 961
Cdd:cd14205   92 GSLRDYLQKHKE---RIDHIKLLQYTSQICKGMEYL---GTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  962 TTELVGT--LGYIPPEYGQAWVATLRGDVYSFGVVMLELLT----GKRPMEVFRPKMSRE------LVAWVHTMKRDGKp 1029
Cdd:cd14205  166 KVKEPGEspIFWYAPESLTESKFSVASDVWSFGVVLYELFTyiekSKSPPAEFMRMIGNDkqgqmiVFHLIELLKNNGR- 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 15218425 1030 eevfdtLLRESGNEEAMLRVLDiacMCVNQNPMKRPNIQQV 1070
Cdd:cd14205  245 ------LPRPDGCPDEIYMIMT---ECWNNNVNQRPSFRDL 276
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
808-1004 1.98e-20

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


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 92.40  E-value: 1.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLdNGTKLAVKKLTGD----YGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd14147   10 VIGIGGFGKVYRGSW-RGELVAVKAARQDpdedISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENPEGPAQL-DWPKRLnimrgaSSGLAYMHQICEPHIVHRDIKSSNILLDGNFKA--------YVADFGLSRli 954
Cdd:cd14147   89 LSRALAGRRVPPHVLvNWAVQI------ARGMHYLHCEALVPVIHRDLKSNNILLLQPIENddmehktlKITDFGLAR-- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  955 lpyRTHVTTEL--VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14147  161 ---EWHKTTQMsaAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVP 209
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
801-1081 2.66e-20

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 92.49  E-value: 2.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKK--LTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCV--HDSARILIY 876
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKtiTTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLdeQDSSIGIAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLS-RLIl 955
Cdd:cd06621   81 EYCEGGSLDSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLH---SRKIIHRDIKPSNILLTRKGQVKLCDFGVSgELV- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 pyrTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPM--EVFRPKMSRELVAWVHTMKrdgKPEevf 1033
Cdd:cd06621  157 ---NSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFppEGEPPLGPIELLSYIVNMP---NPE--- 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425 1034 dtLLRESGNEEAMLRVL-DIACMCVNQNPMKRPNIQQVV--DWLKNIEAEK 1081
Cdd:cd06621  228 --LKDEPENGIKWSESFkDFIEKCLEKDGTRRPGPWQMLahPWIKAQEKKK 276
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
802-1002 3.50e-20

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: 92.82  E-value: 3.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTgdygmMEKEFKA-------EVEVLSRAKHENLVALQ---------- 863
Cdd:cd07845    8 EFEKLNRIGEGTYGIVYRArDTTSGEIVALKKVR-----MDNERDGipisslrEITLLLNLRHPNIVELKevvvgkhlds 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  864 -----GYCVHDSARILiysfmENGSldywlheNPEGPAQLDwpkrlNIMRGASSGLAYMHQICephIVHRDIKSSNILLD 938
Cdd:cd07845   83 iflvmEYCEQDLASLL-----DNMP-------TPFSESQVK-----CLMLQLLRGLQYLHENF---IIHRDLKVSNLLLT 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  939 GNFKAYVADFGLSRLILPYRTHVTTELVgTLGYIPPE--YGqAWVATLRGDVYSFGVVMLELLTGK 1002
Cdd:cd07845  143 DKGCLKIADFGLARTYGLPAKPMTPKVV-TLWYRAPEllLG-CTTYTTAIDMWAVGCILAELLAHK 206
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
801-1069 3.78e-20

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: 91.12  E-value: 3.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQaniIGCGGFGLVYKATlDNGT--KLAVKKLTGDYGMMEKEFKaEVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd06614    3 KNLEK---IGEGASGEVYKAT-DRATgkEVAIKKMRLRKQNKELIIN-EILIMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENPegpaqldwpKRLN------IMRGASSGLAYMHQIcepHIVHRDIKSSNILL--DGNFKayVADFGL 950
Cdd:cd06614   78 MDGGSLTDIITQNP---------VRMNesqiayVCREVLQGLEYLHSQ---NVIHRDIKSDNILLskDGSVK--LADFGF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  951 SRLILPYRTHVTTeLVGTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVA--WVHT 1022
Cdd:cd06614  144 AAQLTKEKSKRNS-VVGTPYWMAPEvikrkdYGP------KVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITtkGIPP 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425 1023 MkrdgKPEEVFDTLLREsgneeamlrVLDiacMCVNQNPMKRPNIQQ 1069
Cdd:cd06614  217 L----KNPEKWSPEFKD---------FLN---KCLVKDPEKRPSAEE 247
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
809-1075 7.87e-20

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: 90.20  E-value: 7.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL-DNGTKLAVK----KLTGDygmMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd05041    3 IGRGNFGDVYRGVLkPDNTEVAVKtcreTLPPD---LKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENPegpAQLDWPKRLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFGLSRlilpYRTHVTT 963
Cdd:cd05041   80 LLTFLRKKG---ARLTVKQLLQMCLDAAAGMEYLESKN---CIHRDLAARNCLVGENNVLKISDFGMSR----EEEDGEY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  964 ELVGTLGYIP-----PE---YGQawvATLRGDVYSFGVVMLELLT-GKRPMevfrPKMS----RELVAWVHTMKR-DGKP 1029
Cdd:cd05041  150 TVSDGLKQIPikwtaPEalnYGR---YTSESDVWSFGILLWEIFSlGATPY----PGMSnqqtREQIESGYRMPApELCP 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15218425 1030 EEVFDTLLResgneeamlrvldiacmCVNQNPMKRPNIQQVVDWLK 1075
Cdd:cd05041  223 EAVYRLMLQ-----------------CWAYDPENRPSFSEIYNELQ 251
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
809-1004 1.30e-19

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: 90.08  E-value: 1.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARIlIYSFMENGSLDYWL 888
Cdd:cd14150    8 IGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAI-ITQWCEGSSLYRHL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HenpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlilpyrthVTTELVGT 968
Cdd:cd14150   87 H---VTETRFDTMQLIDVARQTAQGMDYLHA---KNIIHRDLKSNNIFLHEGLTVKIGDFGLAT--------VKTRWSGS 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425  969 LGYIPPEYGQAWVA------------TLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14150  153 QQVEQPSGSILWMApevirmqdtnpySFQSDVYAYGVVLYELMSGTLP 200
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
809-1004 1.31e-19

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: 90.12  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARIlIYSFMENGSLDYWL 888
Cdd:cd14151   16 IGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAI-VTQWCEGSSLYHHL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENpegPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYR-THVTTELVG 967
Cdd:cd14151   95 HII---ETKFEMIKLIDIARQTAQGMDYLHA---KSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSgSHQFEQLSG 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15218425  968 TLGYIPPEYGQAWVA---TLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14151  169 SILWMAPEVIRMQDKnpySFQSDVYAFGIVLYELMTGQLP 208
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
808-1077 2.71e-19

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 89.13  E-value: 2.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATL--DNGT--KLAVK--KLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSAR------ILI 875
Cdd:cd05035    6 ILGEGEFGSVMEAQLkqDDGSqlKVAVKtmKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppspMVI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWL--HENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd05035   86 LPFMKHGDLHSYLlySRLGGLPEKLPLQTLLKFMVDIAKGMEYLSN---RNFIHRDLAARNCMLDENMTVCVADFGLSRK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  954 ILP---YR-THVTTELVgtlGYIPPEYGQAWVATLRGDVYSFGVVMLELLTgkRPMEVFRPKMSRELVAWVHTMKRDGKP 1029
Cdd:cd05035  163 IYSgdyYRqGRISKMPV---KWIALESLADNVYTSKSDVWSFGVTMWEIAT--RGQTPYPGVENHEIYDYLRNGNRLKQP 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425 1030 EEVFDtllresgneeamlRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05035  238 EDCLD-------------EVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
809-1077 3.19e-19

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: 88.63  E-value: 3.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTK-LAVKKLTGDyGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd05052   14 LGGGQYGEVYEGVWKKYNLtVAVKTLKED-TMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENpeGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL--PYRTHVTTEL 965
Cdd:cd05052   93 LREC--NREELNAVVLLYMATQIASAMEYLE---KKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTgdTYTAHAGAKF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  966 vgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELVAWVHTMKR-DGKPEEVFDTLLResgne 1043
Cdd:cd05052  168 --PIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYELLEKGYRMERpEGCPPKVYELMRA----- 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15218425 1044 eamlrvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05052  241 ------------CWQWNPSDRPSFAEIHQALETM 262
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
809-999 4.24e-19

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 88.46  E-value: 4.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLD-NGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14222    1 LGKGFFGQAIKVTHKaTGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEGPaqldWPKRLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTE--- 964
Cdd:cd14222   81 LRADDPFP----WQQKVSFAKGIASGMAYLHSMS---IIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPPPDkpt 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  965 ----------------LVGTLGYIPPEY--GQAWVATLrgDVYSFGVVMLELL 999
Cdd:cd14222  154 tkkrtlrkndrkkrytVVGNPYWMAPEMlnGKSYDEKV--DIFSFGIVLCEII 204
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
809-1005 5.17e-19

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: 88.53  E-value: 5.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTGDYG--MMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd07833    9 VGEGAYGVVLKCrNKATGEIVAIKKFKESEDdeDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVERTLLE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YwLHENPEGpaqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLI-----LPYRTH 960
Cdd:cd07833   89 L-LEASPGG---LPPDAVRSYIWQLLQAIAYCHSH---NIIHRDIKPENILVSESGVLKLCDFGFARALtarpaSPLTDY 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  961 VTTE-------LVGtlgyiPPEYGQAwvatlrGDVYSFGVVMLELLTGkRPM 1005
Cdd:cd07833  162 VATRwyrapelLVG-----DTNYGKP------VDVWAIGCIMAELLDG-EPL 201
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
809-1071 5.28e-19

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: 88.13  E-value: 5.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN---GTKLAVKKLTGDYG-MMEKEFKA----EVEVLSRAKHENLVALQGYCVHDSARILIysFME 880
Cdd:cd13994    1 IGKGATSVVRIVTKKNprsGVLYAVKEYRRRDDeSKRKDYVKrltsEYIISSKLHHPNIVKVLDLCQDLHGKWCL--VME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 ---NGSLdYWLHENPEGPAQLD---WPKRlnIMRGassgLAYMHQicepH-IVHRDIKSSNILLD--GNFKayVADFGLS 951
Cdd:cd13994   79 ycpGGDL-FTLIEKADSLSLEEkdcFFKQ--ILRG----VAYLHS----HgIAHRDLKPENILLDedGVLK--LTDFGTA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  952 ---RLILPYRTHVTTELVGTLGYIPPE-YGQAWVATLRGDVYSFGVVMLELLTGKRPMEVfrPKMSRElvAWVHTMKRDG 1027
Cdd:cd13994  146 evfGMPAEKESPMSAGLCGSEPYMAPEvFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRS--AKKSDS--AYKAYEKSGD 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15218425 1028 KPEEVFDTLLRESGNEEAMLrvldIACMcVNQNPMKRPNIQQVV 1071
Cdd:cd13994  222 FTNGPYEPIENLLPSECRRL----IYRM-LHPDPEKRITIDEAL 260
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
808-1004 5.43e-19

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: 88.26  E-value: 5.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVKKLT------GDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFME 880
Cdd:cd06630    7 LLGTGAFSSCYQARdVKTGTLMAVKQVSfcrnssSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHEnpEGPAQLDWPKR--LNIMRGassgLAYMHqicEPHIVHRDIKSSNILLDGN-FKAYVADFG-LSRLilp 956
Cdd:cd06630   87 GGSVASLLSK--YGAFSENVIINytLQILRG----LAYLH---DNQIIHRDLKGANLLVDSTgQRLRIADFGaAARL--- 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  957 yRTHVTT------ELVGTLGYIPPEygqawvaTLRG-------DVYSFGVVMLELLTGKRP 1004
Cdd:cd06630  155 -ASKGTGagefqgQLLGTIAFMAPE-------VLRGeqygrscDVWSVGCVIIEMATAKPP 207
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
809-1074 6.21e-19

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: 87.77  E-value: 6.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN-GTKLAVKK--LTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL- 884
Cdd:cd14069    9 LGEGAFGEVFLAVNRNtEEAVAVKFvdMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGELf 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 -----DYWLhenPEGPAQLDWPKRLnimrgasSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGL-SRLILPYR 958
Cdd:cd14069   89 dkiepDVGM---PEDVAQFYFQQLM-------AGLKYLHSC---GITHRDIKPENLLLDENDNLKISDFGLaTVFRYKGK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  959 THVTTELVGTLGYIPPE--YGQAWVATlRGDVYSFGVVMLELLTGKRPMEvfRPK-MSRELVAWVHTMKRDGKPEEVFDT 1035
Cdd:cd14069  156 ERLLNKMCGTLPYVAPEllAKKKYRAE-PVDVWSCGIVLFAMLAGELPWD--QPSdSCQEYSDWKENKKTYLTPWKKIDT 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 15218425 1036 llresgneeamlRVLDIACMCVNQNPMKRPNIQQVVD--WL 1074
Cdd:cd14069  233 ------------AALSLLRKILTENPNKRITIEDIKKhpWY 261
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
802-1026 6.72e-19

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: 87.70  E-value: 6.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKATL-DNGTKLAVKkltgdYGMMEK--EFKA------EVEVLSRAKHENLVALQgYCVHDSAR 872
Cdd:cd05578    1 HFQILRVIGKGSFGKVCIVQKkDTKKMFAMK-----YMNKQKciEKDSvrnvlnELEILQELEHPFLVNLW-YSFQDEED 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 I-LIYSFMENGSLDYWLHENP---EGPAQLdwpkrlnIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADF 948
Cdd:cd05578   75 MyMVVDLLLGGDLRYHLQQKVkfsEETVKF-------YICEIVLALDYLH---SKNIIHRDIKPDNILLDEQGHVHITDF 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  949 GLSRlILPYRThVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAWVHTMKRD 1026
Cdd:cd05578  145 NIAT-KLTDGT-LATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVL 220
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
809-1004 7.05e-19

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: 87.74  E-value: 7.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN-GTKLAVK-----KLTGDYgmMEKEFKAEVEVLSRAKHENLVALqgY-CVHDSARI-LIYSFME 880
Cdd:cd14162    8 LGHGSYAVVKKAYSTKhKCKVAIKivskkKAPEDY--LQKFLPREIEVIKGLKHPNLICF--YeAIETTSRVyIIMELAE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHEN---PEGPAQLdWPKRLnimrgaSSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL-- 955
Cdd:cd14162   84 NGDLLDYIRKNgalPEPQARR-WFRQL------VAGVEYCH---SKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMkt 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  956 -PYRTHVTTELVGTLGYIPPEY--GQAWVATLrGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14162  154 kDGKPKLSETYCGSYAYASPEIlrGIPYDPFL-SDIWSMGVVLYTMVYGRLP 204
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
788-1077 1.05e-18

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 87.67  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  788 VKDLTIFELLkatdnFSQANIIGCGGFGLVYKATL----DNGTKLAVKKLTGDYGMME--KEFKAEVEVLSRAKHENLVA 861
Cdd:cd05074    1 LKDVLIQEQQ-----FTLGRMLGKGEFGSVREAQLksedGSFQKVAVKMLKADIFSSSdiEEFLREAACMKEFDHPNVIK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  862 LQGYCVHDSAR------ILIYSFMENGSLDYWLHENP--EGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSS 933
Cdd:cd05074   76 LIGVSLRSRAKgrlpipMVILPFMKHGDLHTFLLMSRigEEPFTLPLQTLVRFMIDIASGMEYLSS---KNFIHRDLAAR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  934 NILLDGNFKAYVADFGLSRLILP---YRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfr 1009
Cdd:cd05074  153 NCMLNENMTVCVADFGLSKKIYSgdyYRQGCASKL--PVKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPY---- 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425 1010 pkmsrelvAWVHTmkrdgkpEEVFDTLLreSGNE-----EAMLRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05074  227 --------AGVEN-------SEIYNYLI--KGNRlkqppDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
808-1075 1.27e-18

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: 87.56  E-value: 1.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATL-DNGTKLAVKKLTGDygmmeKEFKA-EVEVLSRAKHENLVALQGYCvhdsariliYSFMENGSLD 885
Cdd:cd14137   11 VIGSGSFGVVYQAKLlETGEVVAIKKVLQD-----KRYKNrELQIMRRLKHPNIVKLKYFF---------YSSGEKKDEV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YwlhEN------PEGPAQL--DWPKRLNIMRGAS---------SGLAYMHQICephIVHRDIKSSNILLD---GNFKayV 945
Cdd:cd14137   77 Y---LNlvmeymPETLYRVirHYSKNKQTIPIIYvklysyqlfRGLAYLHSLG---ICHRDIKPQNLLVDpetGVLK--L 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  946 ADFGLSRLILPYRTHVTtelvgtlgYI------PPE-------YGQAWvatlrgDVYSFGVVMLELLTGKrPMevFRPKM 1012
Cdd:cd14137  149 CDFGSAKRLVPGEPNVS--------YIcsryyrAPElifgatdYTTAI------DIWSAGCVLAELLLGQ-PL--FPGES 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425 1013 SRE-LVAWVHTMkrdGKPeevfdtllresgNEEamlrvlDIACMCVNQNPMKRPNIQQvVDWLK 1075
Cdd:cd14137  212 SVDqLVEIIKVL---GTP------------TRE------QIKAMNPNYTEFKFPQIKP-HPWEK 253
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
801-1075 1.34e-18

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: 87.06  E-value: 1.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGT------KLAVKKLTGDYGMM-EKEFKAEVEVLSRAKHENLVALQGYCVHDSARI 873
Cdd:cd05036    6 KNLTLIRALGQGAFGEVYEGTVSGMPgdpsplQVAVKTLPELCSEQdEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 LIYSFMENGSLDYWLHEN---PEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL---DGNFKAYVAD 947
Cdd:cd05036   86 ILLELMAGGDLKSFLRENrprPEQPSSLTMLDLLQLAQDVAKGCRYLE---ENHFIHRDIAARNCLLtckGPGRVAKIGD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  948 FGLSRLILP---YRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTM 1023
Cdd:cd05036  163 FGMARDIYRadyYRKGGKAML--PVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMP---YPGKSNQEVMEFVTSG 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425 1024 KRDGKPEEVFDTLLResgneeamlrvldIACMCVNQNPMKRPNIQQVVDWLK 1075
Cdd:cd05036  238 GRMDPPKNCPGPVYR-------------IMTQCWQHIPEDRPNFSTILERLN 276
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
809-1080 1.51e-18

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 86.38  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVK--KLTGDYGMMEKEfkaeVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd14155    1 IGSGFFSEVYKVRhRTSGQVMALKmnTLSSNRANMLRE----VQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHENpegpAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL---DGNFKAYVADFGLSRLILPYRTHVT 962
Cdd:cd14155   77 QLLDSN----EPLSWTVRVKLALDIARGLSYLH---SKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKIPDYSDGKE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  963 T-ELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSR---ELVAWVHtMKRDGKPEevfdtllr 1038
Cdd:cd14155  150 KlAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDfglDYDAFQH-MVGDCPPD-------- 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 15218425 1039 esgneeamlrVLDIACMCVNQNPMKRPNIQQVVDWLKNIEAE 1080
Cdd:cd14155  221 ----------FLQLAFNCCNMDPKSRPSFHDIVKTLEEILEK 252
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
809-1004 1.60e-18

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: 87.01  E-value: 1.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARIlIYSFMENGSLDYWL 888
Cdd:cd14149   20 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAI-VTQWCEGSSLYKHL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENPegpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYR-THVTTELVG 967
Cdd:cd14149   99 HVQE---TKFQMFQLIDIARQTAQGMDYLHA---KNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSgSQQVEQPTG 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15218425  968 TLGYIPPEYGQAW---VATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14149  173 SILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELP 212
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
803-1004 1.73e-18

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: 86.76  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT-LDNGTKLAVK-----KLTGDYGMMEKeFKAEVEVLSRAKHENLVALQGYCVHDSARILIY 876
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVeVETGKMRAIKqivkrKVAGNDKNLQL-FQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHENPEGPAQLDWPKRLNIMRgassGLAYMHQIcepHIVHRDIKSSNILL--DGNFKAYVADFGLSRLI 954
Cdd:cd14098   81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILE----AMAYTHSM---GITHRDLKPENILItqDDPVIVKISDFGLAKVI 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  955 lpyrtHVTTEL---VGTLGYIPPEYGQAWVATLRG------DVYSFGVVMLELLTGKRP 1004
Cdd:cd14098  154 -----HTGTFLvtfCGTMAYLAPEILMSKEQNLQGgysnlvDMWSVGCLVYVMLTGALP 207
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
847-1071 1.76e-18

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 86.68  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  847 EVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWLhENPEGPaqLDWPKRLNIMRGASSGLAYMHQicEPHIV 926
Cdd:cd13992   46 ELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVL-LNREIK--MDWMFKSSFIKDIVKGMNYLHS--SSIGY 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  927 HRDIKSSNILLDGNFKAYVADFGLSRLIlpyRTHVTTELVGT-----LGYIPPE----YGQAWVATLRGDVYSFGVVMLE 997
Cdd:cd13992  121 HGRLKSSNCLVDSRWVVKLTDFGLRNLL---EEQTNHQLDEDaqhkkLLWTAPEllrgSLLEVRGTQKGDVYSFAIILYE 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  998 LLTGKRPMEVFRPKMSRELVawvhtmKRDGKPEEVFDTLLREsgnEEAMLRVLDIACMCVNQNPMKRPNIQQVV 1071
Cdd:cd13992  198 ILFRSDPFALEREVAIVEKV------ISGGNKPFRPELAVLL---DEFPPRLVLLVKQCWAENPEKRPSFKQIK 262
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
783-1004 1.88e-18

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 90.24  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   783 NSRYEVKDLtifellkatdnfsqaniIGCGGFGLVYKAtLDN--GTKLAVKKLTGDY----GMMEKeFKAEVEVLSRAKH 856
Cdd:NF033483    6 GGRYEIGER-----------------IGRGGMAEVYLA-KDTrlDRDVAVKVLRPDLardpEFVAR-FRREAQSAASLSH 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   857 ENLVAlqgycvhdsarilIYSFMENGSLDY-------------WLHENpeGPaqLDWPKRLNIMRGASSGLAYMHQiceP 923
Cdd:NF033483   67 PNIVS-------------VYDVGEDGGIPYivmeyvdgrtlkdYIREH--GP--LSPEEAVEIMIQILSALEHAHR---N 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   924 HIVHRDIKSSNILL--DGNFKayVADFGLSRLILPYRTHVTTELVGTLGYIPPEygQAW--VATLRGDVYSFGVVMLELL 999
Cdd:NF033483  127 GIVHRDIKPQNILItkDGRVK--VTDFGIARALSSTTMTQTNSVLGTVHYLSPE--QARggTVDARSDIYSLGIVLYEML 202

                  ....*
gi 15218425  1000 TGKRP 1004
Cdd:NF033483  203 TGRPP 207
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
809-1076 2.01e-18

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: 86.63  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN------GTKLAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd05032   14 LGQGSFGMVYEGLAKGvvkgepETRVAIKTVNENASMRERiEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMELMAK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHE---NPEGPAQLDWPKRLNIMRGA---SSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLI- 954
Cdd:cd05032   94 GDLKSYLRSrrpEAENNPGLGPPTLQKFIQMAaeiADGMAYLA---AKKFVHRDLAARNCMVAEDLTVKIGDFGMTRDIy 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 ------------LPYRthvttelvgtlgYIPPEYGQAWVATLRGDVYSFGVVMLELLT-------GKRPMEVFRPKMSRE 1015
Cdd:cd05032  171 etdyyrkggkglLPVR------------WMAPESLKDGVFTTKSDVWSFGVVLWEMATlaeqpyqGLSNEEVLKFVIDGG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425 1016 LvawvhtMKRdgkPEEVFDtllresgneeamlRVLDIACMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd05032  239 H------LDL---PENCPD-------------KLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
809-1002 2.09e-18

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: 86.13  E-value: 2.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKaEVEVLsraKHENLVALQGYCVHdsariLIYSFMENGSLDYW 887
Cdd:cd05118    7 IGEGAFGTVWLArDKVTGEKVAIKKIKNDFRHPKAALR-EIKLL---KHLNDVEGHPNIVK-----LLDVFEHRGGNHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 L-----HENpegpaqldwpkRLNIMRGASSGLA------YMHQICEP----H---IVHRDIKSSNILLDG-NFKAYVADF 948
Cdd:cd05118   78 LvfelmGMN-----------LYELIKDYPRGLPldliksYLYQLLQAldflHsngIIHRDLKPENILINLeLGQLKLADF 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  949 GLSRlilPYRTHVTTELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd05118  147 GLAR---SFTSPPYTPYVATRWYRAPEvllgakpYGSSI------DIWSLGCILAELLTGR 198
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
469-688 2.11e-18

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 89.22  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  469 GFPSLQIFGIGACRLTgEIPAWLIKLQRVEVMDLSMNRFvGTIPGWLGTLPDLFYLDLSDNFLTgELPKELFQLRALmsq 548
Cdd:COG4886  111 NLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQL-TDLPEPLGNLTNLKSLDLSNNQLT-DLPEELGNLTNL--- 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  549 kaydaterNYLELpvfvnpnnvttnqQYNQLSSLPPTIyikrnnltgtipvevGQLKVLHILELLGNNFSgSIPDELSNL 628
Cdd:COG4886  185 --------KELDL-------------SNNQITDLPEPL---------------GNLTNLEELDLSGNQLT-DLPEPLANL 227
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  629 TNLERLDLSNNNLSgRIPWsLTGLHFLSYFNVANNTLSGpIPTGTQFDTFPKANFEGNPL 688
Cdd:COG4886  228 TNLETLDLSNNQLT-DLPE-LGNLTNLEELDLSNNQLTD-LPPLANLTNLKTLDLSNNQL 284
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
809-1002 2.14e-18

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: 86.82  E-value: 2.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKltgdygmMEKEFKA--------EVEVLSRAK-HENLVAL-----QGYCVHdsari 873
Cdd:cd07830    7 LGDGTFGSVYLARnKETGELVAIKK-------MKKKFYSweecmnlrEVKSLRKLNeHPNIVKLkevfrENDELY----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 LIYSFMEnGSLdYWLHENPEGPAqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd07830   75 FVFEYME-GNL-YQLMKDRKGKP-FSESVIRSIIYQILQGLAHIHKH---GFFHRDLKPENLLVSGPEVVKIADFGLARE 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  954 IL---PYrthvtTELVGTLGYIPPE-------YGQAwVatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd07830  149 IRsrpPY-----TDYVSTRWYRAPEillrstsYSSP-V-----DIWALGCIMAELYTLR 196
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
784-1071 3.18e-18

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: 86.27  E-value: 3.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  784 SRYevkdLTIFELLKatdnfsqanIIGCGGFGLVYKA--TLDnGTKLAVKKLTGDYG-MMEKEFKAEVEVLSRAKHENLV 860
Cdd:cd14046    2 SRY----LTDFEELQ---------VLGKGAFGQVVKVrnKLD-GRYYAIKKIKLRSEsKNNSRILREVMLLSRLNHQHVV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  861 ALQG-------------YCVHDSARILIYSFMENGSLDYWlhenpegpaqldwpkRLniMRGASSGLAYMHQicePHIVH 927
Cdd:cd14046   68 RYYQawieranlyiqmeYCEKSTLRDLIDSGLFQDTDRLW---------------RL--FRQILEGLAYIHS---QGIIH 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  928 RDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTEL-----------------VGTLGYIPPEYGQAWVATL--RGDV 988
Cdd:cd14046  128 RDLKPVNIFLDSNGNVKIGDFGLATSNKLNVELATQDInkstsaalgssgdltgnVGTALYVAPEVQSGTKSTYneKVDM 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  989 YSFGVVMLELltgkrpMEVFRPKMSRelvawVHTMKRDGKPEEVFDTLLRESgneEAMLRVLDIACMcVNQNPMKRPNIQ 1068
Cdd:cd14046  208 YSLGIIFFEM------CYPFSTGMER-----VQILTALRSVSIEFPPDFDDN---KHSKQAKLIRWL-LNHDPAKRPSAQ 272

                 ...
gi 15218425 1069 QVV 1071
Cdd:cd14046  273 ELL 275
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
808-1004 4.65e-18

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: 85.48  E-value: 4.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYG-------MMEKEFKAEVEVLSRA-KHENLVALQGYCVHDSARILIYSF 878
Cdd:cd13993    7 PIGEGAYGVVYLAVdLRTGRKYAIKCLYKSGPnskdgndFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIYIVLEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENPEGPAQLDWPKrlNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNF-KAYVADFGLSrlilpy 957
Cdd:cd13993   87 CPNGDLFEAITENRIYVGKTELIK--NVFLQLIDAVKHCH---SLGIYHRDIKPENILLSQDEgTVKLCDFGLA------ 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  958 rthvTTEL------VGTLGYIPPEYGQAW------VATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd13993  156 ----TTEKismdfgVGSEFYMAPECFDEVgrslkgYPCAAGDIWSLGIILLNLTFGRNP 210
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
26-379 4.92e-18

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 88.07  E-value: 4.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   26 VLFVLLYVLSISVFFLTVSEAVCNLQDRDSLLWFSGNVSSPVSPLHWNSSIDCCSWEGISCDKSPENRVTSIILSSRGLS 105
Cdd:COG4886   25 ILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  106 GNLPSSvlDLQRLSRLDLSHNRLSGPlpPGFLSALDQLLVLDLSYNSFKgELPlqQSFGNGSNgifpIQTVDLSSNLLEG 185
Cdd:COG4886  105 GNEELS--NLTNLESLDLSGNQLTDL--PEELANLTNLKELDLSNNQLT-DLP--EPLGNLTN----LKSLDLSNNQLTD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  186 eiLSSSvfLQGAFNLTSFNVSNNSFTgSIPSFMCtASPQLTKLDFSYNDFSgDLSQELSRCSRLSVLRAGFNNLSgEIPk 265
Cdd:COG4886  174 --LPEE--LGNLTNLKELDLSNNQIT-DLPEPLG-NLTNLEELDLSGNQLT-DLPEPLANLTNLETLDLSNNQLT-DLP- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  266 EIYNLPELEQLFLPVNRLSGkIDNgITRLTKLTLLELYSNHIEGEIPKDIGKLSKLSSLQLHVNNLMGSIPVSLANCTKL 345
Cdd:COG4886  245 ELGNLTNLEELDLSNNQLTD-LPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTT 322
                        330       340       350
                 ....*....|....*....|....*....|....
gi 15218425  346 VKLNLRVNQLGGTLSAIDFSRFQSLSILDLGNNS 379
Cdd:COG4886  323 LLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLL 356
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
803-1006 5.36e-18

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 85.54  E-value: 5.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT---LDNGTKL--AVKKLTGDYG-MMEKEFKAEVEVLSRAKHENLVALQGYCVhdSARI-LI 875
Cdd:cd05057    9 LEKGKVLGSGAFGTVYKGVwipEGEKVKIpvAIKVLREETGpKANEEILDEAYVMASVDHPHLVRLLGICL--SSQVqLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHENPE--GPAQLdwpkrLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd05057   87 TQLMPLGCLLDYVRNHRDniGSQLL-----LNWCVQIAKGMSYLE---EKRLVHRDLAARNVLVKTPNHVKITDFGLAKL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  954 ILPYRTHVTTELvgtlGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRPME 1006
Cdd:cd05057  159 LDVDEKEYHAEG----GKVPikwmaLESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYE 213
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
802-1006 5.37e-18

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: 85.01  E-value: 5.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKA---EVEVLSRAKHENLVALqgycvhdsarilIYSF 878
Cdd:cd08225    1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEAskkEVILLAKMKHPNIVTF------------FASF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLdYWLHENPEGPaqlDWPKRLNIMRGA--------------SSGLAYMHqicEPHIVHRDIKSSNILLDGNFK-A 943
Cdd:cd08225   69 QENGRL-FIVMEYCDGG---DLMKRINRQRGVlfsedqilswfvqiSLGLKHIH---DRKILHRDIKSQNIFLSKNGMvA 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  944 YVADFGLSRlILPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd08225  142 KLGDFGIAR-QLNDSMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFE 203
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
809-1001 6.70e-18

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: 85.46  E-value: 6.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGD--YGMMEKEFKAEVEVLSRAK-HENLVALQGYCVHDSARILIYSFMEnGSL 884
Cdd:cd07832    8 IGEGAHGIVFKAKdRETGETVALKKVALRklEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYML-SSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLH--ENPEGPAQLdwpKRlnIMRGASSGLAYMHqicEPHIVHRDIKSSNILLD--GNFKayVADFGLSRLILPYRTH 960
Cdd:cd07832   87 SEVLRdeERPLTEAQV---KR--YMRMLLKGVAYMH---ANRIMHRDLKPANLLISstGVLK--IADFGLARLFSEEDPR 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15218425  961 VTTELVGTLGYIPPE--YG-QAWVATLrgDVYSFGVVMLELLTG 1001
Cdd:cd07832  157 LYSHQVATRWYRAPEllYGsRKYDEGV--DLWAVGCIFAELLNG 198
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
802-1070 1.14e-17

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 84.63  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT------LDNGTKLAVKKLTGDYGMME-KEFKAEVEVLSRAKHENLVALQGYCVHDSARIL 874
Cdd:cd05045    1 NLVLGKTLGEGEFGKVVKATafrlkgRAGYTTVAVKMLKENASSSElRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYWLHENPE-GPAQLDWPKRLNIMRGASSG---------LAYMHQIC-------EPHIVHRDIKSSNILL 937
Cdd:cd05045   81 IVEYAKYGSLRSFLRESRKvGPSYLGSDGNRNSSYLDNPDeraltmgdlISFAWQISrgmqylaEMKLVHRDLAARNVLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  938 DGNFKAYVADFGLSRLILPYRTHVTTelvgTLGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRPK 1011
Cdd:cd05045  161 AEGRKMKISDFGLSRDVYEEDSYVKR----SKGRIPvkwmaIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPE 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425 1012 MSRELVAWVHTMKR-DGKPEEVFDTLLResgneeamlrvldiacmCVNQNPMKRPNIQQV 1070
Cdd:cd05045  237 RLFNLLKTGYRMERpENCSEEMYNLMLT-----------------CWKQEPDKRPTFADI 279
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
808-1077 1.27e-17

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 83.88  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLdNGTKLAVKKLTGDygMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYS-FMENGSLDY 886
Cdd:cd05082   13 TIGKGEFGDVMLGDY-RGNKVAVKCIKND--ATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTeYMAKGSLVD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHEnpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIlpYRTHVTTELv 966
Cdd:cd05082   90 YLRS--RGRSVLGGDCLLKFSLDVCEAMEYLEG---NNFVHRDLAARNVLVSEDNVAKVSDFGLTKEA--SSTQDTGKL- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  967 gTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMS-RELVAWVHTMKR----DGKPEEVFDTLLRes 1040
Cdd:cd05082  162 -PVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY----PRIPlKDVVPRVEKGYKmdapDGCPPAVYDVMKN-- 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15218425 1041 gneeamlrvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05082  235 ---------------CWHLDAAMRPSFLQLREQLEHI 256
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
809-1033 1.40e-17

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: 84.42  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVykaTL----DNGTKLAVKKLTGDYGMMEKE---FKAEVEVLSRAKHENLVA-------LQGYCVHDSArIL 874
Cdd:cd13989    1 LGSGGFGYV---TLwkhqDTGEYVAIKKCRQELSPSDKNrerWCLEVQIMKKLNHPNVVSardvppeLEKLSPNDLP-LL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYWLH--ENPEGPAQLDWpkrLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLD--GNFKAY-VADFG 949
Cdd:cd13989   77 AMEYCSGGDLRKVLNqpENCCGLKESEV---RTLLSDISSAISYLH---ENRIIHRDLKPENIVLQqgGGRVIYkLIDLG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  950 LSRLIlpYRTHVTTELVGTLGYIPPE--YGQAWVATLrgDVYSFGVVMLELLTGKRPmevFRPKmsRELVAWvHTMKRDG 1027
Cdd:cd13989  151 YAKEL--DQGSLCTSFVGTLQYLAPElfESKKYTCTV--DYWSFGTLAFECITGYRP---FLPN--WQPVQW-HGKVKQK 220

                 ....*.
gi 15218425 1028 KPEEVF 1033
Cdd:cd13989  221 KPEHIC 226
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
806-1070 1.55e-17

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: 83.86  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  806 ANIIGCGGFG-LVYKATLDnGTKLAVKKLTGD-YGMMEKEfkaeVEVLSRA-KHENLValQGYCVHDSARILiYSFME-- 880
Cdd:cd13982    6 PKVLGYGSEGtIVFRGTFD-GRPVAVKRLLPEfFDFADRE----VQLLRESdEHPNVI--RYFCTEKDRQFL-YIALElc 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYwLHENPEGPAQLDWPKR--LNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLD-----GNFKAYVADFGLSRL 953
Cdd:cd13982   78 AASLQD-LVESPRESKLFLRPGLepVRLLRQIASGLAHLHSL---NIVHRDLKPQNILIStpnahGNVRAMISDFGLCKK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  954 iLPYRTHV---TTELVGTLGYIPPEY---GQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRElvawVHTMKrd 1026
Cdd:cd13982  154 -LDVGRSSfsrRSGVAGTSGWIAPEMlsgSTKRRQTRAVDIFSLGCVFYYVLSgGSHP---FGDKLERE----ANILK-- 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15218425 1027 GKPEEVFDTLLRESGNEEAmlrvlDIACMCVNQNPMKRPNIQQV 1070
Cdd:cd13982  224 GKYSLDKLLSLGEHGPEAQ-----DLIERMIDFDPEKRPSAEEV 262
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
808-1074 1.83e-17

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: 83.46  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDnGTKLAVKKLTGDYGMmeKEFKAEVEVLSRAKHENLVALQGYCVHdsARILIYSFMENGSLDYW 887
Cdd:cd14068    1 LLGDGGFGSVYRAVYR-GEDVAVKIFNKHTSF--RLLRQELVVLSHLHHPSLVALLAAGTA--PRMLVMELAPKGSLDAL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 L-HENpegpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILL-----DGNFKAYVADFGLSRLILpyRTHV 961
Cdd:cd14068   76 LqQDN----ASLTRTLQHRIALHVADGLRYLHS---AMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCC--RMGI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  962 TTElVGTLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLT-GKRPMEVFR-PKMSRELVawVHtmkrdGK-PEEVFDTLL 1037
Cdd:cd14068  147 KTS-EGTPGFRAPEVARGNVIyNQQADVYSFGLLLYDILTcGERIVEGLKfPNEFDELA--IQ-----GKlPDPVKEYGC 218
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15218425 1038 RESGNEEAMLRvldiacMCVNQNPMKRPNIQQVVDWL 1074
Cdd:cd14068  219 APWPGVEALIK------DCLKENPQCRPTSAQVFDIL 249
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
801-1004 2.09e-17

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: 83.80  E-value: 2.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATL-DNGTKLAVKKLTG---------DYGMMEKEfkaeveVLSRAKHENLVALQgYCVHDS 870
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEkETGKEYAIKVLDKrhiikekkvKYVTIEKE------VLSRLAHPGIVKLY-YTFQDE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  871 ARI-LIYSFMENGSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd05581   74 SKLyFVLEYAPNGDLLEYIRKY----GSLDEKCTRFYTAEIVLALEYLHSK---GIIHRDLKPENILLDEDMHIKITDFG 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  950 LSRL----------------ILPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05581  147 TAKVlgpdsspestkgdadsQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPP 217
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
801-1077 2.31e-17

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 84.01  E-value: 2.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKAT---LDNGTK----LAVKKLTGDygMMEKEFK---AEVEVLSR-AKHENLVALQGYCVHD 869
Cdd:cd05053   12 DRLTLGKPLGEGAFGQVVKAEavgLDNKPNevvtVAVKMLKDD--ATEKDLSdlvSEMEMMKMiGKHKNIINLLGACTQD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  870 SARILIYSFMENGSLDYWLHEN-PEGPAQ---LDWPKRLNIMRGASSGLAY-----MHQICEPHIVHRDIKSSNILLDGN 940
Cdd:cd05053   90 GPLYVVVEYASKGNLREFLRARrPPGEEAspdDPRVPEEQLTQKDLVSFAYqvargMEYLASKKCIHRDLAARNVLVTED 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  941 FKAYVADFGLSRLILP---YRTHvttelvgTLGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEvfrpk 1011
Cdd:cd05053  170 NVMKIADFGLARDIHHidyYRKT-------TNGRLPvkwmaPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYP----- 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425 1012 msrelvawvhtmkrdGKP-EEVFDtLLRESGNEE----AMLRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05053  238 ---------------GIPvEELFK-LLKEGHRMEkpqnCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRI 292
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
809-1038 3.22e-17

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: 82.99  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTgDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL 888
Cdd:cd05114   12 LGSGLFGVVRLGKWRAQYKVAIKAIR-EGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLLNYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENpegPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVGT 968
Cdd:cd05114   91 RQR---RGKLSRDMLLSMCQDVCEGMEYLER---NNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGAKFP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  969 LGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPME----------------VFRPKMSRELVAWVHTMKRDGKPE- 1030
Cdd:cd05114  165 VKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFEsksnyevvemvsrghrLYRPKLASKSVYEVMYSCWHEKPEg 244

                 ....*....
gi 15218425 1031 -EVFDTLLR 1038
Cdd:cd05114  245 rPTFADLLR 253
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
809-1072 3.25e-17

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 83.03  E-value: 3.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKK--LTGDYGMMEKEFKAEVEVLSRAKHE-NLVALQGYCVHDSARiLIYSFMENGSLD 885
Cdd:cd14131    9 LGKGGSSKVYKVLNPKKKIYALKRvdLEGADEQTLQSYKNEIELLKKLKGSdRIIQLYDYEVTDEDD-YLYMVMECGEID 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 Y--WLHENPEGPAQLDWpkrlnIMRGASSGLAYMHQICEPHIVHRDIKSSNILL-DGNFKayVADFGLSRLILPYRTHVT 962
Cdd:cd14131   88 LatILKKKRPKPIDPNF-----IRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLvKGRLK--LIDFGIAKAIQNDTTSIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  963 TEL-VGTLGYIPPE------YGQAWVATLR----GDVYSFGVVMLELLTGKRP---MEVFRPKMSR-------------E 1015
Cdd:cd14131  161 RDSqVGTLNYMSPEaikdtsASGEGKPKSKigrpSDVWSLGCILYQMVYGKTPfqhITNPIAKLQAiidpnheiefpdiP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425 1016 LVAWVHTMKRdgkpeevfdtllresgneeamlrvldiacmCVNQNPMKRPNIQQVVD 1072
Cdd:cd14131  241 NPDLIDVMKR------------------------------CLQRDPKKRPSIPELLN 267
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
808-1004 3.68e-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: 82.84  E-value: 3.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGyCVHDSARILIysFMEN---GS 883
Cdd:cd06624   15 VLGKGTFGVVYAArDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLG-SVSEDGFFKI--FMEQvpgGS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLhENPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLD---GNFKayVADFGLS-RL--ILPY 957
Cdd:cd06624   92 LSALL-RSKWGPLKDNENTIGYYTKQILEGLKYLH---DNKIVHRDIKGDNVLVNtysGVVK--ISDFGTSkRLagINPC 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  958 rthvTTELVGTLGYIPPE---YGQawvatlRG-----DVYSFGVVMLELLTGKRP 1004
Cdd:cd06624  166 ----TETFTGTLQYMAPEvidKGQ------RGygppaDIWSLGCTIIEMATGKPP 210
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
808-1008 5.14e-17

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: 82.43  E-value: 5.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKA-TLDNGTKLAVKKLT--------GDYGM--MEKEFKAEVEVLSRAKHENLVALQGYCVHDsariLIY 876
Cdd:cd06629    8 LIGKGTYGRVYLAmNATTGEMLAVKQVElpktssdrADSRQktVVDALKSEIDTLKDLDHPNIVQYLGFEETE----DYF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 S-FME---NGSLDYWLHEnpegPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLD--GNFKayVADFGL 950
Cdd:cd06629   84 SiFLEyvpGGSIGSCLRK----YGKFEEDLVRFFTRQILDGLAYLH---SKGILHRDLKADNILVDleGICK--ISDFGI 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  951 SRLILP-YRTHVTTELVGTLGYIPPE----YGQAWVATLrgDVYSFGVVMLELLTGKRP---MEVF 1008
Cdd:cd06629  155 SKKSDDiYGNNGATSMQGSVFWMAPEvihsQGQGYSAKV--DIWSLGCVVLEMLAGRRPwsdDEAI 218
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
801-1004 6.04e-17

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: 81.91  E-value: 6.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE---FKAEVEVLSRAKHENLVAL-------QGYC-VHD 869
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKElrnLRQEIEILRKLNHPNIIEMldsfetkKEFVvVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  870 SARILIYSFME-NGSLdywlhenPEGPAQldwpkrlNIMRGASSGLAYMHQicepH-IVHRDIKSSNILLDGNFKAYVAD 947
Cdd:cd14002   81 YAQGELFQILEdDGTL-------PEEEVR-------SIAKQLVSALHYLHS----NrIIHRDMKPQNILIGKGGVVKLCD 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  948 FGLSRLIlPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14002  143 FGFARAM-SCNTLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPP 198
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
178-663 6.52e-17

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 84.60  E-value: 6.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  178 LSSNLLEGEILSSSVFLQGAFNLTSFNVSNNSFTGSIPSFMCTASPQLTKLDFSYNDFSGDLSQELSRCSRLSVLRAGFN 257
Cdd:COG4886    3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  258 NLSGEIPKEIYNLPELEQLFLPVNrlsgkidNGITRLTKLTLLELYSNHIEgEIPKDIGKLSKLSSLQLHVNNLmGSIPV 337
Cdd:COG4886   83 SLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQL-TDLPE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  338 SLANCTKLVKLNLRVNQLGgTLSAiDFSRFQSLSILDLGNNSFTgEFPSTVYSCKmmtamrfagnkltgqispqvlELES 417
Cdd:COG4886  154 PLGNLTNLKSLDLSNNQLT-DLPE-ELGNLTNLKELDLSNNQIT-DLPEPLGNLT---------------------NLEE 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  418 LSFftfSDNKMTNLTGALSilqgckklstlimaknfydetvpsnkdflrsdGFPSLQIFGIGACRLTgEIPaWLIKLQRV 497
Cdd:COG4886  210 LDL---SGNQLTDLPEPLA--------------------------------NLTNLETLDLSNNQLT-DLP-ELGNLTNL 252
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  498 EVMDLSMNRfVGTIPGwLGTLPDLFYLDLSDNFLTGELPKELFQLRALmsQKAYDATERNYLELPVFVNPNNVTTNQQYN 577
Cdd:COG4886  253 EELDLSNNQ-LTDLPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGL--NSLLLLLLLLNLLELLILLLLLTTLLLLLL 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  578 QLSSLPPTIYIKRNNLTGTIPVEVGQLKVLHILELLGNNFSGSIPDELSNLTNLERLDLSNNNLSGRIPWSLTGLHFLSY 657
Cdd:COG4886  329 LLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALL 408

                 ....*.
gi 15218425  658 FNVANN 663
Cdd:COG4886  409 DAVNTE 414
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
809-1004 7.81e-17

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: 81.50  E-value: 7.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVK-----KLTGDygmMEKEFKAEVEVLSRAKHENLVALQGyCVHDSARI-LIYSFMEN 881
Cdd:cd14009    1 IGRGSFATVWKGrHKQTGEVVAIKeisrkKLNKK---LQENLESEIAILKSIKHPNIVRLYD-VQKTEDFIyLVLEYCAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENpegpaqldwpKRLN------IMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYV---ADFGLSR 952
Cdd:cd14009   77 GDLSQYIRKR----------GRLPeavarhFMQQLASGLKFLRS---KNIIHRDLKPQNLLLSTSGDDPVlkiADFGFAR 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  953 LILPYRTHVTteLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14009  144 SLQPASMAET--LCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPP 193
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
809-1002 8.68e-17

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: 82.23  E-value: 8.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKL-TGDYGMMEK--EFKA--EVEVLSRAKHENLVALQGYCVHDSARILIYSFME-- 880
Cdd:cd07841    8 LGEGTYAVVYKARdKETGRIVAIKKIkLGERKEAKDgiNFTAlrEIKLLQELKHPNIIGLLDVFGHKSNINLVFEFMEtd 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 ------NGSLDYwlhenpeGPAQLDwpkrlNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd07841   88 lekvikDKSIVL-------TPADIK-----SYMLMTLRGLEYLH---SNWILHRDLKPNNLLIASDGVLKLADFGLARSF 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  955 LPYRTHVTTELVgTLGYIPPE--YGqawvATLRG---DVYSFGVVMLELLTGK 1002
Cdd:cd07841  153 GSPNRKMTHQVV-TRWYRAPEllFG----ARHYGvgvDMWSVGCIFAELLLRV 200
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
812-998 8.78e-17

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 82.01  E-value: 8.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  812 GGFGLVYKATLDNGTkLAVKKL-TGDYGMMEKEFkaEVEVLSRAKHENLVALQGYCVH----DSARILIYSFMENGSLDY 886
Cdd:cd14141    6 GRFGCVWKAQLLNEY-VAVKIFpIQDKLSWQNEY--EIYSLPGMKHENILQFIGAEKRgtnlDVDLWLITAFHEKGSLTD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENpegpaQLDWPKRLNIMRGASSGLAYMHQIC-------EPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRT 959
Cdd:cd14141   83 YLKAN-----VVSWNELCHIAQTMARGLAYLHEDIpglkdghKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKS 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15218425  960 HVTTE-LVGTLGYIPPEYGQAWV-----ATLRGDVYSFGVVMLEL 998
Cdd:cd14141  158 AGDTHgQVGTRRYMAPEVLEGAInfqrdAFLRIDMYAMGLVLWEL 202
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
801-1069 1.03e-16

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: 81.24  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKAT-LDNGTKLAVK--KLTGDygmmEKEFKA---EVEVLSRAKHENLVALQGYCVHDSARIL 874
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRhRPSGQIMAVKviRLEID----EALQKQilrELDVLHKCNSPYIVGFYGAFYSEGDISI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYWLHENpeGPAqldwPKRL--NIMRGASSGLAYMHQicEPHIVHRDIKSSNILLD--GNFKayVADFGL 950
Cdd:cd06605   77 CMEYMDGGSLDKILKEV--GRI----PERIlgKIAVAVVKGLIYLHE--KHKIIHRDVKPSNILVNsrGQVK--LCDFGV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  951 S-RLIlpyrTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPM---EVFRPKMSRELVAWVHTMKRD 1026
Cdd:cd06605  147 SgQLV----DSLAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYpppNAKPSMMIFELLSYIVDEPPP 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 15218425 1027 GKPEEVFDTLLResgneeamlrvlDIACMCVNQNPMKRPNIQQ 1069
Cdd:cd06605  223 LLPSGKFSPDFQ------------DFVSQCLQKDPTERPSYKE 253
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
807-1002 1.14e-16

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: 82.57  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKAT-LDNGTKLAVKKLTgdygmmeKEFKA---------EVEVLSRAKHENLVALQGYCVHDSAR---- 872
Cdd:cd07834    6 KPIGSGAYGVVCSAYdKRTGRKVAIKKIS-------NVFDDlidakrilrEIKILRHLKHENIIGLLDILRPPSPEefnd 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 -ILIYSFMENgSLDYWLHEnpegpaqldwPKRL----------NIMRGassgLAYMHqicEPHIVHRDIKSSNILLDGNF 941
Cdd:cd07834   79 vYIVTELMET-DLHKVIKS----------PQPLtddhiqyflyQILRG----LKYLH---SAGVIHRDLKPSNILVNSNC 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  942 KAYVADFGLSRLILP-YRTHVTTELVGTLGYIPPE-------YGQAwVatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd07834  141 DLKICDFGLARGVDPdEDKGFLTEYVVTRWYRAPElllsskkYTKA-I-----DIWSVGCIFAELLTRK 203
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
824-1077 1.22e-16

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: 81.44  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  824 NGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL-DYWLHENpegpAQLDWPK 902
Cdd:cd14045   29 DGRTVAIKKIAKKSFTLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLnDVLLNED----IPLNWGF 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  903 RLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlilpYRTHVTTELVGTLG------YIPPEY 976
Cdd:cd14045  105 RFSFATDIARGMAYLHQ---HKIYHGRLKSSNCVIDDRWVCKIADYGLTT----YRKEDGSENASGYQqrlmqvYLPPEN 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  977 GQA--WVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRelvAWVHTMkrdgkPEevfdtllRESGNEEAML----RVL 1050
Cdd:cd14045  178 HSNtdTEPTQATDVYSYAIILLEIATRNDPVPEDDYSLDE---AWCPPL-----PE-------LISGKTENSCpcpaDYV 242
                        250       260
                 ....*....|....*....|....*..
gi 15218425 1051 DIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14045  243 ELIRRCRKNNPAQRPTFEQIKKTLHKI 269
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
809-1004 1.29e-16

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: 80.77  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVY----KATldnGTKLAVKKLTgdYGMMEKE-FKAEVEVLSRAKHENLVALqgycvHDSAR-----ILIYSF 878
Cdd:cd14006    1 LGRGRFGVVKrcieKAT---GREFAAKFIP--KRDKKKEaVLREISILNQLQHPRIIQL-----HEAYEsptelVLILEL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSL-DYWLHenpegPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYV--ADFGLSRLIL 955
Cdd:cd14006   71 CSGGELlDRLAE-----RGSLSEEEVRTYMRQLLEGLQYLHNH---HILHLDLKPENILLADRPSPQIkiIDFGLARKLN 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425  956 PyrTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14006  143 P--GEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSP 189
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
809-1004 1.47e-16

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: 81.33  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKL--TGDYGMMEkEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDY 886
Cdd:cd06611   13 LGDGAFGKVYKAQHKETGLFAAAKIiqIESEEELE-DFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGALDS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENPEGpaqLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL--DGNFKayVADFGLSRLILPYRTHVTTe 964
Cdd:cd06611   92 IMLELERG---LTEPQIRYVCRQMLEALNFLH---SHKVIHRDLKAGNILLtlDGDVK--LADFGVSAKNKSTLQKRDT- 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425  965 LVGTLGYIPPEYgqawVAT---------LRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd06611  163 FIGTPYWMAPEV----VACetfkdnpydYKADIWSLGITLIELAQMEPP 207
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
840-1004 1.49e-16

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: 81.25  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  840 MEKEFKAEVEVLSR-AKHENLVALQGYCVHDSARILIYSFMENGSL-DYwLHENpegpAQLDWPKRLNIMRGASSGLAYM 917
Cdd:cd14093   51 LREATRREIEILRQvSGHPNIIELHDVFESPTFIFLVFELCRKGELfDY-LTEV----VTLSEKKTRRIMRQLFEAVEFL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  918 HQICephIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRThvTTELVGTLGYIPPEYGQA-WVATLRG-----DVYSF 991
Cdd:cd14093  126 HSLN---IVHRDLKPENILLDDNLNVKISDFGFATRLDEGEK--LRELCGTPGYLAPEVLKCsMYDNAPGygkevDMWAC 200
                        170
                 ....*....|...
gi 15218425  992 GVVMLELLTGKRP 1004
Cdd:cd14093  201 GVIMYTLLAGCPP 213
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
807-1077 1.52e-16

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: 80.98  E-value: 1.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATL----DNGTKLAVKKLTGDYGMME-KEFKAEVEVLSRAKHENLVALQGYCV-HDSARILIYSFME 880
Cdd:cd05058    1 EVIGKGHFGCVYHGTLidsdGQKIHCAVKSLNRITDIEEvEQFLKEGIIMKDFSHPNVLSLLGICLpSEGSPLVVLPYMK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHENPEGPAQLDWPK-RLNIMRGassglayMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP--- 956
Cdd:cd05058   81 HGDLRNFIRSETHNPTVKDLIGfGLQVAKG-------MEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDkey 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  957 YRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKRDGKPEEVFDT 1035
Cdd:cd05058  154 YSVHNHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTrGAPP---YPDVDSFDITVYLLQGRRLLQPEYCPDP 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 15218425 1036 LLresgneEAMLRvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05058  231 LY------EVMLS-------CWHPKPEMRPTFSELVSRISQI 259
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
802-1074 1.55e-16

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: 81.00  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT--LDNGTkLAVKKLTgdygMMEKEFKAEVEVLSRAKHENLVALQG------YC------- 866
Cdd:cd14047    7 DFKEIELIGSGGFGQVFKAKhrIDGKT-YAIKRVK----LNNEKAEREVKALAKLDHPNIVRYNGcwdgfdYDpetsssn 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  867 ---VHDSARILIYSFMENGSLDYWLHENpeGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKA 943
Cdd:cd14047   82 ssrSKTKCLFIQMEFCEKGTLESWIEKR--NGEKLDKVLALEIFEQITKGVEYIHS---KKLIHRDLKPSNIFLVDTGKV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  944 YVADFGLSrlilpyrTHVT-----TELVGTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTgkrpmeVFRPKM 1012
Cdd:cd14047  157 KIGDFGLV-------TSLKndgkrTKSKGTLSYMSPEqissqdYGK------EVDIYALGLILFELLH------VCDSAF 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425 1013 SRELVaWvhTMKRDGKPEEVFDTLLREsgnEEAMLRVLdiacmcVNQNPMKRPNIQQVVDWL 1074
Cdd:cd14047  218 EKSKF-W--TDLRNGILPDIFDKRYKI---EKTIIKKM------LSKKPEDRPNASEILRTL 267
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
800-1072 1.89e-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: 80.81  E-value: 1.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  800 TDNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSR-AKHENLVALQG-------------- 864
Cdd:cd06608    5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKfSNHPNIATFYGafikkdppggddql 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  865 -----YCVHDSARILIYSFMENGSLdywLHENpegpaQLDWpkrlnIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDG 939
Cdd:cd06608   85 wlvmeYCGGGSVTDLVKGLRKKGKR---LKEE-----WIAY-----ILRETLRGLAYLH---ENKVIHRDIKGQNILLTE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  940 NFKAYVADFGLSRlilpyrtHVTTEL------VGTLGYIPPEYgqawVA---------TLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd06608  149 EAEVKLVDFGVSA-------QLDSTLgrrntfIGTPYWMAPEV----IAcdqqpdasyDARCDVWSLGITAIELADGKPP 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425 1005 MevfrpkmsrelvAWVHTMK------RDGKPEevfdtlLRESGNEEAMLRvlDIACMCVNQNPMKRPNIQQVVD 1072
Cdd:cd06608  218 L------------CDMHPMRalfkipRNPPPT------LKSPEKWSKEFN--DFISECLIKNYEQRPFTEELLE 271
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
809-998 2.19e-16

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 80.98  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLdNGTKLAVKKLtgdYGMMEKEFKAEVE----VLSRakHENLValqGYCVHD-------SARILIYS 877
Cdd:cd14144    3 VGKGRYGEVWKGKW-RGEKVAVKIF---FTTEEASWFRETEiyqtVLMR--HENIL---GFIAADikgtgswTQLYLITD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYWLHENpegpaQLDWPKRLNIMRGASSGLAYMH-QIC----EPHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd14144   74 YHENGSLYDFLRGN-----TLDTQSMLKLAYSAACGLAHLHtEIFgtqgKPAIAHRDIKSKNILVKKNGTCCIADLGLAV 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  953 LILPYRTHV---TTELVGTLGYIPPEY------GQAWVATLRGDVYSFGVVMLEL 998
Cdd:cd14144  149 KFISETNEVdlpPNTRVGTKRYMAPEVldeslnRNHFDAYKMADMYSFGLVLWEI 203
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
803-997 2.38e-16

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: 80.54  E-value: 2.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT--LDNGTKLAVKKLTGDYGMMEKEFK--AEVEVLSRAK---HENLVALQGYCVHDSARILI 875
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSerVPTGKVYAVKKLKPNYAGAKDRLRrlEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHENPEgPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL--DGNFKayVADFGLSrL 953
Cdd:cd14052   82 TELCENGSLDVFLSELGL-LGRLDEFRVWKILVELSLGLRFIHDH---HFVHLDLKPANVLItfEGTLK--IGDFGMA-T 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  954 ILPYRTHVttELVGTLGYIPPE------YGQAwvatlrGDVYSFGVVMLE 997
Cdd:cd14052  155 VWPLIRGI--EREGDREYIAPEilsehmYDKP------ADIFSLGLILLE 196
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
793-1005 2.69e-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: 80.04  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  793 IFELLKAtdnfsqaniIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSA 871
Cdd:cd06613    1 DYELIQR---------IGSGTYGDVYKArNIATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  872 RILIYSFMENGSLDYWLHENpeGPaqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL--DGNFKayVADFG 949
Cdd:cd06613   72 LWIVMEYCGGGSLQDIYQVT--GP--LSELQIAYVCRETLKGLAYLHST---GKIHRDIKGANILLteDGDVK--LADFG 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  950 LSRLIlpyrTHVT---TELVGTLGYIPPE---------YGQawvatlRGDVYSFGVVMLELLTGKRPM 1005
Cdd:cd06613  143 VSAQL----TATIakrKSFIGTPYWMAPEvaaverkggYDG------KCDIWALGITAIELAELQPPM 200
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
809-1072 2.80e-16

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: 80.01  E-value: 2.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTgDYGMMEKEFKA----EVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd08224    8 IGKGQFSVVYRARcLLDGRLVALKKVQ-IFEMMDAKARQdclkEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRlILPYRTHVTT 963
Cdd:cd08224   87 LSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMH---SKRIMHRDIKPANVFITANGVVKLGDLGLGR-FFSSKTTAAH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  964 ELVGTLGYIPPE--YGQAWvaTLRGDVYSFGVVMLELLTGKRPMevFRPKMSreLVAWVHTMKR---DGKPEEVFDTLLR 1038
Cdd:cd08224  163 SLVGTPYYMSPEriREQGY--DFKSDIWSLGCLLYEMAALQSPF--YGEKMN--LYSLCKKIEKceyPPLPADLYSQELR 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15218425 1039 esgneeamlrvlDIACMCVNQNPMKRPNIQQVVD 1072
Cdd:cd08224  237 ------------DLVAACIQPDPEKRPDISYVLD 258
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
829-1074 4.04e-16

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR 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: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 80.46  E-value: 4.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  829 AVKKLTGDYG-MMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL--HEnPEGPAqldwPKRLN 905
Cdd:cd05051   50 AVKMLRPDASkNAREDFLKEVKIMSQLKDPNIVRLLGVCTRDEPLCMIVEYMENGDLNQFLqkHE-AETQG----ASATN 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  906 IMRGASSGLAYM-HQIC-------EPHIVHRDIKSSNILLDGNFKAYVADFGLSR-------------LILPYRThvtte 964
Cdd:cd05051  125 SKTLSYGTLLYMaTQIAsgmkyleSLNFVHRDLATRNCLVGPNYTIKIADFGMSRnlysgdyyriegrAVLPIRW----- 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 lvgtlgyippeygQAWVATLRG------DVYSFGVVMLELLT--GKRPMEVfrpkMSRElvaWV-----HTMKRDGKPEe 1031
Cdd:cd05051  200 -------------MAWESILLGkfttksDVWAFGVTLWEILTlcKEQPYEH----LTDE---QVienagEFFRDDGMEV- 258
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 15218425 1032 vfdtLLRESGNEEAmlRVLDIACMCVNQNPMKRPNIQQVVDWL 1074
Cdd:cd05051  259 ----YLSRPPNCPK--EIYELMLECWRRDEEDRPTFREIHLFL 295
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
809-1002 4.69e-16

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: 80.44  E-value: 4.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLtgdygMM--EKE-FKA----EVEVLSRAKHENLVALQGYCVHDSARI------- 873
Cdd:cd07866   16 LGEGTFGEVYKArQIKTGRVVALKKI-----LMhnEKDgFPItalrEIKILKKLKHPNVVPLIDMAVERPDKSkrkrgsv 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 -LIYSFME---NGSLdywlhENPEgpAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd07866   91 yMVTPYMDhdlSGLL-----ENPS--VKLTESQIKCYMLQLLEGINYLH---ENHILHRDIKAANILIDNQGILKIADFG 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  950 LSRlilPYR-------------THVTTELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd07866  161 LAR---PYDgpppnpkggggggTRKYTNLVVTRWYRPPElllgerrYTTAV------DIWGIGCVFAEMFTRR 224
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
801-1005 4.77e-16

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: 80.23  E-value: 4.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYgmmEKE-FKA----EVEVLSRAKHENLVALQGYCVHDS---- 870
Cdd:cd07864    7 DKFDIIGIIGEGTYGQVYKAKdKDTGELVALKKVRLDN---EKEgFPItairEIKILRQLNHRSVVNLKEIVTDKQdald 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  871 ------ARILIYSFMEN---GSLDywlhenpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNF 941
Cdd:cd07864   84 fkkdkgAFYLVFEYMDHdlmGLLE-------SGLVHFSEDHIKSFMKQLLEGLNYCHK---KNFLHRDIKCSNILLNNKG 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  942 KAYVADFGLSRLILPYRTHVTTELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLTgKRPM 1005
Cdd:cd07864  154 QIKLADFGLARLYNSEESRPYTNKVITLWYRPPElllgeerYGPAI------DVWSCGCILGELFT-KKPI 217
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
802-1075 4.98e-16

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 79.15  E-value: 4.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKATLdNGTKLAVKKLTGDygMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIySFMEN 881
Cdd:cd05083    7 KLTLGEIIGEGEFGAVLQGEY-MGQKVAVKNIKCD--VTAQAFLEETAVMTKLQHKNLVRLLGVILHNGLYIVM-ELMSK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHEnpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlilPYRTHV 961
Cdd:cd05083   83 GNLVNFLRS--RGRALVPVIQLLQFSLDVAEGMEYLES---KKLVHRDLAARNILVSEDGVAKISDFGLAK---VGSMGV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  962 TTELVgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMS-RELVAWVHTMKRDGKPEEVFDTllre 1039
Cdd:cd05083  155 DNSRL-PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY----PKMSvKEVKEAVEKGYRMEPPEGCPPD---- 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 15218425 1040 sgneeamlrVLDIACMCVNQNPMKRPNIQQVVDWLK 1075
Cdd:cd05083  226 ---------VYSIMTSCWEAEPGKRPSFKKLREKLE 252
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
801-1005 5.24e-16

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: 79.96  E-value: 5.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKAtLDNGTK--LAVKKLTgdygmMEKEFKA-------EVEVLSRAKHENLVALQGYCV---H 868
Cdd:cd07843    5 DEYEKLNRIEEGTYGVVYRA-RDKKTGeiVALKKLK-----MEKEKEGfpitslrEINILLKLQHPNIVTVKEVVVgsnL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  869 DSarilIYSFMEngsldYWLHE-------NPEGPAQldwPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLD--G 939
Cdd:cd07843   79 DK----IYMVME-----YVEHDlkslmetMKQPFLQ---SEVKCLMLQLLSGVAHLHD---NWILHRDLKTSNLLLNnrG 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  940 NFKayVADFGLSRL----ILPYrthvtTELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLTgKRPM 1005
Cdd:cd07843  144 ILK--ICDFGLAREygspLKPY-----TQLVVTLWYRAPElllgakeYSTAI------DMWSVGCIFAELLT-KKPL 206
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
809-1079 5.47e-16

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 79.59  E-value: 5.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLV----YKATLDN-GTKLAVKKLT-GDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSAR--ILIYSFME 880
Cdd:cd05079   12 LGEGHFGKVelcrYDPEGDNtGEQVAVKSLKpESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNgiKLIMEFLP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLhenPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTH 960
Cdd:cd05079   92 SGSLKEYL---PRNKNKINLKQQLKYAVQICKGMDYLGS---RQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTT--ELVGTLGYIPPE---YGQAWVATlrgDVYSFGVVMLELLT----GKRPMEVFR----PKMSRELVAWVHTMKRDG 1027
Cdd:cd05079  166 YTVkdDLDSPVFWYAPEcliQSKFYIAS---DVWSFGVTLYELLTycdsESSPMTLFLkmigPTHGQMTVTRLVRVLEEG 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425 1028 K--------PEEVFDTLLResgneeamlrvldiacmCVNQNPMKRPNIQqvvDWLKNIEA 1079
Cdd:cd05079  243 KrlprppncPEEVYQLMRK-----------------CWEFQPSKRTTFQ---NLIEGFEA 282
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
809-1006 6.57e-16

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: 78.70  E-value: 6.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGlvyKATL----DNGTKLAVKKLtGDYGMMEKE---FKAEVEVLSRAKHENLVALQGycvhdsariliySFMEN 881
Cdd:cd08218    8 IGEGSFG---KALLvkskEDGKQYVIKEI-NISKMSPKEreeSRKEVAVLSKMKHPNIVQYQE------------SFEEN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLdYWLHENPEGPaqlDWPKRLNIMRGA----SSGLAYMHQIC-------EPHIVHRDIKSSNILLDGNFKAYVADFGL 950
Cdd:cd08218   72 GNL-YIVMDYCDGG---DLYKRINAQRGVlfpeDQILDWFVQLClalkhvhDRKILHRDIKSQNIFLTKDGIIKLGDFGI 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  951 SRLIlpyrtHVTTEL----VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd08218  148 ARVL-----NSTVELartcIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFE 202
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
808-1004 6.75e-16

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: 79.13  E-value: 6.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVKKL----TGDYGMmeKEFKAEVEVLSRAKHENLVALQgYCVHDSARI-LIYSFMEN 881
Cdd:cd14097    8 KLGQGSFGVVIEAThKETQTKWAIKKInrekAGSSAV--KLLEREVDILKHVNHAHIIHLE-EVFETPKRMyLVMELCED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWL-HENPEGPAQLDWpkrlnIMRGASSGLAYMHQicePHIVHRDIKSSNILL-----DGNFK--AYVADFGLSRL 953
Cdd:cd14097   85 GELKELLlRKGFFSENETRH-----IIQSLASAVAYLHK---NDIVHRDLKLENILVkssiiDNNDKlnIKVTDFGLSVQ 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425  954 ILPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14097  157 KYGLGEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPP 207
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
808-1000 7.11e-16

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 79.73  E-value: 7.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATL--DNGTK---LAVKKLTGD-YG--MMEKEFKAEVEVlsraKHENLV----ALQGYCVHDSARILI 875
Cdd:cd14055    2 LVGKGRFAEVWKAKLkqNASGQyetVAVKIFPYEeYAswKNEKDIFTDASL----KHENILqfltAEERGVGLDRQYWLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHENPegpaqLDWPKRLNIMRGASSGLAYMHQICEPH------IVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd14055   78 TAYHENGSLQDYLTRHI-----LSWEDLCKMAGSLARGLAHLHSDRTPCgrpkipIAHRDLKSSNILVKNDGTCVLADFG 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  950 LSRLILPyrTHVTTEL-----VGTLGYIPPEYGQAWV------ATLRGDVYSFGVVMLELLT 1000
Cdd:cd14055  153 LALRLDP--SLSVDELansgqVGTARYMAPEALESRVnledleSFKQIDVYSMALVLWEMAS 212
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
808-1077 7.15e-16

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 79.21  E-value: 7.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATL--DNGT--KLAVKKLTGD-YGMME-KEFKAEVEVLSRAKHENLVALQGYCVHDSAR-----ILIY 876
Cdd:cd14204   14 VLGEGEFGSVMEGELqqPDGTnhKVAVKTMKLDnFSQREiEEFLSEAACMKDFNHPNVIRLLGVCLEVGSQripkpMVIL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHEN--PEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd14204   94 PFMKYGDLHSFLLRSrlGSGPQHVPLQTLLKFMIDIALGMEYLSS---RNFLHRDLAARNCMLRDDMTVCVADFGLSKKI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 LP---YRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTgkRPMEVFRPKMSRELVAWVHTMKRDGKPEE 1031
Cdd:cd14204  171 YSgdyYRQGRIAKM--PVKWIAVESLADRVYTVKSDVWAFGVTMWEIAT--RGMTPYPGVQNHEIYDYLLHGHRLKQPED 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15218425 1032 VFDTLlresgneeamlrvLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14204  247 CLDEL-------------YDIMYSCWRSDPTDRPTFTQLRENLEKL 279
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
812-1000 8.16e-16

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 79.30  E-value: 8.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  812 GGFGLVYKATLDNgTKLAVKKltgdYGMMEKE-FKAEVEVLSRA--KHENL---VALQGYCVHDSARI-LIYSFMENGSL 884
Cdd:cd14140    6 GRFGCVWKAQLMN-EYVAVKI----FPIQDKQsWQSEREIFSTPgmKHENLlqfIAAEKRGSNLEMELwLITAFHDKGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHENpegpaQLDWPKRLNIMRGASSGLAYMHQIC--------EPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP 956
Cdd:cd14140   81 TDYLKGN-----IVSWNELCHIAETMARGLSYLHEDVprckgeghKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  957 YRTHVTTE-LVGTLGYIPPEYGQAWV-----ATLRGDVYSFGVVMLELLT 1000
Cdd:cd14140  156 GKPPGDTHgQVGTRRYMAPEVLEGAInfqrdSFLRIDMYAMGLVLWELVS 205
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
808-1010 8.27e-16

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: 78.46  E-value: 8.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVKKL--TGDYGMMEKEfkaeVEVLSRAKHENLVALQGycvhdsariliySFMENGsl 884
Cdd:cd06612   10 KLGEGSYGSVYKAIhKETGQVVAIKVVpvEEDLQEIIKE----ISILKQCDSPYIVKYYG------------SYFKNT-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYW-LHENPEGPAQLDWPKRLN----------IMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRl 953
Cdd:cd06612   72 DLWiVMEYCGAGSVSDIMKITNktlteeeiaaILYQTLKGLEYLHSN---KKIHRDIKAGNILLNEEGQAKLADFGVSG- 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  954 ILPYRTHVTTELVGTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRPMEVFRP 1010
Cdd:cd06612  148 QLTDTMAKRNTVIGTPFWMAPEviqeigYNN------KADIWSLGITAIEMAEGKPPYSDIHP 204
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
808-1014 8.52e-16

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: 78.73  E-value: 8.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKE---------FKAEVEVLSRAKHENLVALQGyCVHDSARILIY- 876
Cdd:cd06628    7 LIGSGSFGSVYLGmNASSGELMAVKQVELPSVSAENKdrkksmldaLQREIALLRELQHENIVQYLG-SSSDANHLNIFl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHENPEGPAQLdwpkRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP 956
Cdd:cd06628   86 EYVPGGSVATLLNNYGAFEESL----VRNFVRQILKGLNYLH---NRGIIHRDIKGANILVDNKGGIKISDFGISKKLEA 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  957 YRTHVTT-----ELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMevfrPKMSR 1014
Cdd:cd06628  159 NSLSTKNngarpSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF----PDCTQ 217
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
801-1006 9.06e-16

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: 78.75  E-value: 9.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATL-DNGTKLAVKKLTGDYgmMEKE-----FKAEVEVLSRAKHENLVALQGYcVHDSARI- 873
Cdd:cd14117    6 DDFDIGRPLGKGKFGNVYLAREkQSKFIVALKVLFKSQ--IEKEgvehqLRREIEIQSHLRHPNILRLYNY-FHDRKRIy 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 LIYSFMENGSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd14117   83 LILEYAPRGELYKELQKH----GRFDEQRTATFMEELADALHYCH---EKKVIHRDIKPENLLMGYKGELKIADFGWSVH 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  954 ILPYRTHVtteLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14117  156 APSLRRRT---MCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFE 205
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
803-998 9.91e-16

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: 78.86  E-value: 9.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT-LDNGTKLAVKKL---TGDYGM---MEKEFkAEVEVLSRAKHENLVALQGYC-VHDSARI- 873
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARdLQDGRFVALKKVrvpLSEEGIplsTIREI-ALLKQLESFEHPNVVRLLDVChGPRTDREl 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 ---LIYSFMENgSLDYWLHENPegPAQLDWPKRLNIMRGASSGLAYMHQICephIVHRDIKSSNILL--DGNFKayVADF 948
Cdd:cd07838   80 kltLVFEHVDQ-DLATYLDKCP--KPGLPPETIKDLMRQLLRGLDFLHSHR---IVHRDLKPQNILVtsDGQVK--LADF 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  949 GLSRLilpYRTHVT-TELVGTLGYIPPE--YGQAWVATLrgDVYSFGVVMLEL 998
Cdd:cd07838  152 GLARI---YSFEMAlTSVVVTLWYRAPEvlLQSSYATPV--DMWSVGCIFAEL 199
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
809-1064 1.16e-15

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: 78.29  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYkatldngtkLAVKKLTGDY---------GMMEKE----FKAEVEVL-SRAKHENLVALqgYCVHDSARIL 874
Cdd:cd05611    4 ISKGAFGSVY---------LAKKRSTGDYfaikvlkksDMIAKNqvtnVKAERAIMmIQGESPYVAKL--YYSFQSKDYL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 iYSFME--NG----SLDYWLhenpeGPAQLDWPKrlNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADF 948
Cdd:cd05611   73 -YLVMEylNGgdcaSLIKTL-----GGLPEDWAK--QYIAEVVLGVEDLHQ---RGIIHRDIKPENLLIDQTGHLKLTDF 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  949 GLSRLILPYRThvTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMsrelvAWVHTMKRD-G 1027
Cdd:cd05611  142 GLSRNGLEKRH--NKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDA-----VFDNILSRRiN 214
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15218425 1028 KPEEVFdtllrESGNEEAMLRVLDIACMcvnqNPMKR 1064
Cdd:cd05611  215 WPEEVK-----EFCSPEAVDLINRLLCM----DPAKR 242
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
828-1000 1.33e-15

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 78.86  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  828 LAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWLHENpEGPAQL----DWP- 901
Cdd:cd05097   47 VAVKMLRADVTKTARnDFLKEIKIMSRLKNPNIIRLLGVCVSDDPLCMITEYMENGDLNQFLSQR-EIESTFthanNIPs 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  902 -KRLNIMRGA---SSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP---YRTHVTTELvgtlgyipP 974
Cdd:cd05097  126 vSIANLLYMAvqiASGMKYLASL---NFVHRDLATRNCLVGNHYTIKIADFGMSRNLYSgdyYRIQGRAVL--------P 194
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15218425  975 EYGQAWVATLRG------DVYSFGVVMLELLT 1000
Cdd:cd05097  195 IRWMAWESILLGkfttasDVWAFGVTLWEMFT 226
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
809-1000 1.37e-15

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 78.40  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLV----YKATLDN-GTKLAVKKLTGDYGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARI--LIYSFME 880
Cdd:cd05080   12 LGEGHFGKVslycYDPTNDGtGEMVAVKALKADCGPQHRSgWKQEIDILKTLYHENIVKYKGCCSEQGGKSlqLIMEYVP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHENPEGPAQLdwpkrLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlilpyrtH 960
Cdd:cd05080   92 LGSLRDYLPKHSIGLAQL-----LLFAQQICEGMAYLHS---QHYIHRDLAARNVLLDNDRLVKIGDFGLAK-------A 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  961 VTTelvGTLGYIPPEYGQA---WVAT---------LRGDVYSFGVVMLELLT 1000
Cdd:cd05080  157 VPE---GHEYYRVREDGDSpvfWYAPeclkeykfyYASDVWSFGVTLYELLT 205
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
802-1070 1.56e-15

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: 77.85  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKA---EVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAalnEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHEnpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAY-VADFGLSRlILPY 957
Cdd:cd08220   81 APGGTLFEYIQQ--RKGSLLSEEEILHFFVQILLALHHVHS---KQILHRDLKTQNILLNKKRTVVkIGDFGISK-ILSS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  958 RTHVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEvfrpkmSRELVAWVHTMKRD--GKPEEVFDT 1035
Cdd:cd08220  155 KSKAYT-VVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFE------AANLPALVLKIMRGtfAPISDRYSE 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15218425 1036 LLREsgneeamlrvldIACMCVNQNPMKRPNIQQV 1070
Cdd:cd08220  228 ELRH------------LILSMLHLDPNKRPTLSEI 250
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
809-1077 1.59e-15

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 77.56  E-value: 1.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLtGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL 888
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKI-YKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENpegPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILL---DGNFKAYVADFGLSRLI--LPYRT-HVT 962
Cdd:cd14156   80 ARE---ELPLSWREKVELACDISRGMVYLHS---KNIYHRDLNSKNCLIrvtPRGREAVVTDFGLAREVgeMPANDpERK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  963 TELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELL------------TGKRPMEVfrpKMSRELVawvhtmkrDGKPE 1030
Cdd:cd14156  154 LSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILaripadpevlprTGDFGLDV---QAFKEMV--------PGCPE 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425 1031 evfdtllresgneeamlRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14156  223 -----------------PFLDLAASCCRMDAFKRPSFAELLDELEDI 252
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
807-1072 1.67e-15

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: 77.86  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLDNGTKLAVKKL---TGDYGMMEKEFKA---EVEVLSRAKHENLVALQGYCVHDSARILIYSFME 880
Cdd:cd06631    7 NVLGKGAYGTVYCGLTSTGQLIAVKQVeldTSDKEKAEKEYEKlqeEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLheNPEGPaqLDWPKRLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTH 960
Cdd:cd06631   87 GGSIASIL--ARFGA--LEEPVFCRYTKQILEGVAYLHNNN---VIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLSS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTTELV-----GTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRPMEVFrPKMSrelvAWVHTMKRDGKP 1029
Cdd:cd06631  160 GSQSQLlksmrGTPYWMAPEvinetgHGR------KSDIWSIGCTVFEMATGKPPWADM-NPMA----AIFAIGSGRKPV 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 15218425 1030 EEvfdtlLRESGNEEAMlrvlDIACMCVNQNPMKRPNIQQVVD 1072
Cdd:cd06631  229 PR-----LPDKFSPEAR----DFVHACLTRDQDERPSAEQLLK 262
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
807-1000 1.90e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 78.56  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKA-TLDNGTKLAVKKLtgdygMMEKEFKA-------EVEVLSRAKHENLVALQ--------------- 863
Cdd:cd07865   18 AKIGQGTFGEVFKArHRKTGQIVALKKV-----LMENEKEGfpitalrEIKILQLLKHENVVNLIeicrtkatpynrykg 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  864 ------GYCVHDSARILiysfmENGSLDYWLHEnpegpaqldwPKRlnIMRGASSGLAYMHQicePHIVHRDIKSSNILL 937
Cdd:cd07865   93 siylvfEFCEHDLAGLL-----SNKNVKFTLSE----------IKK--VMKMLLNGLYYIHR---NKILHRDMKAANILI 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  938 DGNFKAYVADFGLSRLIL----PYRTHVTTELVgTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLT 1000
Cdd:cd07865  153 TKDGVLKLADFGLARAFSlaknSQPNRYTNRVV-TLWYRPPElllgerdYGPPI------DMWGAGCIMAEMWT 219
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
809-999 2.14e-15

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 78.44  E-value: 2.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKL-----------------AVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDS 870
Cdd:cd05096   13 LGEGQFGEVHLCEVVNPQDLptlqfpfnvrkgrpllvAVKILRPDANKNARnDFLKEVKILSRLKDPNIIRLLGVCVDED 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  871 ARILIYSFMENGSLDYWLH----ENPEGPAQ-----------LDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNI 935
Cdd:cd05096   93 PLCMITEYMENGDLNQFLSshhlDDKEENGNdavppahclpaISYSSLLHVALQIASGMKYLSSL---NFVHRDLATRNC 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  936 LLDGNFKAYVADFGLSRLILP---YRTHVTTELvgtlgyipPEYGQAWVATLRG------DVYSFGVVMLELL 999
Cdd:cd05096  170 LVGENLTIKIADFGMSRNLYAgdyYRIQGRAVL--------PIRWMAWECILMGkfttasDVWAFGVTLWEIL 234
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
803-1070 2.54e-15

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 77.55  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKA--TLDnGTKLAVKKLTGDYGMMEKEFK--AEVEVLSRAKHENLVALQ-GYCVHDSARILIYS 877
Cdd:cd14049    8 FEEIARLGKGGYGKVYKVrnKLD-GQYYAIKKILIKKVTKRDCMKvlREVKVLAGLQHPNIVGYHtAWMEHVQLMLYIQM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYWLHE------------NPEGPAQLDWPkrLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDG-NFKAY 944
Cdd:cd14049   87 QLCELSLWDWIVErnkrpceeefksAPYTPVDVDVT--TKILQQLLEGVTYIHSM---GIVHRDLKPRNIFLHGsDIHVR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  945 VADFGLS-RLIL----------PYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLtgkrpmEVFRPKMS 1013
Cdd:cd14049  162 IGDFGLAcPDILqdgndsttmsRLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF------QPFGTEME 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425 1014 RelvAWVHTMKRDGKPEEVFDTLLRESGNEEAMLrvldiacmcVNQNPMKRPNIQQV 1070
Cdd:cd14049  236 R---AEVLTQLRNGQIPKSLCKRWPVQAKYIKLL---------TSTEPSERPSASQL 280
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
809-1074 3.17e-15

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: 76.82  E-value: 3.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGT-KLAVK---KLTGDYGMMEKEFKAEVEVLSRAKHENLValQGYCVHDSARILIYSFMENGSL 884
Cdd:cd14164    8 IGEGSFSKVKLATSQKYCcKVAIKivdRRRASPDFVQKFLPRELSILRRVNHPNIV--QMFECIEVANGRLYIVMEAAAT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DY--WLHENPEGPAqldwPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL--DGNfKAYVADFGLSRLILPYrTH 960
Cdd:cd14164   86 DLlqKIQEVHHIPK----DLARDMFAQMVGAVNYLHDM---NIVHRDLKCENILLsaDDR-KIKIADFGFARFVEDY-PE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTTELVGTLGYIPPEygqAWVAT----LRGDVYSFGVVMLELLTGKRPMEVFRPKMSRelvawvhtMKRDGkpeevfdtL 1036
Cdd:cd14164  157 LSTTFCGSRAYTPPE---VILGTpydpKKYDVWSLGVVLYVMVTGTMPFDETNVRRLR--------LQQRG--------V 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15218425 1037 LRESGNE-----EAMLRVLdiacmcVNQNPMKRPNIQQVV--DWL 1074
Cdd:cd14164  218 LYPSGVAleepcRALIRTL------LQFNPSTRPSIQQVAgnSWL 256
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
780-1010 3.41e-15

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: 77.34  E-value: 3.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  780 LFGNSRYEVKDLTIFELLKATDNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVL-SRAKHEN 858
Cdd:cd06639    1 LYGLFPYNSSMLGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILrSLPNHPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  859 LVALQGYCVHDSARI-----LIYSFMENGSLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSS 933
Cdd:cd06639   81 VVKFYGMFYKADQYVggqlwLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHN---NRIIHRDVKGN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  934 NILLDGNFKAYVADFGLSRLILPYRTHVTTElVGTLGYIPPE-------YGQAWVAtlRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd06639  158 NILLTTEGGVKLVDFGVSAQLTSARLRRNTS-VGTPFWMAPEviaceqqYDYSYDA--RCDVWSLGITAIELADGDPPLF 234

                 ....
gi 15218425 1007 VFRP 1010
Cdd:cd06639  235 DMHP 238
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
809-1077 4.49e-15

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 76.97  E-value: 4.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL---DNGTKLAVKKLT---GDYGMMEkEFKAEVEVLSRAKHENLVALQGYCVHDSAR------ILIY 876
Cdd:cd05075    8 LGEGEFGSVMEGQLnqdDSVLKVAVKTMKiaiCTRSEME-DFLSEAVCMKEFDHPNVMRLIGVCLQNTESegypspVVIL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHENPEGPAQLDWPKRL--NIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd05075   87 PFMKHGDLHSFLLYSRLGDCPVYLPTQMlvKFMTDIASGMEYLSS---KNFIHRDLAARNCMLNENMNVCVADFGLSKKI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 LP---YRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKRDGKPE 1030
Cdd:cd05075  164 YNgdyYRQGRISKM--PVKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTP---YPGVENSEIYDYLRQGNRLKQPP 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425 1031 EVFDTLLresgneEAMLRvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05075  239 DCLDGLY------ELMSS-------CWLLNPKDRPSFETLRCELEKI 272
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
792-1002 5.09e-15

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: 77.61  E-value: 5.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  792 TIFELlkaTDNFSQANIIGCGGFGLVYKATLD-NGTKLAVKKLTGDYG--MMEKEFKAEVEVLSRAKHENLVALQG---- 864
Cdd:cd07856    4 TVFEI---TTRYSDLQPVGMGAFGLVCSARDQlTGQNVAVKKIMKPFStpVLAKRTYRELKLLKHLRHENIISLSDifis 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  865 -----YCVH-----DSARILIYSFMENGSLDYWLHEnpegpaqldwpkrlnIMRGassgLAYMHQicePHIVHRDIKSSN 934
Cdd:cd07856   81 plediYFVTellgtDLHRLLTSRPLEKQFIQYFLYQ---------------ILRG----LKYVHS---AGVIHRDLKPSN 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  935 ILLDGNFKAYVADFGLSRLILPYrthvTTELVGTLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLTGK 1002
Cdd:cd07856  139 ILVNENCDLKICDFGLARIQDPQ----MTGYVSTRYYRAPEIMLTWQKyDVEVDIWSAGCIFAEMLEGK 203
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
801-1074 5.44e-15

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 77.14  E-value: 5.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATL------DNGTKLAVKKLTGDYGMMEKE-FKAEVEVLSR-AKHENLVALQGYCVHDSAR 872
Cdd:cd05055   35 NNLSFGKTLGAGAFGKVVEATAyglsksDAVMKVAVKMLKPTAHSSEREaLMSELKIMSHlGNHENIVNLLGACTIGGPI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 ILIYSFMENGSLDYWLHENPEgpAQLDWPKRLNIMRGASSGLAYMhqiCEPHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd05055  115 LVITEYCCYGDLLNFLRRKRE--SFLTLEDLLSFSYQVAKGMAFL---ASKNCIHRDLAARNVLLTHGKIVKICDFGLAR 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  953 LILPYRTHV---TTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMSRElvAWVHTMKRDGk 1028
Cdd:cd05055  190 DIMNDSNYVvkgNARL--PVKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPY----PGMPVD--SKFYKLIKEG- 260
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15218425 1029 peevfdtlLRESGNEEAMLRVLDIACMCVNQNPMKRPNIQQVVDWL 1074
Cdd:cd05055  261 --------YRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLI 298
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
801-1005 5.54e-15

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: 77.73  E-value: 5.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTG-DYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSAR-----I 873
Cdd:cd07849    5 PRYQNLSYIGEGAYGMVCSAVhKPTGQKVAIKKISPfEHQTYCLRTLREIKILLRFKHENIIGILDIQRPPTFEsfkdvY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 LIYSFME-------------NGSLDYWLHEnpegpaqldwpkrlnIMRGassgLAYMHQicePHIVHRDIKSSNILLDGN 940
Cdd:cd07849   85 IVQELMEtdlykliktqhlsNDHIQYFLYQ---------------ILRG----LKYIHS---ANVLHRDLKPSNLLLNTN 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  941 FKAYVADFGLSRLILPYRTH--VTTELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLTGkRPM 1005
Cdd:cd07849  143 CDLKICDFGLARIADPEHDHtgFLTEYVATRWYRAPEimlnskgYTKAI------DIWSVGCILAEMLSN-RPL 209
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
801-1081 5.59e-15

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: 77.40  E-value: 5.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLtgdygmMEKEFKA--------EVEVLSRAKHENLVALQGYCVHDSAR 872
Cdd:cd06650    5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKL------IHLEIKPairnqiirELQVLHECNSPYIVGFYGAFYSDGEI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 ILIYSFMENGSLDYWLHENPEGPAQLDWPKRLNIMRGassgLAYMHqicEPH-IVHRDIKSSNILLDGNFKAYVADFGLS 951
Cdd:cd06650   79 SICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKG----LTYLR---EKHkIMHRDVKPSNILVNSRGEIKLCDFGVS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  952 RLILpyrTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPM---------EVFRPKMSRELVAWVHT 1022
Cdd:cd06650  152 GQLI---DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpppdakeleLMFGCQVEGDAAETPPR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425 1023 MKRDGKPE--------------EVFDTLLRE------SGNEEAMLRvlDIACMCVNQNPMKRPNIQQVV--DWLKNIEAE 1080
Cdd:cd06650  229 PRTPGRPLssygmdsrppmaifELLDYIVNEpppklpSGVFSLEFQ--DFVNKCLIKNPAERADLKQLMvhAFIKRSDAE 306

                 .
gi 15218425 1081 K 1081
Cdd:cd06650  307 E 307
PLN03150 PLN03150
hypothetical protein; Provisional
593-709 5.61e-15

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 79.47  E-value: 5.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   593 LTGTIPVEVGQLKVLHILELLGNNFSGSIPDELSNLTNLERLDLSNNNLSGRIPWSLTGLHFLSYFNVANNTLSGPIPT- 671
Cdd:PLN03150  430 LRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAa 509
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 15218425   672 -------GTQFdtfpkaNFEGNPLLCGGVLLTSCDPTQHSTTKMG 709
Cdd:PLN03150  510 lggrllhRASF------NFTDNAGLCGIPGLRACGPHLSVGAKIG 548
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
808-1070 6.60e-15

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 75.81  E-value: 6.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDY 886
Cdd:cd05085    3 LLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKiKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlilpyRTHVTTELV 966
Cdd:cd05085   83 FLRKKKD---ELKTKQLVKFSLDAAAGMAYLES---KNCIHRDLAARNCLVGENNALKISDFGMSR-----QEDDGVYSS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  967 GTLGYIP-----PE---YGQawvATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELVAWVHTMKRDGK-PEEVFDTL 1036
Cdd:cd05085  152 SGLKQIPikwtaPEalnYGR---YSSESDVWSFGILLWETFSlGVCPYPGMTNQQAREQVEKGYRMSAPQRcPEDIYKIM 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15218425 1037 LResgneeamlrvldiacmCVNQNPMKRPNIQQV 1070
Cdd:cd05085  229 QR-----------------CWDYNPENRPKFSEL 245
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
802-1008 9.13e-15

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: 75.83  E-value: 9.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMME--KEFKA---EVEVLSRAKHENLVALQGyCVHD--SARI 873
Cdd:cd06653    3 NWRLGKLLGRGAFGEVYLCyDADTGRELAVKQVPFDPDSQEtsKEVNAlecEIQLLKNLRHDRIVQYYG-CLRDpeEKKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 LIY-SFMENGSLDYWLheNPEGPAQLDWPKRLNimRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd06653   82 SIFvEYMPGGSVKDQL--KAYGALTENVTRRYT--RQILQGVSYLHS---NMIVHRDIKGANILRDSAGNVKLGDFGASK 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  953 LILP-YRTHVTTELV-GTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRPMEVF 1008
Cdd:cd06653  155 RIQTiCMSGTGIKSVtGTPYWMSPEvisgegYGR------KADVWSVACTVVEMLTEKPPWAEY 212
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
809-1076 9.13e-15

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 76.16  E-value: 9.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL------DNGTKLAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd05061   14 LGQGSFGMVYEGNArdiikgEAETRVAVKTVNESASLRERiEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAH 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLH------ENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIl 955
Cdd:cd05061   94 GDLKSYLRslrpeaENNPGRPPPTLQEMIQMAAEIADGMAYLNA---KKFVHRDLAARNCMVAHDFTVKIGDFGMTRDI- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 pYRTHVTTElvGTLGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEvfrpKMSRELVAwvhTMKRDGkp 1029
Cdd:cd05061  170 -YETDYYRK--GGKGLLPvrwmaPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQ----GLSNEQVL---KFVMDG-- 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425 1030 eevfDTLLRESGNEEamlRVLDIACMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd05061  238 ----GYLDQPDNCPE---RVTDLMRMCWQFNPKMRPTFLEIVNLLKD 277
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
809-1004 9.53e-15

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: 76.15  E-value: 9.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYK-ATLDNGTKLAVKKLTGDYGMMEKE-FKAEVEVLSRAKHENLVA-------LQGYCVHDSArILIYSFM 879
Cdd:cd14038    2 LGTGGFGNVLRwINQETGEQVAIKQCRQELSPKNRErWCLEIQIMKRLNHPNVVAardvpegLQKLAPNDLP-LLAMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSLDYWLH--EN----PEGPAqldwpkrLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYV---ADFGL 950
Cdd:cd14038   81 QGGDLRKYLNqfENccglREGAI-------LTLLSDISSALRYLH---ENRIIHRDLKPENIVLQQGEQRLIhkiIDLGY 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425  951 SRLIlpYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14038  151 AKEL--DQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRP 202
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
804-998 1.11e-14

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 75.94  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  804 SQANIIGCGGFGLVYKATLdNGTKLAVKKLTG-DygmmEKEFKAEVEVLSRA--KHENLValqGYCVHDSAR-------I 873
Cdd:cd14142    8 TLVECIGKGRYGEVWRGQW-QGESVAVKIFSSrD----EKSWFRETEIYNTVllRHENIL---GFIASDMTSrnsctqlW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 LIYSFMENGSLDYWLHENPegpaqLDWPKRLNIMRGASSGLAYMH-QIC----EPHIVHRDIKSSNILLDGNFKAYVADF 948
Cdd:cd14142   80 LITHYHENGSLYDYLQRTT-----LDHQEMLRLALSAASGLVHLHtEIFgtqgKPAIAHRDLKSKNILVKSNGQCCIADL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  949 GLSRLilpyRTHVTTEL-------VGTLGYIPPEY------GQAWVATLRGDVYSFGVVMLEL 998
Cdd:cd14142  155 GLAVT----HSQETNQLdvgnnprVGTKRYMAPEVldetinTDCFESYKRVDIYAFGLVLWEV 213
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
802-1002 1.12e-14

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: 75.62  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKA--EVEVLSRAKHENLVALQGyCVHDSARI-LIYS 877
Cdd:cd07860    1 NFQKVEKIGEGTYGVVYKArNKLTGEVVALKKIRLDTETEGVPSTAirEISLLKELNHPNIVKLLD-VIHTENKLyLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMeNGSLDYWLHENPegPAQLDWPKRLNIMRGASSGLAYmhqiCEPH-IVHRDIKSSNILLDGNFKAYVADFGLSRLI-L 955
Cdd:cd07860   80 FL-HQDLKKFMDASA--LTGIPLPLIKSYLFQLLQGLAF----CHSHrVLHRDLKPQNLLINTEGAIKLADFGLARAFgV 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425  956 PYRTHvTTELVgTLGYIPPE--YGQAWVATLRgDVYSFGVVMLELLTGK 1002
Cdd:cd07860  153 PVRTY-THEVV-TLWYRAPEilLGCKYYSTAV-DIWSLGCIFAEMVTRR 198
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
809-1076 1.21e-14

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: 75.80  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCV------HDSARILIySFMEN 881
Cdd:cd13986    8 LGEGGFSFVYLVeDLSTGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIvkeaggKKEVYLLL-PYYKR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSL----DYWLHEN---PEgpaqldwPKRLNIMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVADFG---LS 951
Cdd:cd13986   87 GSLqdeiERRLVKGtffPE-------DRILHIFLGICRGLKAMHEPELVPYAHRDIKPGNVLLSEDDEPILMDLGsmnPA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  952 RLILPYRT-----HVTTELVGTLGYIPPEY-----GQawVATLRGDVYSFGVVMLELLTGKRPME-VFRPKMSRELVAwv 1020
Cdd:cd13986  160 RIEIEGRRealalQDWAAEHCTMPYRAPELfdvksHC--TIDEKTDIWSLGCTLYALMYGESPFErIFQKGDSLALAV-- 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425 1021 htMKRDGKPEevfdtllRESGNEEAMLRVLDiACMCVnqNPMKRPNIQQVVDWLKN 1076
Cdd:cd13986  236 --LSGNYSFP-------DNSRYSEELHQLVK-SMLVV--NPAERPSIDDLLSRVHD 279
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
788-1005 1.32e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 76.23  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  788 VKDLTIFELLKATDN---FSQANIIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLV 860
Cdd:cd06633    5 LKDPEIADLFYKDDPeeiFVDLHEIGHGSFGAVYFATNSHTNEVvAIKKMSYSGKQTNEKWQdiiKEVKFLQQLKHPNTI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  861 ALQGYCVHDSARILIYSFMENGSLDYW-LHENPEGPAQLdwpkrLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDG 939
Cdd:cd06633   85 EYKGCYLKDHTAWLVMEYCLGSASDLLeVHKKPLQEVEI-----AAITHGALQGLAYLHSHN---MIHRDIKAGNILLTE 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  940 NFKAYVADFGLSRLILPyrthvTTELVGTLGYIPPEygqAWVATLRG------DVYSFGVVMLELLTGKRPM 1005
Cdd:cd06633  157 PGQVKLADFGSASIASP-----ANSFVGTPYWMAPE---VILAMDEGqydgkvDIWSLGITCIELAERKPPL 220
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
809-1077 1.41e-14

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 74.99  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14221    1 LGKGCFGQAIKVThRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPegpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTE--- 964
Cdd:cd14221   81 IKSMD---SHYPWSQRVSFAKDIASGMAYLHSM---NIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLrsl 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 ----------LVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKmsrelvawvhTMKRdGKPEEVFd 1034
Cdd:cd14221  155 kkpdrkkrytVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPR----------TMDF-GLNVRGF- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 15218425 1035 tlLRESGNEEAMLRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14221  223 --LDRYCPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETL 263
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
816-1000 1.45e-14

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 75.80  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  816 LVYKATLDNGTKLAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWL-HENPE 893
Cdd:cd05095   37 FALEVSENQPVLVAVKMLRADANKNARnDFLKEIKIMSRLKDPNIIRLLAVCITDDPLCMITEYMENGDLNQFLsRQQPE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  894 GPAQLDWPKRL----NIMRGAS---SGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP---YRTHVTT 963
Cdd:cd05095  117 GQLALPSNALTvsysDLRFMAAqiaSGMKYLSSL---NFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSgdyYRIQGRA 193
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15218425  964 ELvgtlgyipPEYGQAWVATLRG------DVYSFGVVMLELLT 1000
Cdd:cd05095  194 VL--------PIRWMSWESILLGkfttasDVWAFGVTLWETLT 228
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
803-1005 1.49e-14

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 75.36  E-value: 1.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAtLDNGTK--LAVKKLTGDYGMMEKEFKA-EVEVLSRAKHENLVALQGYCVHDSARILIYSFM 879
Cdd:cd06609    3 FTLLERIGKGSFGEVYKG-IDKRTNqvVAIKVIDLEEAEDEIEDIQqEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSLDYWLHENPegpaqLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL--DGNFKayVADFG----LSRL 953
Cdd:cd06609   82 GGGSVLDLLKPGP-----LDETYIAFILREVLLGLEYLH---SEGKIHRDIKAANILLseEGDVK--LADFGvsgqLTST 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  954 ILPYRThvtteLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPM 1005
Cdd:cd06609  152 MSKRNT-----FVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPL 198
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
807-1074 1.75e-14

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: 75.06  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATlDNGTK--LAVKKLTgdYGMME--KEFKAEVEVLSR-AKHENLValqgyCVHDSA------RILI 875
Cdd:cd13985    6 KQLGEGGFSYVYLAH-DVNTGrrYALKRMY--FNDEEqlRVAIKEIEIMKRlCGHPNIV-----QYYDSAilssegRKEV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMEN--GSLDYWLheNPEGPAQLDWPKRLNIMRGASSGLAYMHQiCEPHIVHRDIKSSNILL--DGNFKayVADFG-L 950
Cdd:cd13985   78 LLLMEYcpGSLVDIL--EKSPPSPLSEEEVLRIFYQICQAVGHLHS-QSPPIIHRDIKIENILFsnTGRFK--LCDFGsA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  951 SRLILPYrthVTTELVG----------TLGYIPPE----YGQAWVATlRGDVYSFGVVMLELLTGKRPMEvfrpkMSREL 1016
Cdd:cd13985  153 TTEHYPL---ERAEEVNiieeeiqkntTPMYRAPEmidlYSKKPIGE-KADIWALGCLLYKLCFFKLPFD-----ESSKL 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425 1017 VAWvhTMKRDGKPEEVFDTLLResgneEAMLRVLDIacmcvnqNPMKRPNIQQVVDWL 1074
Cdd:cd13985  224 AIV--AGKYSIPEQPRYSPELH-----DLIRHMLTP-------DPAERPDIFQVINII 267
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
803-1014 2.06e-14

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: 74.66  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKATLDNGTKLAV-------KKLTGDYGMMEKEFKaeveVLSRAKHENLVALQGYCVHDSARILI 875
Cdd:cd14202    4 FSRKDLIGHGAFAVVFKGRHKEKHDLEVavkcinkKNLAKSQTLLGKEIK----ILKELKHENIVALYDFQEIANSVYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHEnpEGPAQLDwPKRLNIMRGASSglayMHQICEPHIVHRDIKSSNILLD---------GNFKAYVA 946
Cdd:cd14202   80 MEYCNGGDLADYLHT--MRTLSED-TIRLFLQQIAGA----MKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  947 DFGLSRLIlpYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSR 1014
Cdd:cd14202  153 DFGFARYL--QNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLR 218
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
809-1002 2.57e-14

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: 74.61  E-value: 2.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKL---TGDYGMMEKEFKaEVEVLSRAK---HENLVALQGYCV-----HDSARILIY 876
Cdd:cd07863    8 IGVGAYGTVYKArDPHSGHFVALKSVrvqTNEDGLPLSTVR-EVALLKRLEafdHPNIVRLMDVCAtsrtdRETKVTLVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENgSLDYWLHENPegPAQLDWPKRLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYVADFGLSRLilp 956
Cdd:cd07863   87 EHVDQ-DLRTYLDKVP--PPGLPAETIKDLMRQFLRGLDFLHANC---IVHRDLKPENILVTSGGQVKLADFGLARI--- 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425  957 YRTHVT-TELVGTLGYIPPE-YGQAWVATlRGDVYSFGVVMLELLTGK 1002
Cdd:cd07863  158 YSCQMAlTPVVVTLWYRAPEvLLQSTYAT-PVDMWSVGCIFAEMFRRK 204
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
830-1077 2.60e-14

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. 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 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-C 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: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 74.54  E-value: 2.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  830 VKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWLHEN---PEGpAQLDWPKRLNI 906
Cdd:cd14044   36 LKDLKNNEGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKisyPDG-TFMDWEFKISV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  907 MRGASSGLAYMH-QICEphiVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTelvgtlgyipPEYGQAWVATLR 985
Cdd:cd14044  115 MYDIAKGMSYLHsSKTE---VHGRLKSTNCVVDSRMVVKITDFGCNSILPPSKDLWTA----------PEHLRQAGTSQK 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  986 GDVYSFGVVMLELLTGKrpmEVFRPKMSRELVAWVHTMKRDGKPEEVFDTLLRESGNEEAMlRVLDIACMCVNQNPMKRP 1065
Cdd:cd14044  182 GDVYSYGIIAQEIILRK---ETFYTAACSDRKEKIYRVQNPKGMKPFRPDLNLESAGERER-EVYGLVKNCWEEDPEKRP 257
                        250
                 ....*....|..
gi 15218425 1066 NIQQVVDWLKNI 1077
Cdd:cd14044  258 DFKKIENTLAKI 269
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
825-1080 2.70e-14

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. 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 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-A/B 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: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 74.55  E-value: 2.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  825 GTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVhDSARILIysFME---NGSLDYWLhENPEgpAQLDWP 901
Cdd:cd14042   30 GNLVAIKKVNKKRIDLTREVLKELKHMRDLQHDNLTRFIGACV-DPPNICI--LTEycpKGSLQDIL-ENED--IKLDWM 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  902 KRLNIMRGASSGLAYMHqiCEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL----ILPYRTHVTT--------ELVgTL 969
Cdd:cd14042  104 FRYSLIHDIVKGMHYLH--DSEIKSHGNLKSSNCVVDSRFVLKITDFGLHSFrsgqEPPDDSHAYYakllwtapELL-RD 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  970 GYIPPEygqawvATLRGDVYSFGVVMLELLTGKRPMEVFRPKMS-RELVAWVHTMKRDG--KPEevfdtLLRESGNEEam 1046
Cdd:cd14042  181 PNPPPP------GTQKGDVYSFGIILQEIATRQGPFYEEGPDLSpKEIIKKKVRNGEKPpfRPS-----LDELECPDE-- 247
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15218425 1047 lrVLDIACMCVNQNPMKRPNIQQVVDWLKNIEAE 1080
Cdd:cd14042  248 --VLSLMQRCWAEDPEERPDFSTLRNKLKKLNKG 279
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
802-1072 2.91e-14

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: 73.96  E-value: 2.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT--LDnGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAK---HENLVALQGYCVHDSARILIY 876
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRskVD-GCLYAVKKSKKPFRGPKERARALREVEAHAAlgqHPNIVRYYSSWEEGGHLYIQM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHENPEgPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLD--GNFKayVADFGLSrli 954
Cdd:cd13997   80 ELCENGSLQDALEELSP-ISKLSEAEVWDLLLQVALGLAFIH---SKGIVHLDIKPDNIFISnkGTCK--IGDFGLA--- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 lpYRTHVT-TELVGTLGYIPPEYGQAWVATL-RGDVYSFGVVMLELLTGKrpmevfrpKMSRELVAWVHTmkRDGKPeev 1032
Cdd:cd13997  151 --TRLETSgDVEEGDSRYLAPELLNENYTHLpKADIFSLGVTVYEAATGE--------PLPRNGQQWQQL--RQGKL--- 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 15218425 1033 fdTLLRESGNEEAMLRVLDiacMCVNQNPMKRPNIQQVVD 1072
Cdd:cd13997  216 --PLPPGLVLSQELTRLLK---VMLDPDPTRRPTADQLLA 250
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
802-1071 3.04e-14

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 74.42  E-value: 3.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKATL------DNGTKLAVKKLTG-DYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARIL 874
Cdd:cd05046    6 NLQEITTLGRGEFGEVFLAKAkgieeeGGETLVLVKALQKtKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYWL-----HENPEGPAQLDWPKRLNIMRGASSGlayMHQICEPHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd05046   86 ILEYTDLGDLKQFLratksKDEKLKPPPLSTKQKVALCTQIALG---MDHLSNARFVHRDLAARNCLVSSQREVKVSLLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  950 LSRLILPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMK---- 1024
Cdd:cd05046  163 LSKDVYNSEYYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELP---FYGLSDEEVLNRLQAGKlelp 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425 1025 -RDGKPEEVFDTLLResgneeamlrvldiacmCVNQNPMKRPNIQQVV 1071
Cdd:cd05046  240 vPEGCPSRLYKLMTR-----------------CWAVNPKDRPSFSELV 270
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
803-1017 3.65e-14

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: 74.29  E-value: 3.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLV----YKATldnGTKLAVKKLTGDYGMMEK-EFKA--EVEVLSRAKHENLVALQ-GYCVHDsARIL 874
Cdd:cd05630    2 FRQYRVLGKGGFGEVcacqVRAT---GKMYACKKLEKKRIKKRKgEAMAlnEKQILEKVNSRFVVSLAyAYETKD-ALCL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYWLHEnpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd05630   78 VLTLMNGGDLKFHIYH--MGQAGFPEARAVFYAAEICCGLEDLHR---ERIVYRDLKPENILLDDHGHIRISDLGLAVHV 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  955 LPYRThvTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELV 1017
Cdd:cd05630  153 PEGQT--IKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEV 213
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
812-1065 4.19e-14

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 73.69  E-value: 4.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  812 GGFGLVYKATLDNGTKLAVKklTGDYGMMEKEFKA----EVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd14027    4 GGFGKVSLCFHRTQGLVVLK--TVYTGPNCIEHNEalleEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LhENPEGPAQLDWPKRLNIMRGassgLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGL------SRL------IL 955
Cdd:cd14027   82 L-KKVSVPLSVKGRIILEIIEG----MAYLH---GKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSKLtkeehnEQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 PYRTHVTTELVGTLGYIPPEYGQAWVA--TLRGDVYSFGVVMLELLTGKRPMEVFRPKMSrelvaWVHTMKRDGKPEEvf 1033
Cdd:cd14027  154 REVDGTAKKNAGTLYYMAPEHLNDVNAkpTEKSDVYSFAIVLWAIFANKEPYENAINEDQ-----IIMCIKSGNRPDV-- 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 15218425 1034 dtllrESGNEEAMLRVLDIACMCVNQNPMKRP 1065
Cdd:cd14027  227 -----DDITEYCPREIIDLMKLCWEANPEARP 253
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
809-1005 6.07e-14

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: 73.48  E-value: 6.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTgdygmMEKEFKA-------EVEVLSRAKHENLVALQGyCVHDSARI-LIYSFm 879
Cdd:cd07835    7 IGEGTYGVVYKArDKLTGEIVALKKIR-----LETEDEGvpstairEISLLKELNHPNIVRLLD-VVHSENKLyLVFEF- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 engsLDywlhenpegpaqLDWPKRLN----IMRGASSGLAYMHQI------CEPH-IVHRDIKSSNILLD--GNFKayVA 946
Cdd:cd07835   80 ----LD------------LDLKKYMDssplTGLDPPLIKSYLYQLlqgiafCHSHrVLHRDLKPQNLLIDteGALK--LA 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  947 DFGLSRLI-LPYRTHvTTELVgTLGYIPPE--YGQAWVATlRGDVYSFGVVMLELLTgKRPM 1005
Cdd:cd07835  142 DFGLARAFgVPVRTY-THEVV-TLWYRAPEilLGSKHYST-PVDIWSVGCIFAEMVT-RRPL 199
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
829-1076 6.31e-14

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 73.59  E-value: 6.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  829 AVKKLT-----GDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYsfMENG--SLD------YWLHENPEGP 895
Cdd:cd14001   32 AVKKINskcdkGQRSLYQERLKEEAKILKSLNHPNIVGFRAFTKSEDGSLCLA--MEYGgkSLNdlieerYEAGLGPFPA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  896 AQLdwpkrLNIMRGASSGLAYMHQicEPHIVHRDIKSSNILLDGNFKAY-VADFGLSrliLPYRTHVTTELVGTLGYI-- 972
Cdd:cd14001  110 ATI-----LKVALSIARALEYLHN--EKKILHGDIKSGNVLIKGDFESVkLCDFGVS---LPLTENLEVDSDPKAQYVgt 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  973 ----PPE-YGQAWVATLRGDVYSFGVVMLELLTGKRPmevfrpkmsrelvawvHTMKRDGKPEEVFDTLLRESGNEEAML 1047
Cdd:cd14001  180 epwkAKEaLEEGGVITDKADIFAYGLVLWEMMTLSVP----------------HLNLLDIEDDDEDESFDEDEEDEEAYY 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425 1048 -------------------RVLDIACMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd14001  244 gtlgtrpalnlgelddsyqKVIELFYACTQEDPKDRPSAAHIVEALEA 291
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
807-1000 6.72e-14

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: 73.39  E-value: 6.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLV----YKATLDN-GTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSAR--ILIYSFM 879
Cdd:cd05081   10 SQLGKGNFGSVelcrYDPLGDNtGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRRslRLVMEYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSLDYWLHENPegpAQLDwPKRLnimrgassgLAYMHQICE-------PHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd05081   90 PSGCLRDFLQRHR---ARLD-ASRL---------LLYSSQICKgmeylgsRRCVHRDLAARNILVESEAHVKIADFGLAK 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  953 LILPYRTHVTTELVGT--LGYIPPEYGQAWVATLRGDVYSFGVVMLELLT 1000
Cdd:cd05081  157 LLPLDKDYYVVREPGQspIFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
802-1004 7.43e-14

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: 73.02  E-value: 7.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDyGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFM 879
Cdd:cd14193    5 NVNKEEILGGGRFGQVHKCEeKSSGLKLAAKIIKAR-SQKEKEeVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSL-DYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL---DGNfKAYVADFGLSRLIL 955
Cdd:cd14193   84 DGGELfDRIIDEN----YNLTELDTILFIKQICEGIQYMHQM---YILHLDLKPENILCvsrEAN-QVKIIDFGLARRYK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425  956 PyRTHVTTELvGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14193  156 P-REKLRVNF-GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSP 202
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
809-1015 7.50e-14

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: 73.33  E-value: 7.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEFKA---EVEVLSRAKHENLVALqGYCVHDSARI-LIYSFMENGS 883
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMyACKKLDKKRIKKKKGETMalnEKIILEKVSSPFIVSL-AYAFETKDKLcLVLTLMNGGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYwlHENPEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSrLILPYRTHvTT 963
Cdd:cd05577   80 LKY--HIYNVGTRGFSEARAIFYAAEIICGLEHLHNR---FIVYRDLKPENILLDDHGHVRISDLGLA-VEFKGGKK-IK 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  964 ELVGTLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRE 1015
Cdd:cd05577  153 GRVGTHGYMAPEVLQKEVAyDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKE 205
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
809-1006 8.04e-14

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: 72.82  E-value: 8.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVK----KLTGDYGMMEkEFKAEVEVLSRAKHENLVALQGyCVHDSARI-LIYSFMENG 882
Cdd:cd14663    8 LGEGTFAKVKFArNTKTGESVAIKiidkEQVAREGMVE-QIKREIAIMKLLRHPNIVELHE-VMATKTKIfFVMELVTGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLD--GNFKayVADFGLSRLILPYRT- 959
Cdd:cd14663   86 ELFSKIAKN----GRLKEDKARKYFQQLIDAVDYCHS---RGVFHRDLKPENLLLDedGNLK--ISDFGLSALSEQFRQd 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  960 ---HVTtelVGTLGYIPPEygqawVATLRG------DVYSFGVVMLELLTGKRPME 1006
Cdd:cd14663  157 gllHTT---CGTPNYVAPE-----VLARRGydgakaDIWSCGVILFVLLAGYLPFD 204
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
802-1078 9.20e-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: 72.75  E-value: 9.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTgDYGMMEKEFK----AEVEVLSRAKHENLVALQGYCVHDSARILIY 876
Cdd:cd08228    3 NFQIEKKIGRGQFSEVYRATcLLDRKPVALKKVQ-IFEMMDAKARqdcvKEIDLLKQLNHPNVIKYLDSFIEDNELNIVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLD----YWLHENPEGPAQLDWPKRLNImrgaSSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd08228   82 ELADAGDLSqmikYFKKQKRLIPERTVWKYFVQL----CSAVEHMHS---RRVMHRDIKPANVFITATGVVKLGDLGLGR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  953 LiLPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMevFRPKMSreLVAWVHTMKRDGKPeev 1032
Cdd:cd08228  155 F-FSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF--YGDKMN--LFSLCQKIEQCDYP--- 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15218425 1033 fdTLLRESGNEeamlRVLDIACMCVNQNPMKRPNIQQVVDWLKNIE 1078
Cdd:cd08228  227 --PLPTEHYSE----KLRELVSMCIYPDPDQRPDIGYVHQIAKQMH 266
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
809-1004 9.47e-14

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: 73.03  E-value: 9.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVY-KATLDNGTKLAVKKLTGDYGMMEKE-FKAEVEVLSRAKHENLVAL------QGYCVHDsARILIYSFME 880
Cdd:cd14039    1 LGTGGFGNVClYQNQETGEKIAIKSCRLELSVKNKDrWCHEIQIMKKLNHPNVVKAcdvpeeMNFLVND-VPLLAMEYCS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHEnPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL---DGNFKAYVADFGLSRLIlpY 957
Cdd:cd14039   80 GGDLRKLLNK-PENCCGLKESQVLSLLSDIGSGIQYLH---ENKIIHRDLKPENIVLqeiNGKIVHKIIDLGYAKDL--D 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425  958 RTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14039  154 QGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRP 200
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
814-1070 1.24e-13

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 72.74  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  814 FGLVYKATL-----DNGTKLAVKKLTgDYGMMEK--EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDY 886
Cdd:cd05090   18 FGKIYKGHLylpgmDHAQLVAIKTLK-DYNNPQQwnEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WL-------------HENPEGPAQLDWPKRLNIMRGASSGLAYMhqiCEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd05090   97 FLimrsphsdvgcssDEDGTVKSSLDHGDFLHIAIQIAAGMEYL---SSHFFVHKDLAARNILVGEQLHVKISDLGLSRE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  954 ILP---YRTHVTTELvgTLGYIPPE---YGQawvATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELVawvhtMKRD 1026
Cdd:cd05090  174 IYSsdyYRVQNKSLL--PIRWMPPEaimYGK---FSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMV-----RKRQ 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15218425 1027 GKPeevfdtllresGNEEAMLRVLDIACMCVNQNPMKRPNIQQV 1070
Cdd:cd05090  244 LLP-----------CSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
809-1006 1.31e-13

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: 71.91  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEF---KAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd14161   11 LGKGTYGRVKKARDSSGRLVAIKSIRKDRIKDEQDLlhiRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDLY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLilpYRT------ 959
Cdd:cd14161   91 DYISER----QRLSELEARHFFRQIVSAVHYCHA---NGIVHRDLKLENILLDANGNIKIADFGLSNL---YNQdkflqt 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  960 ------HVTTELVGTLGYIPPEYgqawvatlrgDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14161  161 ycgsplYASPEIVNGRPYIGPEV----------DSWSLGVLLYILVHGTMPFD 203
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
801-1018 1.45e-13

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 73.16  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTG--DYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHleIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENPEGPAQLDWPKRLNIMRGassgLAYMHQicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILpyr 958
Cdd:cd06649   85 MDGGSLDQVLKEAKRIPEEILGKVSIAVLRG----LAYLRE--KHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  959 THVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEvfrPKMSRELVA 1018
Cdd:cd06649  156 DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIP---PPDAKELEA 212
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
809-1006 1.64e-13

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: 71.90  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVyKATLDNGT--KLAVKkltgdygMMEKEF-----------KAEVEVLSRAKHENLVALQGYcVHDSARILI 875
Cdd:cd14119    1 LGEGSYGKV-KEVLDTETlcRRAVK-------ILKKRKlrripngeanvKREIQILRRLNHRNVIKLVDV-LYNEEKQKL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFME--NGSLDYWLHENPEgpaqldwpKRLNIMRGAS------SGLAYMHQIcepHIVHRDIKSSNILL--DGNFKayV 945
Cdd:cd14119   72 YMVMEycVGGLQEMLDSAPD--------KRLPIWQAHGyfvqliDGLEYLHSQ---GIIHKDIKPGNLLLttDGTLK--I 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  946 ADFGLSRLILPY-RTHVTTELVGTLGYIPPE--YGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14119  139 SDFGVAEALDLFaEDDTCTTSQGSPAFQPPEiaNGQDSFSGFKVDIWSAGVTLYNMTTGKYPFE 202
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
809-1074 1.81e-13

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: 71.71  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVK---KLTGDYGMMEKEFKAEVEV-----------LSRA-KHENLVALQGYCVHDSAR 872
Cdd:cd14077    9 IGAGSMGKVKLAKhIRTGEKCAIKiipRASNAGLKKEREKRLEKEIsrdirtireaaLSSLlNHPHICRLRDFLRTPNHY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 ILIYSFMENGS-LDYWLHENP--EGPAQldwpkrlNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd14077   89 YMLFEYVDGGQlLDYIISHGKlkEKQAR-------KFARQIASALDYLHR---NSIVHRDLKIENILISKSGNIKIIDFG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  950 LSRLiLPYRTHVTTeLVGTLGYIPPEYGQAWVATlrG---DVYSFGVVMLELLTGKRP-----MEVFRPKMSRELVAWVH 1021
Cdd:cd14077  159 LSNL-YDPRRLLRT-FCGSLYFAAPELLQAQPYT--GpevDVWSFGVVLYVLVCGKVPfddenMPALHAKIKKGKVEYPS 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425 1022 TMKRDGKpeevfdTLLResgneeAMLRVldiacmcvnqNPMKRPNIQQVVD--WL 1074
Cdd:cd14077  235 YLSSECK------SLIS------RMLVV----------DPKKRATLEQVLNhpWM 267
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
809-1030 2.72e-13

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: 71.11  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVA-LQGYCVHDSARILIySFMENGSLDY 886
Cdd:cd06647   15 IGQGASGTVYTAIdVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVM-EYLAGGSLTD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHEnpegpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILL--DGNFKayVADFGLSRLILPYRTHVTTe 964
Cdd:cd06647   94 VVTE-----TCMDEGQIAAVCRECLQALEFLHS---NQVIHRDIKSDNILLgmDGSVK--LTDFGFCAQITPEQSKRST- 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  965 LVGTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvhtmkRDGKPE 1030
Cdd:cd06647  163 MVGTPYWMAPEvvtrkaYGP------KVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA------TNGTPE 222
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
809-1070 2.74e-13

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: 71.12  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL--DNgTKLAVKK----LTGDygmMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd05084    4 IGRGNFGEVFSGRLraDN-TPVAVKScretLPPD---LKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHEnpEGPaQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlilpYRTHVT 962
Cdd:cd05084   80 DFLTFLRT--EGP-RLKVKELIRMVENAAAGMEYLES---KHCIHRDLAARNCLVTEKNVLKISDFGMSR----EEEDGV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  963 TELVGTLGYIP-----PE---YGQawvATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELVAW-VHTMKRDGKPEEV 1032
Cdd:cd05084  150 YAATGGMKQIPvkwtaPEalnYGR---YSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAVEQgVRLPCPENCPDEV 226
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15218425 1033 FDTLLResgneeamlrvldiacmCVNQNPMKRPNIQQV 1070
Cdd:cd05084  227 YRLMEQ-----------------CWEYDPRKRPSFSTV 247
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
809-1010 2.94e-13

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: 71.60  E-value: 2.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd06644   20 LGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEdYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAVDAI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHENPEGpaqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL--DGNFKayVADFGLSR------------L 953
Cdd:cd06644  100 MLELDRG---LTEPQIQVICRQMLEALQYLHSM---KIIHRDLKAGNVLLtlDGDIK--LADFGVSAknvktlqrrdsfI 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  954 ILPYRTHVTTELVGTLGYIPPEYgqawvatlRGDVYSFGVVMLELLTGKRPMEVFRP 1010
Cdd:cd06644  172 GTPYWMAPEVVMCETMKDTPYDY--------KADIWSLGITLIEMAQIEPPHHELNP 220
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
807-1004 2.99e-13

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: 71.58  E-value: 2.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKA-TLDNGTKLAVK--KLTGDygmMEKEFKA--------EVEVLSRAKHENLVALQGYCVHDSARIL- 874
Cdd:cd13990    6 NLLGKGGFSEVYKAfDLVEQRYVACKihQLNKD---WSEEKKQnyikhalrEYEIHKSLDHPRIVKLYDVFEIDTDSFCt 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYWLHEN---PEGPAQLdwpkrlnIMRGASSGLAYMHQIcEPHIVHRDIKSSNILLD-----GNFKayVA 946
Cdd:cd13990   83 VLEYCDGNDLDFYLKQHksiPEREARS-------IIMQVVSALKYLNEI-KPPIIHYDLKPGNILLHsgnvsGEIK--IT 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  947 DFGLSRLI-----LPYRTHVTTELVGTLGYIPPEygqawvATLRG----------DVYSFGVVMLELLTGKRP 1004
Cdd:cd13990  153 DFGLSKIMddesyNSDGMELTSQGAGTYWYLPPE------CFVVGktppkisskvDVWSVGVIFYQMLYGRKP 219
PLN03150 PLN03150
hypothetical protein; Provisional
33-215 3.05e-13

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 74.08  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425    33 VLSISVFFLTVSEAVCNLQDRDSLLWFSGNVSSPvSPLHWNSsiDCCS-----WEGISC--DKSPENRVTSII-LSSRGL 104
Cdd:PLN03150  354 INAIEVFEIITAESKTLLEEVSALQTLKSSLGLP-LRFGWNG--DPCVpqqhpWSGADCqfDSTKGKWFIDGLgLDNQGL 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   105 SGNLPSSVLDLQRLSRLDLSHNRLSGPLPPGFLSaLDQLLVLDLSYNSFKGELPlqQSFGNgsngIFPIQTVDLSSNLLE 184
Cdd:PLN03150  431 RGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGS-ITSLEVLDLSYNSFNGSIP--ESLGQ----LTSLRILNLNGNSLS 503
                         170       180       190
                  ....*....|....*....|....*....|...
gi 15218425   185 GEILSS--SVFLQGAfnltSFNVSNNSFTGSIP 215
Cdd:PLN03150  504 GRVPAAlgGRLLHRA----SFNFTDNAGLCGIP 532
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
802-1079 3.05e-13

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: 71.60  E-value: 3.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTgDYGMMEKEFKA----EVEVLSRAKHENLVALQGYCVHDSARILIY 876
Cdd:cd08229   25 NFRIEKKIGRGQFSEVYRATcLLDGVPVALKKVQ-IFDLMDAKARAdcikEIDLLKQLNHPNVIKYYASFIEDNELNIVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHENPEG----PAQLDWPKRLNImrgaSSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd08229  104 ELADAGDLSRMIKHFKKQkrliPEKTVWKYFVQL----CSALEHMHS---RRVMHRDIKPANVFITATGVVKLGDLGLGR 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  953 LiLPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMevFRPKMS-RELVAWVHTMKRDGKPEE 1031
Cdd:cd08229  177 F-FSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF--YGDKMNlYSLCKKIEQCDYPPLPSD 253
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425 1032 VFDTLLRESGNeeamlrvldiacMCVNQNPMKRPNIQQVVDWLKNIEA 1079
Cdd:cd08229  254 HYSEELRQLVN------------MCINPDPEKRPDITYVYDVAKRMHA 289
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
796-1006 3.16e-13

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 71.98  E-value: 3.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  796 LLKATDnFSQANIIGCGGFGLVYKAT-LDNGTKL----AVKKL-TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVhD 869
Cdd:cd05108    3 ILKETE-FKKIKVLGSGAFGTVYKGLwIPEGEKVkipvAIKELrEATSPKANKEILDEAYVMASVDNPHVCRLLGICL-T 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  870 SARILIYSFMENGSLDYWLHENPE---GPAQLDWPKRLnimrgaSSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVA 946
Cdd:cd05108   81 STVQLITQLMPFGCLLDYVREHKDnigSQYLLNWCVQI------AKGMNYLE---DRRLVHRDLAARNVLVKTPQHVKIT 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  947 DFGLSRLIlpyrTHVTTELVGTLGYIPPEYGQ-----AWVATLRGDVYSFGVVMLELLT-GKRPME 1006
Cdd:cd05108  152 DFGLAKLL----GAEEKEYHAEGGKVPIKWMAlesilHRIYTHQSDVWSYGVTVWELMTfGSKPYD 213
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
809-1074 3.54e-13

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: 70.88  E-value: 3.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAV------KKLTGDYGMMEKEFK---AEVEVLSRAK---HENLVALqgycvhdsariliY 876
Cdd:cd14004    8 MGEGAYGQVNLAIYKSKGKEVVikfifkERILVDTWVRDRKLGtvpLEIHILDTLNkrsHPNIVKL-------------L 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENgSLDYWLHENPEGPA-----------QLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYV 945
Cdd:cd14004   75 DFFED-DEFYYLVMEKHGSGmdlfdfierkpNMDEKEAKYIFRQVADAVKHLH---DQGIVHRDIKDENVILDGNGTIKL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  946 ADFGLSRLILPYRTHVtteLVGTLGYIPPEygqawvaTLRG--------DVYSFGVVMLELLTGKRPM-EVfrpkmsrel 1016
Cdd:cd14004  151 IDFGSAAYIKSGPFDT---FVGTIDYAAPE-------VLRGnpyggkeqDIWALGVLLYTLVFKENPFyNI--------- 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425 1017 vawVHTMKRDGKPEEVFdtllresgNEEAMlrvlDIACMCVNQNPMKRPNIQQVVD--WL 1074
Cdd:cd14004  212 ---EEILEADLRIPYAV--------SEDLI----DLISRMLNRDVGDRPTIEELLTdpWL 256
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
809-1008 3.81e-13

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: 71.09  E-value: 3.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYkatldngtkLAVKKLTGDY-------------GMMEKEFKAEVEVLSRAKHENLVALqgYCVHDSARILi 875
Cdd:cd05579    1 ISRGAYGRVY---------LAKKKSTGDLyaikvikkrdmirKNQVDSVLAERNILSQAQNPFVVKL--YYSFQGKKNL- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFME---NGSLdYWLHEN----PEGPAQldwpkrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADF 948
Cdd:cd05579   69 YLVMEylpGGDL-YSLLENvgalDEDVAR-------IYIAEIVLALEYLHSH---GIIHRDLKPDNILIDANGHLKLTDF 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  949 GLSRLIL--------------PYRTHVTTELVGTLGYIPPEygqawvaTLRGDVYSF-------GVVMLELLTG------ 1001
Cdd:cd05579  138 GLSKVGLvrrqiklsiqkksnGAPEKEDRRIVGTPDYLAPE-------ILLGQGHGKtvdwwslGVILYEFLVGippfha 210

                 ....*..
gi 15218425 1002 KRPMEVF 1008
Cdd:cd05579  211 ETPEEIF 217
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
855-1077 3.96e-13

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. 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 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-2D 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: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 70.90  E-value: 3.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  855 KHENLVALQGyCVHDSARI-LIYSFMENGSLDYWLhENPEgpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSS 933
Cdd:cd14043   54 RHENVNLFLG-LFVDCGILaIVSEHCSRGSLEDLL-RNDD--MKLDWMFKSSLLLDLIKGMRYLHH---RGIVHGRLKSR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  934 NILLDGNFKAYVADFGLSRLI----LPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPmevfr 1009
Cdd:cd14043  127 NCVVDGRFVLKITDYGYNEILeaqnLPLPEPAPEELLWTAPELLRDPRLERRGTFPGDVFSFAIIMQEVIVRGAP----- 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425 1010 pkmsrelvawvHTMkRDGKPEEVFDT------LLRES-GNEEAMLRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14043  202 -----------YCM-LGLSPEEIIEKvrspppLCRPSvSMDQAPLECIQLMKQCWSEAPERRPTFDQIFDQFKSI 264
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
809-1050 4.35e-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: 70.91  E-value: 4.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAtLDNGTKLAV-------KKLTGdygMMEKEFKAEVEVLSRAKHENLV----ALQGYCVHDSARILIYS 877
Cdd:cd14031   18 LGRGAFKTVYKG-LDTETWVEVawcelqdRKLTK---AEQQRFKEEAEMLKGLQHPNIVrfydSWESVLKGKKCIVLVTE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYWLhenpegpaqldwpKRLNIM---------RGASSGLAYMHQICEPhIVHRDIKSSNILLDG-NFKAYVAD 947
Cdd:cd14031   94 LMTSGTLKTYL-------------KRFKVMkpkvlrswcRQILKGLQFLHTRTPP-IIHRDLKCDNIFITGpTGSVKIGD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  948 FGLSRLIlpyRTHVTTELVGTLGYIPPE-YGQAWVATLrgDVYSFGVVMLELLTGKRP-------MEVFRpKMSRELVAW 1019
Cdd:cd14031  160 LGLATLM---RTSFAKSVIGTPEFMAPEmYEEHYDESV--DVYAFGMCMLEMATSEYPysecqnaAQIYR-KVTSGIKPA 233
                        250       260       270
                 ....*....|....*....|....*....|.
gi 15218425 1020 VHTMKRDGKPEEVFDTLLRESGNEEAMLRVL 1050
Cdd:cd14031  234 SFNKVTDPEVKEIIEGCIRQNKSERLSIKDL 264
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
803-1071 4.49e-13

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: 70.86  E-value: 4.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAtLDNGTKLAVKKLTGDYGMMEKEF---KAEVEVLSRAKHENLVALQGYCVHDSARILIYSFM 879
Cdd:cd06642    6 FTKLERIGKGSFGEVYKG-IDNRTKEVVAIKIIDLEEAEDEIediQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGS-LDYWlhenpeGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYR 958
Cdd:cd06642   85 GGGSaLDLL------KPGPLEETYIATILREILKGLDYLHS---ERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  959 THVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAWVHTMKRDGKPEEVFDtllr 1038
Cdd:cd06642  156 IKRNT-FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFK---- 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 15218425 1039 esgneeamlrvlDIACMCVNQNPMKRPNIQQVV 1071
Cdd:cd06642  231 ------------EFVEACLNKDPRFRPTAKELL 251
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
803-1004 4.56e-13

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: 70.42  E-value: 4.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANI-IGCGGFGLVYKAtLDNGTKLAV-------KKLTGdygMMEKEFKAEVEVLSRAKHENLV--------ALQGY- 865
Cdd:cd14033    2 FLKFNIeIGRGSFKTVYRG-LDTETTVEVawcelqtRKLSK---GERQRFSEEVEMLKGLQHPNIVrfydswksTVRGHk 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  866 CVhdsarILIYSFMENGSLDYWLHENPEGPAQL--DWPKRlnIMRGassgLAYMHQICEPhIVHRDIKSSNILLDG-NFK 942
Cdd:cd14033   78 CI-----ILVTELMTSGTLKTYLKRFREMKLKLlqRWSRQ--ILKG----LHFLHSRCPP-ILHRDLKCDNIFITGpTGS 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  943 AYVADFGLSRLilpYRTHVTTELVGTLGYIPPE-YGQAWVATLrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14033  146 VKIGDLGLATL---KRASFAKSVIGTPEFMAPEmYEEKYDEAV--DVYAFGMCILEMATSEYP 203
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
808-1006 5.22e-13

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: 70.39  E-value: 5.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFG---LVYKATLDNGTKLAVKKLTGDYGMMEKEFKaEVEVLSRAKHENLVALQgycvhdsariliYSFMENGSL 884
Cdd:cd08219    7 VVGEGSFGralLVQHVNSDQKYAMKEIRLPKSSSAVEDSRK-EAVLLAKMKHPNIVAFK------------ESFEADGHL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 dYWLHENPEGPaqlDWPKRLNIMRG----ASSGLAYMHQIC-------EPHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd08219   74 -YIVMEYCDGG---DLMQKIKLQRGklfpEDTILQWFVQMClgvqhihEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  954 ILPYRTHVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd08219  150 LTSPGAYACT-YVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQ 201
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
809-1010 5.35e-13

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: 70.83  E-value: 5.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYW 887
Cdd:cd06643   13 LGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEdYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  888 LHEnPEGPaqLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNIL--LDGNFKayVADFGLSrlILPYRT-HVTTE 964
Cdd:cd06643   93 MLE-LERP--LTEPQIRVVCKQTLEALVYLH---ENKIIHRDLKAGNILftLDGDIK--LADFGVS--AKNTRTlQRRDS 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425  965 LVGTLGYIPPEYGQAWVATLR-----GDVYSFGVVMLELLTGKRPMEVFRP 1010
Cdd:cd06643  163 FIGTPYWMAPEVVMCETSKDRpydykADVWSLGVTLIEMAQIEPPHHELNP 213
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
802-1070 5.73e-13

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: 70.11  E-value: 5.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLtgDYGMMEKEFKA----EVEVLSRAKHENLVAL-QGYCvhDSARILI 875
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKrLSDNQVYALKEV--NLGSLSQKEREdsvnEIRLLASVNHPNIIRYkEAFL--DGNRLCI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YS-FMENGSLDYWLHENPEG----PAQLDWPKRLNIMRGassgLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGL 950
Cdd:cd08530   77 VMeYAPFGDLSKLISKRKKKrrlfPEDDIWRIFIQMLRG----LKALH---DQKILHRDLKSANILLSAGDLVKIGDLGI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  951 SRLIlpyRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPmevFRPKMSRELVAWVHTMKRDGKPe 1030
Cdd:cd08530  150 SKVL---KKNLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPP---FEARTMQELRYKVCRGKFPPIP- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 15218425 1031 evfdtllreSGNEEAMLRVLDiacMCVNQNPMKRPNIQQV 1070
Cdd:cd08530  223 ---------PVYSQDLQQIIR---SLLQVNPKKRPSCDKL 250
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
843-1065 6.66e-13

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 70.38  E-value: 6.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  843 EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMenGSLDYWLHENPEGPAQLDWPKRLN--IMRGASSGLAYMHQi 920
Cdd:cd14067   56 EFRQEASMLHSLQHPCIVYLIGISIHPLCFALELAPL--GSLNTVLEENHKGSSFMPLGHMLTfkIAYQIAAGLAYLHK- 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  921 cePHIVHRDIKSSNIL---LDG----NFKayVADFGLSRlilpyrtHVTTELV----GTLGYIPPEYGQAWVATLRGDVY 989
Cdd:cd14067  133 --KNIIFCDLKSDNILvwsLDVqehiNIK--LSDYGISR-------QSFHEGAlgveGTPGYQAPEIRPRIVYDEKVDMF 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  990 SFGVVMLELLTGKRP-MEVFRPKMSRELVAWVHTMKrdGKPEEV----FDTLLRESGNEEAMLRVLdiACMCVNQnpMKR 1064
Cdd:cd14067  202 SYGMVLYELLSGQRPsLGHHQLQIAKKLSKGIRPVL--GQPEEVqffrLQALMMECWDTKPEKRPL--ACSVVEQ--MKD 275

                 .
gi 15218425 1065 P 1065
Cdd:cd14067  276 P 276
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
802-1008 6.72e-13

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: 70.07  E-value: 6.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMME--KEFKA---EVEVLSRAKHENLVALQGyCVHDSARILI 875
Cdd:cd06652    3 NWRLGKLLGQGAFGRVYLCyDADTGRELAVKQVQFDPESPEtsKEVNAlecEIQLLKNLLHERIVQYYG-CLRDPQERTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFME---NGSLDYWLheNPEGPAQLDWPKRLNimRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd06652   82 SIFMEympGGSIKDQL--KSYGALTENVTRKYT--RQILEGVHYLHS---NMIVHRDIKGANILRDSVGNVKLGDFGASK 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  953 LILPYRTHVT--TELVGTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRPMEVF 1008
Cdd:cd06652  155 RLQTICLSGTgmKSVTGTPYWMSPEvisgegYGR------KADIWSVGCTVVEMLTEKPPWAEF 212
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
803-1071 7.06e-13

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: 70.49  E-value: 7.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAtLDNGTKLAVKKLTGDYGMMEKEF---KAEVEVLSRAKHENLVALQGYCVHDSARILIYSFM 879
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKG-IDNRTQKVVAIKIIDLEEAEDEIediQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSLDYWLHenpegPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRT 959
Cdd:cd06641   85 GGGSALDLLE-----PGPLDETQIATILREILKGLDYLHS---EKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  960 HvTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvhtmkRDGKPeevfdtLLRe 1039
Cdd:cd06641  157 K-RN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIP------KNNPP------TLE- 222
                        250       260       270
                 ....*....|....*....|....*....|..
gi 15218425 1040 sGNEEAMLRVLDIACMcvNQNPMKRPNIQQVV 1071
Cdd:cd06641  223 -GNYSKPLKEFVEACL--NKEPSFRPTAKELL 251
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
807-1070 7.40e-13

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 70.07  E-value: 7.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLD-NGTKL-AVKKLTGDYGMME--KEFKAEVEVLSR-AKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd05047    1 DVIGEGNFGQVLKARIKkDGLRMdAAIKRMKEYASKDdhRDFAGELEVLCKlGHHPNIINLLGACEHRGYLYLAIEYAPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAY-------------MHQICEPHIVHRDIKSSNILLDGNFKAYVADF 948
Cdd:cd05047   81 GNLLDFLRKS----RVLETDPAFAIANSTASTLSSqqllhfaadvargMDYLSQKQFIHRDLAARNILVGENYVAKIADF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  949 GLSRLILPYrthvtteLVGTLGYIPPEygqaWVA---------TLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVA 1018
Cdd:cd05047  157 GLSRGQEVY-------VKKTMGRLPVR----WMAieslnysvyTTNSDVWSYGVLLWEIVSlGGTP---YCGMTCAELYE 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425 1019 WVHTMKRDGKPEEVFDtllresgneeamlRVLDIACMCVNQNPMKRPNIQQV 1070
Cdd:cd05047  223 KLPQGYRLEKPLNCDD-------------EVYDLMRQCWREKPYERPSFAQI 261
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
914-1007 7.71e-13

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 70.11  E-value: 7.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  914 LAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVGTLGYIPPEygqawvaTLRG------- 986
Cdd:cd05583  112 LEHLHKL---GIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYSFCGTIEYMAPE-------VVRGgsdghdk 181
                         90       100
                 ....*....|....*....|...
gi 15218425  987 --DVYSFGVVMLELLTGKRPMEV 1007
Cdd:cd05583  182 avDWWSLGVLTYELLTGASPFTV 204
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
808-1004 8.45e-13

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: 70.02  E-value: 8.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL-D 885
Cdd:cd14166   10 VLGSGAFSEVYLVKqRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELfD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHEN--PEGPAQldwpkrlNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL---DGNFKAYVADFGLSRLilpYRTH 960
Cdd:cd14166   90 RILERGvyTEKDAS-------RVINQVLSAVKYLH---ENGIVHRDLKPENLLYltpDENSKIMITDFGLSKM---EQNG 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14166  157 IMSTACGTPGYVAPEvlaqkpYSKAV------DCWSIGVITYILLCGYPP 200
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
788-1005 9.35e-13

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 70.46  E-value: 9.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  788 VKDLTIFELLKATDN---FSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLV 860
Cdd:cd06635    9 LKDPDIAELFFKEDPeklFSDLREIGHGSFGAVYFArDVRTSEVVAIKKMSYSGKQSNEKWQdiiKEVKFLQRIKHPNSI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  861 ALQGYCVHDSARILIYSFMENGSLDYW-LHENPEGPAQLdwpkrLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDG 939
Cdd:cd06635   89 EYKGCYLREHTAWLVMEYCLGSASDLLeVHKKPLQEIEI-----AAITHGALQGLAYLHS---HNMIHRDIKAGNILLTE 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  940 NFKAYVADFGLSRLILPyrthvTTELVGTLGYIPPEygqAWVATLRG------DVYSFGVVMLELLTGKRPM 1005
Cdd:cd06635  161 PGQVKLADFGSASIASP-----ANSFVGTPYWMAPE---VILAMDEGqydgkvDVWSLGITCIELAERKPPL 224
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
812-1066 9.39e-13

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: 69.65  E-value: 9.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  812 GGFGLVYKATlDNGTK--LAVKKLTGDygmmekEFK-AEVEVLSRAKHENLVALQGYCVHDSArilIYSFMENGSLDYWL 888
Cdd:cd13995   15 GAFGKVYLAQ-DTKTKkrMACKLIPVE------QFKpSDVEIQACFRHENIAELYGALLWEET---VHLFMEAGEGGSVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HE----NPEGPAQLDWPKRlNIMRgassGLAYMHQicePHIVHRDIKSSNILLDGNfKAYVADFGLSrLILPYRTHVTTE 964
Cdd:cd13995   85 EKlescGPMREFEIIWVTK-HVLK----GLDFLHS---KNIIHHDIKPSNIVFMST-KAVLVDFGLS-VQMTEDVYVPKD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRElvAWVHTMKRDGKP-EEVFDTLlresgnE 1043
Cdd:cd13995  155 LRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYP--SYLYIIHKQAPPlEDIAQDC------S 226
                        250       260
                 ....*....|....*....|...
gi 15218425 1044 EAMLRVLDIAcmcVNQNPMKRPN 1066
Cdd:cd13995  227 PAMRELLEAA---LERNPNHRSS 246
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
802-1002 9.97e-13

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: 69.82  E-value: 9.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKA-TLDNGTKLAVK--KLTGDYGMMEKEFKaEVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd07836    1 NFKQLEKLGEGTYATVYKGrNRTTGEIVALKeiHLDAEEGTPSTAIR-EISLMKELKHENIVRLHDVIHTENKLMLVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENPEGPAQLDWPKrlNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLI-LPY 957
Cdd:cd07836   80 MDKDLKKYMDTHGVRGALDPNTVK--SFTYQLLKGIAFCH---ENRVLHRDLKPQNLLINKRGELKLADFGLARAFgIPV 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425  958 RThVTTELVgTLGYIPPE--YGQAWVATlRGDVYSFGVVMLELLTGK 1002
Cdd:cd07836  155 NT-FSNEVV-TLWYRAPDvlLGSRTYST-SIDIWSVGCIMAEMITGR 198
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
809-1004 1.05e-12

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: 69.53  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL--- 884
Cdd:cd14114   10 LGTGAFGVVHRCTeRATGNNFAAKFIMTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGELfer 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 ----DYWLHENpegpaqldwpKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVA--DFGLSRLILPYR 958
Cdd:cd14114   90 iaaeHYKMSEA----------EVINYMRQVCEGLCHMH---ENNIVHLDIKPENIMCTTKRSNEVKliDFGLATHLDPKE 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425  959 T-HVTTelvGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14114  157 SvKVTT---GTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSP 200
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
426-666 1.14e-12

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.12  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  426 NKMTNLTGALSILQGCKKLSTLIMAKNFYDETVPSNKDFLRSDGFPSLQIFGIGACRLTGEIPAWLIKLQRVEVMDLSMN 505
Cdd:COG4886    3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  506 RFVGTIPGWLGTLPDLFYLDLSDNfltgelpKELFQLRALmsqKAYDATERNYLELPVFV-NPNNVTT-NQQYNQLSSLP 583
Cdd:COG4886   83 SLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNL---ESLDLSGNQLTDLPEELaNLTNLKElDLSNNQLTDLP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  584 PTI---------YIKRNNLTgTIPVEVGQLKVLHILELLGNNFSgSIPDELSNLTNLERLDLSNNNLSgRIPWSLTGLHF 654
Cdd:COG4886  153 EPLgnltnlkslDLSNNQLT-DLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANLTN 229
                        250
                 ....*....|..
gi 15218425  655 LSYFNVANNTLS 666
Cdd:COG4886  230 LETLDLSNNQLT 241
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
793-1071 1.19e-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: 69.65  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  793 IFELLKatdnfsqanIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSR-AKHENLVALQGYCV---- 867
Cdd:cd06636   17 IFELVE---------VVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKySHHRNIATYYGAFIkksp 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  868 --HDSARILIYSFMENGSLDYWLHENPEGPAQLDWPKRlnIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYV 945
Cdd:cd06636   88 pgHDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAY--ICREILRGLAHLHA---HKVIHRDIKGQNVLLTENAEVKL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  946 ADFGLSRLiLPYRTHVTTELVGTLGYIPPEY-----GQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwv 1020
Cdd:cd06636  163 VDFGVSAQ-LDRTVGRRNTFIGTPYWMAPEViacdeNPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIP-- 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425 1021 htmkRDGKPEevfdtlLRESGNEEAMLRVLDiacMCVNQNPMKRPNIQQVV 1071
Cdd:cd06636  240 ----RNPPPK------LKSKKWSKKFIDFIE---GCLVKNYLSRPSTEQLL 277
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
808-1018 1.29e-12

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: 69.94  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEF---KAEVEVLSRA-KHENLVALQGyCVHDSARIliYSFME-- 880
Cdd:cd05570    2 VLGKGSFGKVMLAERKKTDELyAIKVLKKEVIIEDDDVectMTEKRVLALAnRHPFLTGLHA-CFQTEDRL--YFVMEyv 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 -NGSLDYWLHENpegpaqldwpKRLNIMRGA------SSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd05570   79 nGGDLMFHIQRA----------RRFTEERARfyaaeiCLALQFLH---ERGIIYRDLKLDNVLLDAEGHIKIADFGMCKE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  954 -ILPYRThvTTELVGTLGYIPPE------YGQAwVatlrgDVYSFGVVMLELLTGKRPM------EVFR----------P 1010
Cdd:cd05570  146 gIWGGNT--TSTFCGTPDYIAPEilreqdYGFS-V-----DWWALGVLLYEMLAGQSPFegddedELFEailndevlypR 217

                 ....*...
gi 15218425 1011 KMSRELVA 1018
Cdd:cd05570  218 WLSREAVS 225
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
809-1001 1.40e-12

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: 69.71  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKL--TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd07847    9 IGEGSYGVVFKCrNRETGQIVAIKKFveSEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDHTVLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YwLHENPEGpaqLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP----YRTHV 961
Cdd:cd07847   89 E-LEKNPRG---VPEHLIKKIIWQTLQAVNFCHK---HNCIHRDVKPENILITKQGQIKLCDFGFARILTGpgddYTDYV 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425  962 TTE-------LVGTLGYIPPEygqawvatlrgDVYSFGVVMLELLTG 1001
Cdd:cd07847  162 ATRwyrapelLVGDTQYGPPV-----------DVWAIGCVFAELLTG 197
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
817-1004 1.49e-12

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: 69.17  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  817 VYKATLDngtKLAVK--KLTGDYGMMEKEFK-------AEVEVLSR-AKHENLVALQGYCVHDSARILIYSFMENGSLDY 886
Cdd:cd14182   23 IHKPTRQ---EYAVKiiDITGGGSFSPEEVQelreatlKEIDILRKvSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENpegpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRThvTTELV 966
Cdd:cd14182  100 YLTEK----VTLSEKETRKIMRALLEVICALHKL---NIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEK--LREVC 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  967 GTLGYIPPE------------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14182  171 GTPGYLAPEiiecsmddnhpgYGKEV------DMWSTGVIMYTLLAGSPP 214
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
809-1071 1.62e-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: 69.07  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNG--TKLAVKKL---TGDYGMMEKE-------FKAEVEVL-SRAKHENLVALQGYCVHDSARILI 875
Cdd:cd08528    8 LGSGAFGCVYKVRKKSNgqTLLALKEInmtNPAFGRTEQErdksvgdIISEVNIIkEQLRHPNIVRYYKTFLENDRLYIV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL 955
Cdd:cd08528   88 MELIEGAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHK--EKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQKG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 PYRTHVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPmevFRPKMSRELVAWVHTMKRDGKPEEVFDT 1035
Cdd:cd08528  166 PESSKMTS-VVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPP---FYSTNMLTLATKIVEAEYEPLPEGMYSD 241
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 15218425 1036 LLResgneeamlrvlDIACMCVNQNPMKRPNIQQVV 1071
Cdd:cd08528  242 DIT------------FVIRSCLTPDPEARPDIVEVS 265
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
801-1004 1.66e-12

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: 70.81  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE----FKAEVEVLSRAKHENLVALQgYCVHDSARI-LI 875
Cdd:cd05624   72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAetacFREERNVLVNGDCQWITTLH-YAFQDENYLyLV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHENPEgpaqlDWPKRLNIMRGASSGLAyMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL 955
Cdd:cd05624  151 MDYYVGGDLLTLLSKFED-----KLPEDMARFYIGEMVLA-IHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMN 224
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425  956 PYRTHVTTELVGTLGYIPPEYGQAWVATL-----RGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05624  225 DDGTVQSSVAVGTPDYISPEILQAMEDGMgkygpECDWWSLGVCMYEMLYGETP 278
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
808-1072 1.66e-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: 68.61  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFG--LVYKATLDNgtKLAVKKLTGDYGMMEKEFKA---EVEVLSRAKHENLVAlqgYCVHdsariliysFMENG 882
Cdd:cd08221    7 VLGRGAFGeaVLYRKTEDN--SLVVWKEVNLSRLSEKERRDalnEIDILSLLNHDNIIT---YYNH---------FLDGE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLhENPEGPAQLDwpkRLNIMRG----ASSGLAYMHQIC-------EPHIVHRDIKSSNILLDGNFKAYVADFGLS 951
Cdd:cd08221   73 SLFIEM-EYCNGGNLHD---KIAQQKNqlfpEEVVLWYLYQIVsavshihKAGILHRDIKTLNIFLTKADLVKLGDFGIS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  952 RlILPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRP-KMSRELVawvhtmkrDGKpe 1030
Cdd:cd08221  149 K-VLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPlRLAVKIV--------QGE-- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 15218425 1031 evfdtllRESGNEEAMLRVLDIACMCVNQNPMKRPNIQQVVD 1072
Cdd:cd08221  218 -------YEDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLE 252
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
809-1009 1.70e-12

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: 68.79  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKL-AVKKLTGDY---GMMEKEFKAEVEVLSRAKHENLVALqgYCV-HDSARIliYSFME--- 880
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTfALKCVKKRHivqTRQQEHIFSEKEILEECNSPFIVKL--YRTfKDKKYL--YMLMEycl 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHENpegpAQLD-WPKRLNImrgAS--SGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLIlpY 957
Cdd:cd05572   77 GGELWTILRDR----GLFDeYTARFYT---ACvvLAFEYLHSR---GIIYRDLKPENLLLDSNGYVKLVDFGFAKKL--G 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  958 RTHVTTELVGTLGYIPPE------YGQAwvatlrGDVYSFGVVMLELLTGK--------RPMEVFR 1009
Cdd:cd05572  145 SGRKTWTFCGTPEYVAPEiilnkgYDFS------VDYWSLGILLYELLTGRppfggddeDPMKIYN 204
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
801-1079 1.92e-12

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 69.61  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATL--------DNGTKLAVKKLTGDygMMEKEFK---AEVEVLS-RAKHENLVALQGYCVH 868
Cdd:cd05099   12 DRLVLGKPLGEGCFGQVVRAEAygidksrpDQTVTVAVKMLKDN--ATDKDLAdliSEMELMKlIGKHKNIINLLGVCTQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  869 DSARILIYSFMENGSLDYWLH-ENPEGP-----------AQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNIL 936
Cdd:cd05099   90 EGPLYVIVEYAAKGNLREFLRaRRPPGPdytfditkvpeEQLSFKDLVSCAYQVARGMEYLES---RRCIHRDLAARNVL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  937 LDGNFKAYVADFGLSRLI--LPYRTHVTTELVgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMS 1013
Cdd:cd05099  167 VTEDNVMKIADFGLARGVhdIDYYKKTSNGRL-PVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVEEL 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425 1014 RELVAWVHTMKRDGK-PEEVFdTLLREsgneeamlrvldiacmCVNQNPMKRPNIQQVVDWLKNIEA 1079
Cdd:cd05099  246 FKLLREGHRMDKPSNcTHELY-MLMRE----------------CWHAVPTQRPTFKQLVEALDKVLA 295
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
799-1076 1.99e-12

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 68.91  E-value: 1.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  799 ATDNFSQANIIGCGGFGLVYKATL------DNGTKLAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSA 871
Cdd:cd05062    4 AREKITMSRELGQGSFGMVYEGIAkgvvkdEPETRVAIKTVNEAASMRERiEFLNEASVMKEFNCHHVVRLLGVVSQGQP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  872 RILIYSFMENGSLDYWLH------ENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYV 945
Cdd:cd05062   84 TLVIMELMTRGDLKSYLRslrpemENNPVQAPPSLKKMIQMAGEIADGMAYLNA---NKFVHRDLAARNCMVAEDFTVKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  946 ADFGLSRLIlpYRTHVTTElvGTLGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAW 1019
Cdd:cd05062  161 GDFGMTRDI--YETDYYRK--GGKGLLPvrwmsPESLKDGVFTTYSDVWSFGVVLWEIATlAEQP---YQGMSNEQVLRF 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425 1020 VHTMKRDGKPEEVFDTLLResgneeaMLRvldiacMCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd05062  234 VMEGGLLDKPDNCPDMLFE-------LMR------MCWQYNPKMRPSFLEIISSIKE 277
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
802-1004 2.12e-12

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: 68.96  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMME--KEFKA---EVEVLSRAKHENLVALQGyCVHDSARILI 875
Cdd:cd06651    8 NWRRGKLLGQGAFGRVYLCyDVDTGRELAAKQVQFDPESPEtsKEVSAlecEIQLLKNLQHERIVQYYG-CLRDRAEKTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFME---NGSLDYWLhenpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd06651   87 TIFMEympGGSVKDQL----KAYGALTESVTRKYTRQILEGMSYLHS---NMIVHRDIKGANILRDSAGNVKLGDFGASK 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425  953 LILPYRTHVT--TELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd06651  160 RLQTICMSGTgiRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPP 213
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
803-1005 2.22e-12

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: 68.66  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMME-KEFKAEVEVLSRAKH---ENLVALQGYCVHDSARILIYS 877
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYhVKTGRVVALKVLNLDTDDDDvSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYWLHENPegpaqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPY 957
Cdd:cd06917   83 YCEGGSIRTLMRAGP-----IAERYIAVIMREVLVALKFIHKD---GIIHRDIKAANILVTNTGNVKLCDFGVAASLNQN 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425  958 RTHVTTeLVGTLGYIPPEY---GQAWVAtlRGDVYSFGVVMLELLTGKRPM 1005
Cdd:cd06917  155 SSKRST-FVGTPYWMAPEViteGKYYDT--KADIWSLGITTYEMATGNPPY 202
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
812-1070 2.38e-12

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: 68.85  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  812 GGFGLVYKATLDNGTKLAVKK--LTGDYGMMEkEFKAEVEVLSRAK-HENLValqGY--CVHDSARILIYS---FME--- 880
Cdd:cd14037   14 GGFAHVYLVKTSNGGNRAALKrvYVNDEHDLN-VCKREIEIMKRLSgHKNIV---GYidSSANRSGNGVYEvllLMEyck 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 --------NGSLDYWLHEnpegpaqldwPKRLNIMRGASSGLAYMHQiCEPHIVHRDIKSSNILLD--GNFKayVADFG- 949
Cdd:cd14037   90 gggvidlmNQRLQTGLTE----------SEILKIFCDVCEAVAAMHY-LKPPLIHRDLKVENVLISdsGNYK--LCDFGs 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  950 LSRLILPYRTHVTTELV-------GTLGYIPPE----YGQAWVaTLRGDVYSFGVVMLELLTGKRPMEvfrpkMSRELvA 1018
Cdd:cd14037  157 ATTKILPPQTKQGVTYVeedikkyTTLQYRAPEmidlYRGKPI-TEKSDIWALGCLLYKLCFYTTPFE-----ESGQL-A 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425 1019 WVHtmkrdGKPEevFDTLLRESGNEEAMLRVldiacmCVNQNPMKRPNIQQV 1070
Cdd:cd14037  230 ILN-----GNFT--FPDNSRYSKRLHKLIRY------MLEEDPEKRPNIYQV 268
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
803-1010 3.09e-12

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 68.54  E-value: 3.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAtLDNGTKLAVKKLTGDYGMMEKEF---KAEVEVLSRAKHENLVALQGYCVHDSARILIYSFM 879
Cdd:cd06640    6 FTKLERIGKGSFGEVFKG-IDNRTQQVVAIKIIDLEEAEDEIediQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSLDYWLHENPEGPAQLdwpkrLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRT 959
Cdd:cd06640   85 GGGSALDLLRAGPFDEFQI-----ATMLKEILKGLDYLHS---EKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQI 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425  960 HVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRP 1010
Cdd:cd06640  157 KRNT-FVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHP 206
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
794-1006 3.10e-12

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: 67.80  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  794 FELLKAtdnfsqaniIGCGGFGLVYKAT-LDNGTKLAVK-----KLTGDYGMMEkeFKAEVEVLSRAKHENLVALqgYCV 867
Cdd:cd14073    3 YELLET---------LGKGTYGKVKLAIeRATGREVAIKsikkdKIEDEQDMVR--IRREIEIMSSLNHPHIIRI--YEV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  868 HDSAR--ILIYSFMENGSL-DYW--LHENPEGPAQldwpkrlNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFK 942
Cdd:cd14073   70 FENKDkiVIVMEYASGGELyDYIseRRRLPEREAR-------RIFRQIVSAVHYCHK---NGVVHRDLKLENILLDQNGN 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  943 AYVADFGLSRLIlpYRTHVTTELVGTLGYIPPEY--GQAWVATlRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14073  140 AKIADFGLSNLY--SKDKLLQTFCGSPLYASPEIvnGTPYQGP-EVDCWSLGVLLYTLVYGTMPFD 202
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
802-1005 3.31e-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: 68.22  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKL---TGDYGMMEKEFKaEVEVLSRAKHENLVALQGYCVHDSARILIYS 877
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGrNKKTGQIVAMKKIrleSEEEGVPSTAIR-EISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENgSLDYWLHENPEGpaqldwpKRLNIMRGASsglaYMHQI------CEPH-IVHRDIKSSNILLDGNFKAYVADFGL 950
Cdd:cd07861   80 FLSM-DLKKYLDSLPKG-------KYMDAELVKS----YLYQIlqgilfCHSRrVLHRDLKPQNLLIDNKGVIKLADFGL 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  951 SRLI-LPYRthVTTELVGTLGYIPPE--YGQAWVATlRGDVYSFGVVMLELLTgKRPM 1005
Cdd:cd07861  148 ARAFgIPVR--VYTHEVVTLWYRAPEvlLGSPRYST-PVDIWSIGTIFAEMAT-KKPL 201
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
801-1005 3.36e-12

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 68.93  E-value: 3.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKAtLDNGT--KLAVKKLTGDYGMME--KEFKAEVEVLSRAKHENLVALQG------------ 864
Cdd:cd07855    5 DRYEPIETIGSGAYGVVCSA-IDTKSgqKVAIKKIPNAFDVVTtaKRTLRELKILRHFKHDNIIAIRDilrpkvpyadfk 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  865 --YCVHDsariliysFMENgSLDYWLHENpeGPAQLDWPKRL--NIMRGassgLAYMHQICephIVHRDIKSSNILLDGN 940
Cdd:cd07855   84 dvYVVLD--------LMES-DLHHIIHSD--QPLTLEHIRYFlyQLLRG----LKYIHSAN---VIHRDLKPSNLLVNEN 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  941 FKAYVADFGLSRLILPY---RTHVTTELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLtGKRPM 1005
Cdd:cd07855  146 CELKIGDFGMARGLCTSpeeHKYFMTEYVATRWYRAPElmlslpeYTQAI------DMWSVGCIFAEML-GRRQL 213
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
807-1004 3.75e-12

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: 67.98  E-value: 3.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGM-MEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd06619    7 EILGHGNGGTVYKAYhLLTRRILAVKVIPLDITVeLQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 D-YWlhENPEgpaqldwPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILpyrTHVTT 963
Cdd:cd06619   87 DvYR--KIPE-------HVLGRIAVAVVKGLTYLWSL---KILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV---NSIAK 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15218425  964 ELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd06619  152 TYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFP 192
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
842-1004 3.96e-12

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: 67.76  E-value: 3.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  842 KEFKAEVEVLSRAK-HENLVALQGycVHDSAR--ILIYSFMENGSLDYWLHEN---PEGPAQldwpkRLniMRGASSGLA 915
Cdd:cd14106   52 NEILHEIAVLELCKdCPRVVNLHE--VYETRSelILILELAAGGELQTLLDEEeclTEADVR-----RL--MRQILEGVQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  916 YMHQIcepHIVHRDIKSSNILLDGNFK---AYVADFGLSRLILPyRTHVtTELVGTLGYIPPEYGQAWVATLRGDVYSFG 992
Cdd:cd14106  123 YLHER---NIVHLDLKPQNILLTSEFPlgdIKLCDFGISRVIGE-GEEI-REILGTPDYVAPEILSYEPISLATDMWSIG 197
                        170
                 ....*....|..
gi 15218425  993 VVMLELLTGKRP 1004
Cdd:cd14106  198 VLTYVLLTGHSP 209
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
807-1037 4.22e-12

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: 67.74  E-value: 4.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATL-DNGTKLAVK-----KLTGDYGMMEKEfkaeVEVLSRAKHENLVALqgYCVHDSARiLIYSFME 880
Cdd:cd14095    6 RVIGDGNFAVVKECRDkATDKEYALKiidkaKCKGKEHMIENE----VAILRRVKHPNIVQL--IEEYDTDT-ELYLVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 ---NGSLDYWLHEN---PEGPAQLdwpkrlnIMRGASSGLAYMHqicEPHIVHRDIKSSNILL----DGNFKAYVADFGL 950
Cdd:cd14095   79 lvkGGDLFDAITSStkfTERDASR-------MVTDLAQALKYLH---SLSIVHRDIKPENLLVveheDGSKSLKLADFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  951 SrlilpyrTHVTTEL---VGTLGYIPPE------YGqawvatLRGDVYSFGVVMLELLTGKRPmevFRPKmsrelvawvh 1021
Cdd:cd14095  149 A-------TEVKEPLftvCGTPTYVAPEilaetgYG------LKVDIWAAGVITYILLCGFPP---FRSP---------- 202
                        250
                 ....*....|....*.
gi 15218425 1022 tmkrDGKPEEVFDTLL 1037
Cdd:cd14095  203 ----DRDQEELFDLIL 214
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
807-1000 4.31e-12

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: 68.47  E-value: 4.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGC---GGFGLVYKATLDN---GTKLAVKKLTGDYGMMEKEFKA---EVEVLSRAKHENLVALQGYCVHdSARILIYS 877
Cdd:cd07842    3 EIEGCigrGTYGRVYKAKRKNgkdGKEYAIKKFKGDKEQYTGISQSacrEIALLRELKHENVVSLVEVFLE-HADKSVYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYW----LHENPEGpAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL--DGNFKAYV--ADFG 949
Cdd:cd07842   82 LFDYAEHDLWqiikFHRQAKR-VSIPPSMVKSLLWQILNGIHYLH---SNWVLHRDLKPANILVmgEGPERGVVkiGDLG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  950 LSRLILPYRTHVTTE--LVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLT 1000
Cdd:cd07842  158 LARLFNAPLKPLADLdpVVVTIWYRAPElllgarhYTKAI------DIWAIGCIFAELLT 211
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
801-1004 4.63e-12

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: 67.75  E-value: 4.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKL------AVKKLTGDYGMMEKEfkaeVEVLSRAKHENLVALQGYCVHDSARIL 874
Cdd:cd14167    3 DIYDFREVLGTGAFSEVVLAEEKRTQKLvaikciAKKALEGKETSIENE----IAVLHKIKHPNIVALDDIYESGGHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYWLHEnpegpaqldwpKRLNIMRGAS-------SGLAYMHQIcepHIVHRDIKSSNIL---LDGNFKAY 944
Cdd:cd14167   79 IMQLVSGGELFDRIVE-----------KGFYTERDASklifqilDAVKYLHDM---GIVHRDLKPENLLyysLDEDSKIM 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  945 VADFGLSRLILPyrTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14167  145 ISDFGLSKIEGS--GSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPP 202
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
801-1004 5.79e-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: 5.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLD-NGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRA-KHENLVALqgYCVHDSARILI 875
Cdd:cd05619    5 EDFVLHKMLGKGSFGKVFLAELKgTNQFFAIKALKKDVVLMDDDVEctmVEKRVLSLAwEHPFLTHL--FCTFQTKENLF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 Y--SFMENGSLDYWLhenpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd05619   83 FvmEYLNGGDLMFHI----QSCHKFDLPRATFYAAEIICGLQFLHS---KGIVYRDLKLDNILLDKDGHIKIADFGMCKE 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  954 ILpYRTHVTTELVGTLGYIPPE--YGQAWVATLrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05619  156 NM-LGDAKTSTFCGTPDYIAPEilLGQKYNTSV--DWWSFGVLLYEMLIGQSP 205
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
847-1004 7.22e-12

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: 67.30  E-value: 7.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  847 EVEVLSRAK-HENLVALQGYCVHDSARILIYSFMENGSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQIcepHI 925
Cdd:cd14181   65 EIHILRQVSgHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTEK----VTLSEKETRSIMRSLLEAVSYLHAN---NI 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  926 VHRDIKSSNILLDGNFKAYVADFGLSRLILPyrTHVTTELVGTLGYIPPE------------YGQawvatlRGDVYSFGV 993
Cdd:cd14181  138 VHRDLKPENILLDDQLHIKLSDFGFSCHLEP--GEKLRELCGTPGYLAPEilkcsmdethpgYGK------EVDLWACGV 209
                        170
                 ....*....|.
gi 15218425  994 VMLELLTGKRP 1004
Cdd:cd14181  210 ILFTLLAGSPP 220
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
809-1004 7.49e-12

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: 67.02  E-value: 7.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAtLDNGTKLAV-------KKLTGdygMMEKEFKAEVEVLSRAKHENLVALQGYCvHDSAR-----ILIY 876
Cdd:cd14032    9 LGRGSFKTVYKG-LDTETWVEVawcelqdRKLTK---VERQRFKEEAEMLKGLQHPNIVRFYDFW-ESCAKgkrciVLVT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLhenpegpaqldwpKRLNIM---------RGASSGLAYMHQICEPhIVHRDIKSSNILLDG-NFKAYVA 946
Cdd:cd14032   84 ELMTSGTLKTYL-------------KRFKVMkpkvlrswcRQILKGLLFLHTRTPP-IIHRDLKCDNIFITGpTGSVKIG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  947 DFGLSRLilpYRTHVTTELVGTLGYIPPE-YGQAWVATLrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14032  150 DLGLATL---KRASFAKSVIGTPEFMAPEmYEEHYDESV--DVYAFGMCMLEMATSEYP 203
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
809-1077 7.57e-12

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 67.30  E-value: 7.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLdYWL 888
Cdd:cd14152    8 IGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKGRTL-YSF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  889 HENPEgpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNfKAYVADFGL-------------SRLIL 955
Cdd:cd14152   87 VRDPK--TSLDINKTRQIAQEIIKGMGYLHA---KGIVHKDLKSKNVFYDNG-KVVITDFGLfgisgvvqegrreNELKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 P--YRTHVTTELVGTLGyiPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEvfrpKMSRELVAWvhtmkRDGKPEEVF 1033
Cdd:cd14152  161 PhdWLCYLAPEIVREMT--PGKDEDCLPFSKAADVYAFGTIWYELQARDWPLK----NQPAEALIW-----QIGSGEGMK 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15218425 1034 DTLLRESGNEEamlrVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14152  230 QVLTTISLGKE----VTEILSACWAFDLEERPSFTLLMDMLEKL 269
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
808-998 7.66e-12

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 67.47  E-value: 7.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLdNGTKLAVKKLTGdygMMEKEFKAEVEVLSRA--KHENLValqGYCVHDSARI-------LIYSF 878
Cdd:cd14143    2 SIGKGRFGEVWRGRW-RGEDVAVKIFSS---REERSWFREAEIYQTVmlRHENIL---GFIAADNKDNgtwtqlwLVSDY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENPEGPAQLdwpkrLNIMRGASSGLAYMH-QIC----EPHIVHRDIKSSNILLDGNFKAYVADFGL--- 950
Cdd:cd14143   75 HEHGSLFDYLNRYTVTVEGM-----IKLALSIASGLAHLHmEIVgtqgKPAIAHRDLKSKNILVKKNGTCCIADLGLavr 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  951 -----SRLILPYrthvtTELVGTLGYIPPEY------GQAWVATLRGDVYSFGVVMLEL 998
Cdd:cd14143  150 hdsatDTIDIAP-----NHRVGTKRYMAPEVlddtinMKHFESFKRADIYALGLVFWEI 203
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
801-1004 7.78e-12

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: 66.70  E-value: 7.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQaniIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQG-YCVHDSARILIySF 878
Cdd:cd06648   10 DNFVK---IGEGSTGIVCIATdKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSsYLVGDELWVVM-EF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSL-DYWLHENpegpaqLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILL--DGNFKayVADFGLSRLI- 954
Cdd:cd06648   86 LEGGALtDIVTHTR------MNEEQIATVCRAVLKALSFLHS---QGVIHRDIKSDSILLtsDGRVK--LSDFGFCAQVs 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  955 --LPYRthvtTELVGTLGYIPPE------YGQawvatlRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd06648  155 keVPRR----KSLVGTPYWMAPEvisrlpYGT------EVDIWSLGIMVIEMVDGEPP 202
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
808-1065 7.80e-12

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: 67.45  E-value: 7.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVKKL--TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd07846    8 LVGEGSYGMVMKCRhKETGQIVAIKKFleSEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYwLHENPEGpaqLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlILPYRTHVTTE 964
Cdd:cd07846   88 DD-LEKYPNG---LDESRVRKYLFQILRGIDFCHS---HNIIHRDIKPENILVSQSGVVKLCDFGFAR-TLAAPGEVYTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLTGkrpmEVFRPKMSrELVAWVHTMKRDG----KPEEVF 1033
Cdd:cd07846  160 YVATRWYRAPEllvgdtkYGKAV------DVWAVGCLVTEMLTG----EPLFPGDS-DIDQLYHIIKCLGnlipRHQELF 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425 1034 D-------TLLRESGNEEAMLR--------VLDIACMCVNQNPMKRP 1065
Cdd:cd07846  229 QknplfagVRLPEVKEVEPLERrypklsgvVIDLAKKCLHIDPDKRP 275
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
808-1004 7.81e-12

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: 67.66  E-value: 7.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLD-NGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRAkHENLVALQGYCVHDSARILIY--SFMEN 881
Cdd:cd05620    2 VLGKGSFGKVLLAELKgKGEYFAVKALKKDVVLIDDDVEctmVEKRVLALA-WENPFLTHLYCTFQTKEHLFFvmEFLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENpegpaqldwpKRLNIMRGA------SSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL 955
Cdd:cd05620   81 GDLMFHIQDK----------GRFDLYRATfyaaeiVCGLQFLHS---KGIIYRDLKLDNVMLDRDGHIKIADFGMCKENV 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425  956 PYRTHVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05620  148 FGDNRAST-FCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSP 195
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
807-1081 8.13e-12

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (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. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. 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. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 67.33  E-value: 8.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATL-DNGTKL--AVKKLTgDYGMME--KEFKAEVEVLSR-AKHENLVALQGYCVHDSARILIYSFME 880
Cdd:cd05088   13 DVIGEGNFGQVLKARIkKDGLRMdaAIKRMK-EYASKDdhRDFAGELEVLCKlGHHPNIINLLGACEHRGYLYLAIEYAP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHEN---PEGPA---------QLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADF 948
Cdd:cd05088   92 HGNLLDFLRKSrvlETDPAfaianstasTLSSQQLLHFAADVARGMDYLSQ---KQFIHRDLAARNILVGENYVAKIADF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  949 GLSRLILPYRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKRDG 1027
Cdd:cd05088  169 GLSRGQEVYVKKTMGRL--PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTP---YCGMTCAELYEKLPQGYRLE 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425 1028 KPEEVFDtllresgneeamlRVLDIACMCVNQNPMKRPNIQQVVDWLKNIEAEK 1081
Cdd:cd05088  244 KPLNCDD-------------EVYDLMRQCWREKPYERPSFAQILVSLNRMLEER 284
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
792-1030 8.38e-12

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: 67.44  E-value: 8.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  792 TIFELLKATDNFSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVA-LQGYCVHD 869
Cdd:cd06655   10 TIVSIGDPKKKYTRYEKIGQGASGTVFTAIdVATGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNfLDSFLVGD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  870 SArILIYSFMENGSLDYWLHENPEGPAQLdwpkrLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd06655   90 EL-FVVMEYLAGGSLTDVVTETCMDEAQI-----AAVCRECLQALEFLHA---NQVIHRDIKSDNVLLGMDGSVKLTDFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  950 LSRLILPYRTHVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvhtmkRDGKP 1029
Cdd:cd06655  161 FCAQITPEQSKRST-MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA------TNGTP 233

                 .
gi 15218425 1030 E 1030
Cdd:cd06655  234 E 234
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
809-1002 8.82e-12

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 68.23  E-value: 8.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATlD--NGTKLAVKKLTG---DYGMMEKEFKaEVEVLSRAKHENLVA----LQGycVHDSARILIYSFM 879
Cdd:cd07853    8 IGYGAFGVVWSVT-DprDGKRVALKKMPNvfqNLVSCKRVFR-ELKMLCFFKHDNVLSaldiLQP--PHIDPFEEIYVVT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSLDywLHENPEGPAQL--DWPKRL--NIMRGassgLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL 955
Cdd:cd07853   84 ELMQSD--LHKIIVSPQPLssDHVKVFlyQILRG----LKYLHS---AGILHRDIKPGNLLVNSNCVLKICDFGLARVEE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  956 P-YRTHVTTELVgTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd07853  155 PdESKHMTQEVV-TQYYRAPEilmgsrhYTSAV------DIWSVGCIFAELLGRR 202
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
803-1071 9.27e-12

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: 67.06  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVA-LQGYCVHDSARILIySFME 880
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMdVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVM-EYLA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHENPEGPAQLdwpkrLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTH 960
Cdd:cd06654  101 GGSLTDVVTETCMDEGQI-----AAVCRECLQALEFLHS---NQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvhtmkRDGKPEevfdtlLRES 1040
Cdd:cd06654  173 RST-MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIA------TNGTPE------LQNP 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 15218425 1041 GNEEAMLRvlDIACMCVNQNPMKRPNIQQVV 1071
Cdd:cd06654  240 EKLSAIFR--DFLNRCLEMDVEKRGSAKELL 268
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
809-1070 1.07e-11

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: 66.51  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDyGMMEKEFKAEVE----VLSRAKHENLVALqgYCVHDSAR--ILIYSFMEN 881
Cdd:cd14081    9 LGKGQTGLVKLAKhCVTGQKVAIKIVNKE-KLSKESVLMKVEreiaIMKLIEHPNVLKL--YDVYENKKylYLVLEYVSG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSL-DYWLHENPEGPAQLdwpkrLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTH 960
Cdd:cd14081   86 GELfDYLVKKGRLTEKEA-----RKFFRQIISALDYCHSH---SICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTTelVGTLGYIPPE--YGQAWvatlRG---DVYSFGVVMLELLTGKRPmevFRPKMSRELvawVHTMKRdGK------- 1028
Cdd:cd14081  158 ETS--CGSPHYACPEviKGEKY----DGrkaDIWSCGVILYALLVGALP---FDDDNLRQL---LEKVKR-GVfhiphfi 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 15218425 1029 PEEVFDtLLResgneeAMLRVldiacmcvnqNPMKRPNIQQV 1070
Cdd:cd14081  225 SPDAQD-LLR------RMLEV----------NPEKRITIEEI 249
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
809-1075 1.08e-11

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: 66.80  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGDygMMEKEFKA---EVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd06622    9 LGKGNYGSVYKVLhRPTGVTMAMKEIRLE--LDESKFNQiimELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYwLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILpyrTHVTTE 964
Cdd:cd06622   87 DK-LYAGGVATEGIPEDVLRRITYAVVKGLKFLKE--EHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV---ASLAKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LVGTLGYIPPEY------GQAWVATLRGDVYSFGVVMLELLTGKRPmevFRPKMSRELVAWVHTMKrDGKPEEvfdtlLR 1038
Cdd:cd06622  161 NIGCQSYMAPERiksggpNQNPTYTVQSDVWSLGLSILEMALGRYP---YPPETYANIFAQLSAIV-DGDPPT-----LP 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 15218425 1039 ESGNEEAMlrvlDIACMCVNQNPMKRPNIQQVVD--WLK 1075
Cdd:cd06622  232 SGYSDDAQ----DFVAKCLNKIPNRRPTYAQLLEhpWLV 266
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
814-1023 1.11e-11

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 66.97  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  814 FGLVYKATL------DNGTKLAVKKLTG-DYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL-D 885
Cdd:cd05091   19 FGKVYKGHLfgtapgEQTQAVAIKTLKDkAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYCSHGDLhE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHENPEG-----------PAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd05091   99 FLVMRSPHSdvgstdddktvKSTLEPADFLHIVTQIAAGMEYLSS---HHVVHKDLATRNVLVFDKLNVKISDLGLFREV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 LPYRTHvttELVGT----LGYIPPE---YGQawvATLRGDVYSFGVVMLELLT-GKRP------MEVFRPKMSRELV--- 1017
Cdd:cd05091  176 YAADYY---KLMGNsllpIRWMSPEaimYGK---FSIDSDIWSYGVVLWEVFSyGLQPycgysnQDVIEMIRNRQVLpcp 249
                        250
                 ....*....|
gi 15218425 1018 ----AWVHTM 1023
Cdd:cd05091  250 ddcpAWVYTL 259
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
794-1004 1.29e-11

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: 67.31  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  794 FELLKatdnfsqanIIGCGGFGLVYkatldngtkLAVKKLTGD-YGM--MEKE----------FKAEVEVLSRAKHENLV 860
Cdd:cd05573    3 FEVIK---------VIGRGAFGEVW---------LVRDKDTGQvYAMkiLRKSdmlkreqiahVRAERDILADADSPWIV 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  861 ALQgYCVHDSARI-LIYSFMENGSLDYWL---HENPEgpaqlDWPKRLnimrGASSGLA--YMHQIcepHIVHRDIKSSN 934
Cdd:cd05573   65 RLH-YAFQDEDHLyLVMEYMPGGDLMNLLikyDVFPE-----ETARFY----IAELVLAldSLHKL---GFIHRDIKPDN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  935 ILLD--GNFKayVADFGLS----------------------------RLILPYRTHVTTELVGTLGYIPPEygqawvaTL 984
Cdd:cd05573  132 ILLDadGHIK--LADFGLCtkmnksgdresylndsvntlfqdnvlarRRPHKQRRVRAYSAVGTPDYIAPE-------VL 202
                        250       260
                 ....*....|....*....|....*..
gi 15218425  985 RGDVY-------SFGVVMLELLTGKRP 1004
Cdd:cd05573  203 RGTGYgpecdwwSLGVILYEMLYGFPP 229
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
809-1005 1.50e-11

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 65.93  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATlDNGTK--LAVKKLTgdYGMMEKEFK-----AEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd06607    9 IGHGSFGAVYYAR-NKRTSevVAIKKMS--YSGKQSTEKwqdiiKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYCLG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYW-LHENPegpaqLDWPKRLNIMRGASSGLAYMHQICEphiVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTh 960
Cdd:cd06607   86 SASDIVeVHKKP-----LQEVEIAAICHGALQGLAYLHSHNR---IHRDVKAGNILLTEPGTVKLADFGSASLVCPANS- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425  961 vtteLVGTLGYIPPEY------GQawvATLRGDVYSFGVVMLELLTGKRPM 1005
Cdd:cd06607  157 ----FVGTPYWMAPEVilamdeGQ---YDGKVDVWSLGITCIELAERKPPL 200
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
803-1015 1.52e-11

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: 66.47  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKATLDNG------TKLAVKKLTGDYGmmEKEFKAEVEVLSRAKHENLVALqGYCVHDSARI-LI 875
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTgqmyacKKLDKKRLKKKSG--EKMALLEKEILEKVNSPFIVSL-AYAFETKTHLcLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYwlHENPEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL 955
Cdd:cd05607   81 MSLMNGGDLKY--HIYNVGERGIEMERVIFYSAQITCGILHLHSL---KIVYRDMKPENVLLDDNGNCRLSDLGLAVEVK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 PYRThvTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRE 1015
Cdd:cd05607  156 EGKP--ITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKE 213
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
807-1000 1.58e-11

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 66.56  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLD-NGTKL-AVKKLTGDYGMM--EKEFKAEVEVLSR-AKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd05089    8 DVIGEGNFGQVIKAMIKkDGLKMnAAIKMLKEFASEndHRDFAGELEVLCKlGHHPNIINLLGACENRGYLYIAIEYAPY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSL-DYW-----LHENP-----EGPAQLDWPKRLniMRGASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGL 950
Cdd:cd05089   88 GNLlDFLrksrvLETDPafakeHGTASTLTSQQL--LQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGL 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  951 SRLILPYrthvtteLVGTLGYIPPEygqaWVA---------TLRGDVYSFGVVMLELLT 1000
Cdd:cd05089  166 SRGEEVY-------VKKTMGRLPVR----WMAieslnysvyTTKSDVWSFGVLLWEIVS 213
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
803-1030 1.69e-11

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: 66.28  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVA-LQGYCVHDSARILIySFME 880
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAiDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVM-EYLA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHENPEGPAQLdwpkrLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTH 960
Cdd:cd06656  100 GGSLTDVVTETCMDEGQI-----AAVCRECLQALDFLHS---NQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvhtmkRDGKPE 1030
Cdd:cd06656  172 RST-MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA------TNGTPE 234
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
801-1069 1.73e-11

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: 66.53  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLD-NGTKLAVKKLTGDYGMMEK-EFKA--EVEVLSRAKHENLVALQGYCVHDSARILIY 876
Cdd:cd05632    2 NTFRQYRVLGKGGFGEVCACQVRaTGKMYACKRLEKKRIKKRKgESMAlnEKQILEKVNSQFVVNLAYAYETKDALCLVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHEnpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSrLILP 956
Cdd:cd05632   82 TIMNGGDLKFHIYN--MGNPGFEEERALFYAAEILCGLEDLHR---ENTVYRDLKPENILLDDYGHIRISDLGLA-VKIP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  957 YRTHVTTElVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvhtmKRDGKPEEVFDTL 1036
Cdd:cd05632  156 EGESIRGR-VGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVD-----RRVLETEEVYSAK 229
                        250       260       270
                 ....*....|....*....|....*....|...
gi 15218425 1037 LRESGNEeamlrvldIACMCVNQNPMKRPNIQQ 1069
Cdd:cd05632  230 FSEEAKS--------ICKMLLTKDPKQRLGCQE 254
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
801-1004 1.98e-11

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: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE----FKAEVEVLSRAKHENLVALQGYCVHDSARILIY 876
Cdd:cd05623   72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAetacFREERDVLVNGDSQWITTLHYAFQDDNNLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHENPEgpaqlDWPKRLNIMRGASSGLAY--MHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd05623  152 DYYVGGDLLTLLSKFED-----RLPEDMARFYLAEMVLAIdsVHQL---HYVHRDIKPDNILMDMNGHIRLADFGSCLKL 223
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  955 LPYRTHVTTELVGTLGYIPPEYGQAwVATLRG------DVYSFGVVMLELLTGKRP 1004
Cdd:cd05623  224 MEDGTVQSSVAVGTPDYISPEILQA-MEDGKGkygpecDWWSLGVCMYEMLYGETP 278
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
808-1004 2.03e-11

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 65.72  E-value: 2.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTK----LAVKKL-TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd05064   12 ILGTGRFGELCRGCLKLPSKrelpVAIHTLrAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENpEGpaQLDWPKRLNIMRGASSGLAYMhqiCEPHIVHRDIKSSNILLDGNFKAYVADFGlsRLILPYRTHVT 962
Cdd:cd05064   92 ALDSFLRKH-EG--QLVAGQLMGMLPGLASGMKYL---SEMGYVHKGLAAHKVLVNSDLVCKISGFR--RLQEDKSEAIY 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15218425  963 TELVG--TLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRP 1004
Cdd:cd05064  164 TTMSGksPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSyGERP 208
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
794-1006 2.10e-11

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: 66.24  E-value: 2.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  794 FELLKATDnFSQANIIGCGGFGLVYKAT-LDNGTKL----AVKKLTGDYG-MMEKEFKAEVEVLSRAKHENLVALQGYCV 867
Cdd:cd05110    1 LRILKETE-LKRVKVLGSGAFGTVYKGIwVPEGETVkipvAIKILNETTGpKANVEFMDEALIMASMDHPHLVRLLGVCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  868 HDSARiLIYSFMENGSLDYWLHENPEGPAQ---LDWPKRLnimrgaSSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAY 944
Cdd:cd05110   80 SPTIQ-LVTQLMPHGCLLDYVHEHKDNIGSqllLNWCVQI------AKGMMYLE---ERRLVHRDLAARNVLVKSPNHVK 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  945 VADFGLSRLIlpyrTHVTTELVGTLGYIPPEygqaWVA---------TLRGDVYSFGVVMLELLT-GKRPME 1006
Cdd:cd05110  150 ITDFGLARLL----EGDEKEYNADGGKMPIK----WMAlecihyrkfTHQSDVWSYGVTIWELMTfGGKPYD 213
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
801-1004 2.14e-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: 66.06  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEFKA---EVEVLSRAKHENLVALQGYCVHDSARILIY 876
Cdd:cd05608    1 DWFLDFRVLGKGGFGEVSACQMRATGKLyACKKLNKKRLKKRKGYEGamvEKRILAKVHSRFIVSLAYAFQTKTDLCLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSrLILP 956
Cdd:cd05608   81 TIMNGGDLRYHIYNVDEENPGFQEPRACFYTAQIISGLEHLHQ---RRIIYRDLKPENVLLDDDGNVRISDLGLA-VELK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425  957 YRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05608  157 DGQTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGP 204
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
807-1002 2.17e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 66.71  E-value: 2.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   807 NIIGCGGFGLVYKA--TLDnGTKLAVKKL---------TGDY---GMMEKEFKA--EVEVLSRAKHENLVALQG-YCVHD 869
Cdd:PTZ00024   15 AHLGEGTYGKVEKAydTLT-GKIVAIKKVkiieisndvTKDRqlvGMCGIHFTTlrELKIMNEIKHENIMGLVDvYVEGD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   870 sariLIYSFMEngSLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:PTZ00024   94 ----FINLVMD--IMASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKW---YFMHRDLSPANIFINSKGICKIADFG 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425   950 LSR-------------LILPYRTHVTTELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLTGK 1002
Cdd:PTZ00024  165 LARrygyppysdtlskDETMQRREEMTSKVVTLWYRAPEllmgaekYHFAV------DMWSVGCIFAELLTGK 231
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
803-1005 2.19e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 66.20  E-value: 2.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd06634   17 FSDLREIGHGSFGAVYFArDVRNNEVVAIKKMSYSGKQSNEKWQdiiKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYW-LHENPEGPAQLdwpkrLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPy 957
Cdd:cd06634   97 CLGSASDLLeVHKKPLQEVEI-----AAITHGALQGLAYLHS---HNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAP- 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425  958 rthvTTELVGTLGYIPPEygqAWVATLRG------DVYSFGVVMLELLTGKRPM 1005
Cdd:cd06634  168 ----ANSFVGTPYWMAPE---VILAMDEGqydgkvDVWSLGITCIELAERKPPL 214
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
803-1021 2.28e-11

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


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 65.33  E-value: 2.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDY---GMMEKEFKAEVEVLSRAKHENLVALQGYcVHDSARIliYSF 878
Cdd:cd14189    3 YCKGRLLGKGGFARCYEMTdLATNKTYAVKVIPHSRvakPHQREKIVNEIELHRDLHHKHVVKFSHH-FEDAENI--YIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHENPEGPAQLDwPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYR 958
Cdd:cd14189   80 LELCSRKSLAHIWKARHTLLE-PEVRYYLKQIISGLKYLHL---KGILHRDLKLGNFFINENMELKVGDFGLAARLEPPE 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  959 THVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAWVH 1021
Cdd:cd14189  156 QRKKT-ICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVK 217
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
803-1010 2.55e-11

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: 65.90  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSR-AKHENLVALQGYCVH------DSARILI 875
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKySHHRNIATYYGAFIKknppgmDDQLWLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHENPEGPAQLDWPKRlnIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLiL 955
Cdd:cd06637   88 MEFCGAGSVTDLIKNTKGNTLKEEWIAY--ICREILRGLSHLHQ---HKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ-L 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 PYRTHVTTELVGTLGYIPPEY-----GQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRP 1010
Cdd:cd06637  162 DRTVGRRNTFIGTPYWMAPEViacdeNPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHP 221
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
808-1004 2.65e-11

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: 66.25  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATL-DNGTKLAVKKLTGDYGMMEKEFKA---EVEVLSRA-KHENLVALqgYCVHDSARILiYSFME-- 880
Cdd:cd05592    2 VLGKGSFGKVMLAELkGTNQYFAIKALKKDVVLEDDDVECtmiERRVLALAsQHPFLTHL--FCTFQTESHL-FFVMEyl 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSlDYWLHENPEGpaqldwpkRLNIMR----GAS--SGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd05592   79 NGG-DLMFHIQQSG--------RFDEDRarfyGAEiiCGLQFLH---SRGIIYRDLKLDNVLLDREGHIKIADFGMCKEN 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 LpYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05592  147 I-YGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSP 195
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
808-1080 2.75e-11

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 65.52  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT--LDNGTKL--AVK--KLTGDYGMMEKeFKAEVEVLSRAKHENLVALQGYCVHDSarilIYSFME- 880
Cdd:cd05056   13 CIGEGQFGDVYQGVymSPENEKIavAVKtcKNCTSPSVREK-FLQEAYIMRQFDHPHIVKLIGVITENP----VWIVMEl 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 --NGSLDYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLI--LP 956
Cdd:cd05056   88 apLGELRSYLQVNKY---SLDLASLILYAYQLSTALAYLESK---RFVHRDIAARNVLVSSPDCVKLGDFGLSRYMedES 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  957 YRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKRDGKPEEVFDT 1035
Cdd:cd05056  162 YYKASKGKL--PIKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKP---FQGVKNNDVIGRIENGERLPMPPNCPPT 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15218425 1036 LLresgneEAMLRvldiacmCVNQNPMKRPNIQQVVDWLKNIEAE 1080
Cdd:cd05056  237 LY------SLMTK-------CWAYDPSKRPRFTELKAQLSDILQE 268
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
785-1062 2.93e-11

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: 66.13  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  785 RYEVKDlTIFELlkaTDNFSQANIIGCGGFGLVYKAtLD--NGTKLAVKKLTGDYG--MMEKEFKAEVEVLSRAKHENLV 860
Cdd:cd07880    3 RQEVNK-TIWEV---PDRYRDLKQVGSGAYGTVCSA-LDrrTGAKVAIKKLYRPFQseLFAKRAYRELRLLKHMKHENVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  861 ALQGYCVHDSAR------ILIYSFMENGSLDYWLHEnpegpaQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSN 934
Cdd:cd07880   78 GLLDVFTPDLSLdrfhdfYLVMPFMGTDLGKLMKHE------KLSEDRIQFLVYQMLKGLKYIHA---AGIIHRDLKPGN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  935 ILLDGNFKAYVADFGLSRlilpyrtHVTTELVG---TLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLTGKrpmEVFrp 1010
Cdd:cd07880  149 LAVNEDCELKILDFGLAR-------QTDSEMTGyvvTRWYRAPEVILNWMHyTQTVDIWSVGCIMAEMLTGK---PLF-- 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425 1011 KMSRELVAWVHTMKRDGKPEEVFDTLLRESGNEEAM-----LRVLDIACMCVNQNPM 1062
Cdd:cd07880  217 KGHDHLDQLMEIMKVTGTPSKEFVQKLQSEDAKNYVkklprFRKKDFRSLLPNANPL 273
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
914-1006 2.94e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 67.20  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   914 LAYMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLilpYRTHVTTEL----VGTLGYIPPEYGQAWVATLRGDVY 989
Cdd:PTZ00283  153 LLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKM---YAATVSDDVgrtfCGTPYYVAPEIWRRKPYSKKADMF 229
                          90
                  ....*....|....*..
gi 15218425   990 SFGVVMLELLTGKRPME 1006
Cdd:PTZ00283  230 SLGVLLYELLTLKRPFD 246
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
801-1071 3.25e-11

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 65.07  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFM 879
Cdd:cd06645   11 EDFELIQRIGSGTYGDVYKArNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSL-DYWLHENPEGPAQLDWpkrlnIMRGASSGLAYMHQICEphiVHRDIKSSNILLDGNFKAYVADFGLSRLILPYR 958
Cdd:cd06645   91 GGGSLqDIYHVTGPLSESQIAY-----VSRETLQGLYYLHSKGK---MHRDIKGANILLTDNGHVKLADFGVSAQITATI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  959 THVTTeLVGTLGYIPPEYgqAWVATLRG-----DVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvhtmKRDGKPEEVF 1033
Cdd:cd06645  163 AKRKS-FIGTPYWMAPEV--AAVERKGGynqlcDIWAVGITAIELAELQPPMFDLHPMRALFLMT-----KSNFQPPKLK 234
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15218425 1034 DTlLRESGNEEAMLRvldiacMCVNQNPMKRPNIQQVV 1071
Cdd:cd06645  235 DK-MKWSNSFHHFVK------MALTKNPKKRPTAEKLL 265
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
809-1079 3.28e-11

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 65.80  E-value: 3.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT---LDNG-----TKLAVKKLTGDygMMEKEFK---AEVEVLSR-AKHENLVALQGYCVHDSARILIY 876
Cdd:cd05098   21 LGEGCFGQVVLAEaigLDKDkpnrvTKVAVKMLKSD--ATEKDLSdliSEMEMMKMiGKHKNIINLLGACTQDGPLYVIV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLH-ENPEGPAQLDWPKRLNIMRGASSGL---AY-----MHQICEPHIVHRDIKSSNILLDGNFKAYVAD 947
Cdd:cd05098   99 EYASKGNLREYLQaRRPPGMEYCYNPSHNPEEQLSSKDLvscAYqvargMEYLASKKCIHRDLAARNVLVTEDNVMKIAD 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  948 FGLSRLIlpyrTHVTTELVGTLGYIP-----PEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMS-RELVAWV 1020
Cdd:cd05098  179 FGLARDI----HHIDYYKKTTNGRLPvkwmaPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPY----PGVPvEELFKLL 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425 1021 HTMKRDGKPEEVFDTLLresgneeAMLRvldiacMCVNQNPMKRPNIQQVVDWLKNIEA 1079
Cdd:cd05098  251 KEGHRMDKPSNCTNELY-------MMMR------DCWHAVPSQRPTFKQLVEDLDRIVA 296
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
794-1032 3.66e-11

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: 65.71  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  794 FELLKatdnfsqanIIGCGGFG---LVYKAtlDNGTKLAVKKLTGDyGMMEKE----FKAEVEVLSRAKHENLVALQgYC 866
Cdd:cd05599    3 FEPLK---------VIGRGAFGevrLVRKK--DTGHVYAMKKLRKS-EMLEKEqvahVRAERDILAEADNPWVVKLY-YS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  867 VHDSARI-LIYSFMENGSLDYWLhenpegpaqldwpkrlniMRG------------ASSGLAyMHQICEPHIVHRDIKSS 933
Cdd:cd05599   70 FQDEENLyLIMEFLPGGDMMTLL------------------MKKdtlteeetrfyiAETVLA-IESIHKLGYIHRDIKPD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  934 NILLDGNFKAYVADFGLS----RLILPYRThvttelVGTLGYIPPE------YGQAwvatlrGDVYSFGVVMLELLTG-- 1001
Cdd:cd05599  131 NLLLDARGHIKLSDFGLCtglkKSHLAYST------VGTPDYIAPEvflqkgYGKE------CDWWSLGVIMYEMLIGyp 198
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15218425 1002 ----KRPMEVFrpkmsRELVAWVHTMKrdgKPEEV 1032
Cdd:cd05599  199 pfcsDDPQETC-----RKIMNWRETLV---FPPEV 225
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
801-1004 4.07e-11

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: 65.79  E-value: 4.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVykatldngtKLAVKKLTGD-YGM--MEKE----------FKAEVEVLSRAKHENLVALQgYCV 867
Cdd:cd05601    1 KDFEVKNVIGRGHFGEV---------QVVKEKATGDiYAMkvLKKSetlaqeevsfFEEERDIMAKANSPWITKLQ-YAF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  868 HDSARI-LIYSFMENGSLDYWL--HENP--EGPAQLdwpkrlnimrgassGLAYM----HQICEPHIVHRDIKSSNILLD 938
Cdd:cd05601   71 QDSENLyLVMEYHPGGDLLSLLsrYDDIfeESMARF--------------YLAELvlaiHSLHSMGYVHRDIKPENILID 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  939 --GNFKayVADFGlSRLILPYRTHVTTEL-VGTLGYIPPEYGQAWVATLRG------DVYSFGVVMLELLTGKRP 1004
Cdd:cd05601  137 rtGHIK--LADFG-SAAKLSSDKTVTSKMpVGTPDYIAPEVLTSMNGGSKGtygvecDWWSLGIVAYEMLYGKTP 208
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
809-1012 4.10e-11

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: 64.63  E-value: 4.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVK---KLTGDYGMMEKEFKAEVEVLSRAKHENLValQGYCVHDSARILIYSFME---N 881
Cdd:cd14163    8 IGEGTYSKVKEAfSKKHQRKVAIKiidKSGGPEEFIQRFLPRELQIVERLDHKNII--HVYEMLESADGKIYLVMElaeD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSL-DYWLHENP--EGPAQldwpkrlNIMRGASSGLAYMHQiCepHIVHRDIKSSNILLDGnFKAYVADFGLSRLILPYR 958
Cdd:cd14163   86 GDVfDCVLHGGPlpEHRAK-------ALFRQLVEAIRYCHG-C--GVAHRDLKCENALLQG-FTLKLTDFGFAKQLPKGG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  959 THVTTELVGTLGYIPPEYGQAWVATLR-GDVYSFGVVMLELLTGKRPM-EVFRPKM 1012
Cdd:cd14163  155 RELSQTFCGSTAYAAPEVLQGVPHDSRkGDIWSMGVVLYVMLCAQLPFdDTDIPKM 210
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
808-1004 4.17e-11

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: 65.75  E-value: 4.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFG--LVYKATLDnGTKLAVKKLTGDYGMMEKEFK---AEVEVLSR-AKHENLVALQgYCVHDSARI-LIYSFME 880
Cdd:cd05604    3 VIGKGSFGkvLLAKRKRD-GKYYAVKVLQKKVILNRKEQKhimAERNVLLKnVKHPFLVGLH-YSFQTTDKLyFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHENPEGPAqldwPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPyRTH 960
Cdd:cd05604   81 GGELFFHLQRERSFPE----PRARFYAAEIASALGYLHSI---NIVYRDLKPENILLDSQGHIVLTDFGLCKEGIS-NSD 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15218425  961 VTTELVGTLGYIPPEY--GQAWVATLrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05604  153 TTTTFCGTPEYLAPEVirKQPYDNTV--DWWCLGSVLYEMLYGLPP 196
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
802-1017 4.82e-11

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: 64.46  E-value: 4.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT-LDNGTKLAVK---KLTGDYGMMEKEFKaEVEVLSRAKHENLVALqgYCVHDSARILiYS 877
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARhVLTGREVAIKiidKTQLNPSSLQKLFR-EVRIMKILNHPNIVKL--FEVIETEKTL-YL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGS----LDYWLHEN--PEGPAQLDWpkrlnimRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLS 951
Cdd:cd14072   77 VMEYASggevFDYLVAHGrmKEKEARAKF-------RQIVSAVQYCHQ---KRIVHRDLKAENLLLDADMNIKIADFGFS 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  952 RLILPYRTHVTteLVGTLGYIPPEYGQAwvATLRG---DVYSFGVVMLELLTGKRPMEVFRPKMSRELV 1017
Cdd:cd14072  147 NEFTPGNKLDT--FCGSPPYAAPELFQG--KKYDGpevDVWSLGVILYTLVSGSLPFDGQNLKELRERV 211
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
809-1005 4.98e-11

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: 64.76  E-value: 4.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKL---TGDYGMMEKEFKaEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd07839    8 IGEGTYGTVFKAkNRETHEIVALKRVrldDDDEGVPSSALR-EICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCDQDLK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHENPEgpaqLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLI-LPYRTHvTT 963
Cdd:cd07839   87 KYFDSCNGD----IDPEIVKSFMFQLLKGLAFCHS---HNVLHRDLKPQNLLINKNGELKLADFGLARAFgIPVRCY-SA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15218425  964 ELVgTLGYIPPE--YGqAWVATLRGDVYSFGVVMLELLTGKRPM 1005
Cdd:cd07839  159 EVV-TLWYRPPDvlFG-AKLYSTSIDMWSAGCIFAELANAGRPL 200
PLN03150 PLN03150
hypothetical protein; Provisional
283-361 5.46e-11

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 66.76  E-value: 5.46e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425   283 LSGKIDNGITRLTKLTLLELYSNHIEGEIPKDIGKLSKLSSLQLHVNNLMGSIPVSLANCTKLVKLNLRVNQLGGTLSA 361
Cdd:PLN03150  430 LRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPA 508
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
805-1045 5.83e-11

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: 64.21  E-value: 5.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  805 QANIIGCGGFGLVYKAT-LDNGTKLAVKkLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd14192    8 PHEVLGGGRFGQVHKCTeLSTGLTLAAK-IIKVKGAKEReEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENPEGPAQLDwpkRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILL---DGNfKAYVADFGLSRLILPyRT 959
Cdd:cd14192   87 ELFDRITDESYQLTELD---AILFTRQICEGVHYLHQ---HYILHLDLKPENILCvnsTGN-QIKIIDFGLARRYKP-RE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  960 HVTTELvGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPmevFRPKMSRELVAWVHTMKRDgkpeevFDTLLRE 1039
Cdd:cd14192  159 KLKVNF-GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSP---FLGETDAETMNNIVNCKWD------FDAEAFE 228

                 ....*.
gi 15218425 1040 SGNEEA 1045
Cdd:cd14192  229 NLSEEA 234
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
800-1004 6.35e-11

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: 63.93  E-value: 6.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  800 TDNFSQANIIGCGGFGLVYKA-TLDNGTKLAVK-----KLTGDYGMMEKEfkaeVEVLSRAKHENLVALqgYCVHDSARI 873
Cdd:cd14083    2 RDKYEFKEVLGTGAFSEVVLAeDKATGKLVAIKcidkkALKGKEDSLENE----IAVLRKIKHPNIVQL--LDIYESKSH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 LiYSFME---NGSL-DYWLHEN--PEGPAQLdwpkrlnIMRGASSGLAYMHQIcepHIVHRDIKSSNIL---LDGNFKAY 944
Cdd:cd14083   76 L-YLVMElvtGGELfDRIVEKGsyTEKDASH-------LIRQVLEAVDYLHSL---GIVHRDLKPENLLyysPDEDSKIM 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  945 VADFGLSRLILPyrtHVTTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14083  145 ISDFGLSKMEDS---GVMSTACGTPGYVAPEvlaqkpYGKAV------DCWSIGVISYILLCGYPP 201
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
794-1004 8.03e-11

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: 64.94  E-value: 8.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  794 FELLKatdnfsqanIIGCGGFG---LVYKATLDNGTKLAVKKLTGDYGMMEKE-----FKAEVEVLSRAKHENLVALQGY 865
Cdd:cd05614    2 FELLK---------VLGTGAYGkvfLVRKVSGHDANKLYAMKVLRKAALVQKAktvehTRTERNVLEHVRQSPFLVTLHY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  866 CVHDSARI-LIYSFMENGSLDYWLHenpegpaQLDWPKRLNIMRGASS---GLAYMHQIcepHIVHRDIKSSNILLDGNF 941
Cdd:cd05614   73 AFQTDAKLhLILDYVSGGELFTHLY-------QRDHFSEDEVRFYSGEiilALEHLHKL---GIVYRDIKLENILLDSEG 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  942 KAYVADFGLSRLILPYRTHVTTELVGTLGYIPPEygqawvaTLRG--------DVYSFGVVMLELLTGKRP 1004
Cdd:cd05614  143 HVVLTDFGLSKEFLTEEKERTYSFCGTIEYMAPE-------IIRGksghgkavDWWSLGILMFELLTGASP 206
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
911-1021 8.44e-11

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: 63.88  E-value: 8.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  911 SSGLAYMHQicePHIVHRDIKSSNILL-DGNF-KAYVADFGLSRlilpyRTHVTTELV-GTLGYIPPEYGQA----WVAT 983
Cdd:cd13987  101 ASALDFMHS---KNLVHRDIKPENVLLfDKDCrRVKLCDFGLTR-----RVGSTVKRVsGTIPYTAPEVCEAkkneGFVV 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15218425  984 LRG-DVYSFGVVMLELLTGKRPME--VFRPKMSRELVAWVH 1021
Cdd:cd13987  173 DPSiDVWAFGVLLFCCLTGNFPWEkaDSDDQFYEEFVRWQK 213
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
836-998 8.50e-11

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 63.71  E-value: 8.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  836 DYGMMEKEFKAEVEVLSRAKHENLVALQGYCV---HDSAR-ILIYSFMENGSLDYWLHENPEGPAQLD---WpKRLniMR 908
Cdd:cd13984   34 IFKAQEEKIRAVFDNLIQLDHPNIVKFHRYWTdvqEEKARvIFITEYMSSGSLKQFLKKTKKNHKTMNeksW-KRW--CT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  909 GASSGLAYMHQiCEPHIVHRDIKSSNILLDGNfkayvadfGLSRL--ILP--YRTHVTT--ELVGTLGYIPPEYGQAWVA 982
Cdd:cd13984  111 QILSALSYLHS-CDPPIIHGNLTCDTIFIQHN--------GLIKIgsVAPdaIHNHVKTcrEEHRNLHFFAPEYGYLEDV 181
                        170
                 ....*....|....*.
gi 15218425  983 TLRGDVYSFGVVMLEL 998
Cdd:cd13984  182 TTAVDIYSFGMCALEM 197
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
847-1005 9.34e-11

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: 64.38  E-value: 9.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  847 EVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWLHENPEGPAQLDWPKRLNIMRGassgLAYMHQicEPHIV 926
Cdd:cd06615   49 ELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRG----LTYLRE--KHKIM 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  927 HRDIKSSNILLDGNFKAYVADFGLS-RLIlpyrTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPM 1005
Cdd:cd06615  123 HRDVKPSNILVNSRGEIKLCDFGVSgQLI----DSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPI 198
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
809-998 9.86e-11

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 63.76  E-value: 9.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLA---VKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd05042    3 IGNGWFGKVLLGEIYSGTSVAqvvVKELKASANPKEQdTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHEnpEGPAQLDWPKRLNIMRGA---SSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLS---------- 951
Cdd:cd05042   83 KAYLRS--EREHERGDSDTRTLQRMAcevAAGLAHLHKL---NFVHSDLALRNCLLTSDLTVKIGDYGLAhsrykedyie 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  952 ---RLILPYRtHVTTELVGTLgyippeYGQAWVA--TLRGDVYSFGVVMLEL 998
Cdd:cd05042  158 tddKLWFPLR-WTAPELVTEF------HDRLLVVdqTKYSNIWSLGVTLWEL 202
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
803-1011 1.11e-10

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: 63.49  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKATLDNGTKLAV-------KKLTGDYGMMEKEFKaeveVLSRAKHENLVALQGYCVHDSARILI 875
Cdd:cd14201    8 YSRKDLVGHGAFAVVFKGRHRKKTDWEVaiksinkKNLSKSQILLGKEIK----ILKELQHENIVALYDVQEMPNSVFLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHenPEGPAQLDwPKRLNIMRGAssglAYMHQICEPHIVHRDIKSSNILLD---------GNFKAYVA 946
Cdd:cd14201   84 MEYCNGGDLADYLQ--AKGTLSED-TIRVFLQQIA----AAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  947 DFGLSRLIlpYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPK 1011
Cdd:cd14201  157 DFGFARYL--QSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQ 219
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
809-1036 1.12e-10

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 63.44  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA---TLDNGTKLAVKKLTGDYG--MMEKEFKAEVEVLSRAKHENLVALQGYCVHDSArILIYSFMENGS 883
Cdd:cd05116    3 LGSGNFGTVKKGyyqMKKVVKTVAVKILKNEANdpALKDELLREANVMQQLDNPYIVRMIGICEAESW-MLVMEMAELGP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTT 963
Cdd:cd05116   82 LNKFLQKN----RHVTEKNITELVHQVSMGMKYLE---ESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  964 ELVGT--LGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKRDGKPE----EVFDTL 1036
Cdd:cd05116  155 QTHGKwpVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKP---YKGMKGNEVTQMIEKGERMECPAgcppEMYDLM 231
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
809-1005 1.13e-10

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 63.39  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL--------DNGTKLAVKKLTGDygMMEKEFKAEVEVLSRAKHENLVALQGYCV-HDSARILIYSFM 879
Cdd:cd14019    9 IGEGTFSSVYKAEDklhdlydrNKGRLVALKHIYPT--SSPSRILNELECLERLGGSNNVSGLITAFrNEDQVVAVLPYI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSL-DYWLHENPEGPAqldwpkrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLD-GNFKAYVADFGLSRLIlPY 957
Cdd:cd14019   87 EHDDFrDFYRKMSLTDIR--------IYLRNLFKALKHVHSF---GIIHRDVKPGNFLYNrETGKGVLVDFGLAQRE-ED 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  958 RTHVTTELVGTLGYIPPE----YGQAWVATlrgDVYSFGVVMLELLTGKRPM 1005
Cdd:cd14019  155 RPEQRAPRAGTRGFRAPEvlfkCPHQTTAI---DIWSAGVILLSILSGRFPF 203
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
792-1002 1.21e-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: 64.29  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  792 TIFELLKATDNFSQaniIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMM--EKEFKAEVEVLSRAKHENLVALQGycVH 868
Cdd:cd07877   11 TIWEVPERYQNLSP---VGSGAYGSVCAAfDTKTGLRVAVKKLSRPFQSIihAKRTYRELRLLKHMKHENVIGLLD--VF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  869 DSARiliySFMENGslDYWLHENPEGpAQLDwpkrlNIMRGAS--------------SGLAYMHQicePHIVHRDIKSSN 934
Cdd:cd07877   86 TPAR----SLEEFN--DVYLVTHLMG-ADLN-----NIVKCQKltddhvqfliyqilRGLKYIHS---ADIIHRDLKPSN 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  935 ILLDGNFKAYVADFGLSRlilpyrtHVTTELVG---TLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLTGK 1002
Cdd:cd07877  151 LAVNEDCELKILDFGLAR-------HTDDEMTGyvaTRWYRAPEIMLNWMHyNQTVDIWSVGCIMAELLTGR 215
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
809-1008 1.30e-10

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: 63.54  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL-DNGTKLAVKK--LTGDyGMMEKEFKAEVEVLSRAKH-ENLVALQGYCVHDSARILIYSFMENgSL 884
Cdd:cd06616   14 IGRGAFGTVNKMLHkPSGTIMAVKRirSTVD-EKEQKRLLMDLDVVMRSSDcPYIVKFYGALFREGDCWICMELMDI-SL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 D--Y---WLHENPEGPAQLDWPKRLNIMRGassgLAYMHQicEPHIVHRDIKSSNILLDGNFKAYVADFGLS-RLIlpyR 958
Cdd:cd06616   92 DkfYkyvYEVLDSVIPEEILGKIAVATVKA----LNYLKE--ELKIIHRDVKPSNILLDRNGNIKLCDFGISgQLV---D 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  959 THVTTELVGTLGYIPPEYGQAWVAT----LRGDVYSFGVVMLELLTGKRP----MEVF 1008
Cdd:cd06616  163 SIAKTRDAGCRPYMAPERIDPSASRdgydVRSDVWSLGITLYEVATGKFPypkwNSVF 220
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
808-1048 1.34e-10

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: 64.16  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATL-DNGTKLAVKKLTGDYGMMEKEFKA---EVEVLSRAKHENLVALQGYCVHDSARIL-IYSFMENG 882
Cdd:cd05590    2 VLGKGSFGKVMLARLkESGRLYAVKVLKKDVILQDDDVECtmtEKRILSLARNHPFLTQLYCCFQTPDRLFfVMEFVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILpYRTHVT 962
Cdd:cd05590   82 DLMFHIQKS----RRFDEARARFYAAEITSALMFLH---DKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGI-FNGKTT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  963 TELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME------VFRPKMSRELV--AWVHT---------MKR 1025
Cdd:cd05590  154 STFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEaeneddLFEAILNDEVVypTWLSQdavdilkafMTK 233
                        250       260
                 ....*....|....*....|...
gi 15218425 1026 DgkPEEVFDTLlrESGNEEAMLR 1048
Cdd:cd05590  234 N--PTMRLGSL--TLGGEEAILR 252
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
809-1004 1.41e-10

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: 63.16  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAV-------KKLTGDYGMMEKEFKaeveVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKPDLPVaikcitkKNLSKSQNLLGKEIK----ILKELSHENVVALLDCQETSSSVYLVMEYCNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHEN---PEGPAQLdwpkrlnIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAY---------VADFG 949
Cdd:cd14120   77 GDLADYLQAKgtlSEDTIRV-------FLQQIAAAMKALH---SKGIVHRDLKPQNILLSHNSGRKpspndirlkIADFG 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  950 LSRLiLPYRTHVTTeLVGTLGYIPPE--YGQAWVAtlRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14120  147 FARF-LQDGMMAAT-LCGSPMYMAPEviMSLQYDA--KADLWSIGTIVYQCLTGKAP 199
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
912-1072 1.49e-10

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: 63.21  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  912 SGLAYMHQicEPHIVHRDIKSSNILLDGNFKAYVADFGLS-RLIlpyRTHVTTELVGTLGYIPPEY----GQAWVATLRG 986
Cdd:cd06617  114 KALEYLHS--KLSVIHRDVKPSNVLINRNGQVKLCDFGISgYLV---DSVAKTIDAGCKPYMAPERinpeLNQKGYDVKS 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  987 DVYSFGVVMLELLTGKRPMEVFRpKMSRELVAWVHtmkrDGKPeevfdTLLRESGNEEamlrVLDIACMCVNQNPMKRPN 1066
Cdd:cd06617  189 DVWSLGITMIELATGRFPYDSWK-TPFQQLKQVVE----EPSP-----QLPAEKFSPE----FQDFVNKCLKKNYKERPN 254

                 ....*.
gi 15218425 1067 IQQVVD 1072
Cdd:cd06617  255 YPELLQ 260
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
803-1064 1.53e-10

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: 63.47  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLV----YKATldnGTKLAVKKLTGDYGMMEK-EFKA--EVEVLSRAKHENLVALQGYCVHDSARILI 875
Cdd:cd05631    2 FRHYRVLGKGGFGEVcacqVRAT---GKMYACKKLEKKRIKKRKgEAMAlnEKRILEKVNSRFVVSLAYAYETKDALCLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYwlHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIl 955
Cdd:cd05631   79 LTIMNGGDLKF--HIYNMGNPGFDEQRAIFYAAELCCGLEDLQR---ERIVYRDLKPENILLDDRGHIRISDLGLAVQI- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 PYRTHVTTElVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvhtmKRDGKPEEVFDt 1035
Cdd:cd05631  153 PEGETVRGR-VGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVD-----RRVKEDQEEYS- 225
                        250       260
                 ....*....|....*....|....*....
gi 15218425 1036 llrESGNEEAMlrvlDIACMCVNQNPMKR 1064
Cdd:cd05631  226 ---EKFSEDAK----SICRMLLTKNPKER 247
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
802-1007 1.66e-10

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: 63.48  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFG---LVYKATLDNGTKLAVKKLTGDYGMMEK-----EFKAEVEVLSRAKHENLVALQGYCVHDSARI 873
Cdd:cd05613    1 NFELLKVLGTGAYGkvfLVRKVSGHDAGKLYAMKVLKKATIVQKaktaeHTRTERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 -LIYSFMENGSLDYWLHENPEGPAQldwpkRLNIMRGASS-GLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLS 951
Cdd:cd05613   81 hLILDYINGGELFTHLSQRERFTEN-----EVQIYIGEIVlALEHLHKL---GIIYRDIKLENILLDSSGHVVLTDFGLS 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  952 RLILPYRTHVTTELVGTLGYIPPEygqawvaTLRG---------DVYSFGVVMLELLTGKRPMEV 1007
Cdd:cd05613  153 KEFLLDENERAYSFCGTIEYMAPE-------IVRGgdsghdkavDWWSLGVLMYELLTGASPFTV 210
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
831-1004 1.71e-10

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: 62.88  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  831 KKLTGDYgmMEKEFKAEVEVLSRAKHENLValQGYCVHDSARILIYSFME---NGSLDYWLHEN---PEGPAQldwpkrl 904
Cdd:cd14165   37 KKAPDDF--VEKFLPRELEILARLNHKSII--KTYEIFETSDGKVYIVMElgvQGDLLEFIKLRgalPEDVAR------- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  905 NIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL---PYRTHVTTELVGTLGYIPPEYGQAWV 981
Cdd:cd14165  106 KMFHQLSSAIKYCH---ELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLrdeNGRIVLSKTFCGSAAYAAPEVLQGIP 182
                        170       180
                 ....*....|....*....|....
gi 15218425  982 ATLR-GDVYSFGVVMLELLTGKRP 1004
Cdd:cd14165  183 YDPRiYDIWSLGVILYIMVCGSMP 206
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
809-1010 1.72e-10

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: 63.66  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLAVKKLTGDYGMME--KEFKAEVEVLSRAKHENLVALQGYCVHDSAR--ILIYSFMENGSL 884
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRplDVQMREFEVLKKLNHKNIVKLFAIEEELTTRhkVLVMELCPCGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 dYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL----DGNFKAYVADFGLSRLILPYRTH 960
Cdd:cd13988   81 -YTVLEEPSNAYGLPESEFLIVLRDVVAGMNHLR---ENGIVHRDIKPGNIMRvigeDGQSVYKLTDFGAARELEDDEQF 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTteLVGTLGYIPP----------EYGQAWVATLrgDVYSFGVVMLELLTGKRPmevFRP 1010
Cdd:cd13988  157 VS--LYGTEEYLHPdmyeravlrkDHQKKYGATV--DLWSIGVTFYHAATGSLP---FRP 209
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
809-1071 1.74e-10

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: 63.12  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL-DY 886
Cdd:cd06646   17 VGSGTYGDVYKArNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLqDI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENPEGPAQLDWpkrlnIMRGASSGLAYMHQICEphiVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTeLV 966
Cdd:cd06646   97 YHVTGPLSELQIAY-----VCRETLQGLAYLHSKGK---MHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRKS-FI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  967 GTLGYIPPEYgqAWVATLRG-----DVYSFGVVMLELLTGKRPMEVFRPKMSRELVAwvhtmKRDGKPEEVFDTlLRESG 1041
Cdd:cd06646  168 GTPYWMAPEV--AAVEKNGGynqlcDIWAVGITAIELAELQPPMFDLHPMRALFLMS-----KSNFQPPKLKDK-TKWSS 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 15218425 1042 NEEAMLRVldiacmCVNQNPMKRPNIQQVV 1071
Cdd:cd06646  240 TFHNFVKI------SLTKNPKKRPTAERLL 263
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
809-1006 1.79e-10

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: 62.79  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVK---KLTGDYGMMEKEFKaEVEVLSRAKHENLVALqgYCVHDSARI--LIYSFMENG 882
Cdd:cd14071    8 IGKGNFAVVKLARhRITKTEVAIKiidKSQLDEENLKKIYR-EVQIMKMLNHPHIIKL--YQVMETKDMlyLVTEYASNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SL-DYWLHEN--PEGPAQldwPKRLNIMrgasSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPyrT 959
Cdd:cd14071   85 EIfDYLAQHGrmSEKEAR---KKFWQIL----SAVEYCHKR---HIVHRDLKAENLLLDANMNIKIADFGFSNFFKP--G 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425  960 HVTTELVGTLGYIPPEY--GQAWVATlRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14071  153 ELLKTWCGSPPYAAPEVfeGKEYEGP-QLDIWSLGVVLYVLVCGALPFD 200
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
780-1077 2.00e-10

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 63.50  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  780 LFGNSRYEVKDLTIFELLKatDNFSQANIIGCGGFGLVYKATL--------DNGTKLAVKKLTGDygMMEKEFK---AEV 848
Cdd:cd05101    5 LAGVSEYELPEDPKWEFPR--DKLTLGKPLGEGCFGQVVMAEAvgidkdkpKEAVTVAVKMLKDD--ATEKDLSdlvSEM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  849 EVLSR-AKHENLVALQGYCVHDSARILIYSFMENGSLDYWLH-ENPEG-----------PAQLDWPKRLNIMRGASSGLA 915
Cdd:cd05101   81 EMMKMiGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRaRRPPGmeysydinrvpEEQMTFKDLVSCTYQLARGME 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  916 YM-HQICephiVHRDIKSSNILLDGNFKAYVADFGLSRLI--LPYRTHVTTELVgTLGYIPPEYGQAWVATLRGDVYSFG 992
Cdd:cd05101  161 YLaSQKC----IHRDLAARNVLVTENNVMKIADFGLARDInnIDYYKKTTNGRL-PVKWMAPEALFDRVYTHQSDVWSFG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  993 VVMLELLT-GKRPMevfrPKMS-RELVAWVHTMKRDGKPEEVFDTLLresgneeAMLRvldiacMCVNQNPMKRPNIQQV 1070
Cdd:cd05101  236 VLMWEIFTlGGSPY----PGIPvEELFKLLKEGHRMDKPANCTNELY-------MMMR------DCWHAVPSQRPTFKQL 298

                 ....*..
gi 15218425 1071 VDWLKNI 1077
Cdd:cd05101  299 VEDLDRI 305
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
809-1000 2.01e-10

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: 62.44  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVY-----KATLDNGTKLAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd08222    8 LGSGNFGTVYlvsdlKATADEELKVLKEISVGELQPDETvDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHE---NPEGPAQ---LDWPKRLnimrgaSSGLAYMHqicEPHIVHRDIKSSNILLDGNFkAYVADFGLSRlILP 956
Cdd:cd08222   88 DLDDKISEykkSGTTIDEnqiLDWFIQL------LLAVQYMH---ERRILHRDLKAKNIFLKNNV-IKVGDFGISR-ILM 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15218425  957 YRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT 1000
Cdd:cd08222  157 GTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCC 200
PLN03150 PLN03150
hypothetical protein; Provisional
300-388 2.10e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 64.84  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   300 LELYSNHIEGEIPKDIGKLSKLSSLQLHVNNLMGSIPVSLANCTKLVKLNLRVNQLGGTLSAiDFSRFQSLSILDLGNNS 379
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPE-SLGQLTSLRILNLNGNS 501

                  ....*....
gi 15218425   380 FTGEFPSTV 388
Cdd:PLN03150  502 LSGRVPAAL 510
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
801-1002 2.17e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 62.91  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   801 DNFSQANIIGCGGFGLVYKATlDNGTK--LAVKKL---TGDYGMMEKEFKaEVEVLSRAKHENLVALQGyCVHDSARI-L 874
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKAR-DRVTNetIALKKIrleQEDEGVPSTAIR-EISLLKEMQHGNIVRLQD-VVHSEKRLyL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   875 IYSFMEngsLDYWLHENpegpAQLDWPKRLNIMRgassglAYMHQI------CEPH-IVHRDIKSSNILLDGNFKAY-VA 946
Cdd:PLN00009   79 VFEYLD---LDLKKHMD----SSPDFAKNPRLIK------TYLYQIlrgiayCHSHrVLHRDLKPQNLLIDRRTNALkLA 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425   947 DFGLSRLI-LPYRTHvTTELVgTLGYIPPE--YGQAWVATlRGDVYSFGVVMLELLTGK 1002
Cdd:PLN00009  146 DFGLARAFgIPVRTF-THEVV-TLWYRAPEilLGSRHYST-PVDIWSVGCIFAEMVNQK 201
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
809-1070 2.44e-10

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 62.70  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNG---TKLAVKKLTGDYGMMEK-EFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd05087    5 IGHGWFGKVFLGEVNSGlssTQVVVKELKASASVQDQmQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLGDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHENPEGPAQLDWPKRLNIMR-GASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTT 963
Cdd:cd05087   85 KGYLRSCRAAESMAPDPLTLQRMAcEVACGLLHLHR---NNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKEDYFVTA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  964 -ELVGTLGYIPPE-----YGQAWVA--TLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKRDGKPEEVFD 1034
Cdd:cd05087  162 dQLWVPLRWIAPElvdevHGNLLVVdqTKQSNVWSLGVTIWELFElGNQP---YRHYSDRQVLTYTVREQQLKLPKPQLK 238
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 15218425 1035 TLLREsgneeamlRVLDIACMCVNQnPMKRPNIQQV 1070
Cdd:cd05087  239 LSLAE--------RWYEVMQFCWLQ-PEQRPTAEEV 265
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
809-1000 3.17e-10

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: 62.29  E-value: 3.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTGDY-GMMEKEFKAEVEVLSR-AKHENLVALQGyCVHD--SARI-LIYSFMEnG 882
Cdd:cd07831    7 IGEGTFSEVLKAqSRKTGKYYAIKCMKKHFkSLEQVNNLREIQALRRlSPHPNILRLIE-VLFDrkTGRLaLVFELMD-M 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLdYWLHENPEGPaqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGN-FKayVADFGLSRLI---LPYr 958
Cdd:cd07831   85 NL-YELIKGRKRP--LPEKRVKNYMYQLLKSLDHMHRN---GIFHRDIKPENILIKDDiLK--LADFGSCRGIyskPPY- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425  959 thvtTELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLT 1000
Cdd:cd07831  156 ----TEYISTRWYRAPEclltdgyYGPKM------DIWAVGCVFFEILS 194
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
809-998 3.25e-10

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


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 62.37  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLdNGTKLAVKKLtgdYGMMEKEFKAEVEVLSRA--KHENLValqGYCVHD-------SARILIYSFM 879
Cdd:cd14220    3 IGKGRYGEVWMGKW-RGEKVAVKVF---FTTEEASWFRETEIYQTVlmRHENIL---GFIAADikgtgswTQLYLITDYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSLDYWLHenpegPAQLDWPKRLNIMRGASSGLAYMHQIC-----EPHIVHRDIKSSNILLDGNFKAYVADFGLS--- 951
Cdd:cd14220   76 ENGSLYDFLK-----CTTLDTRALLKLAYSAACGLCHLHTEIygtqgKPAIAHRDLKSKNILIKKNGTCCIADLGLAvkf 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  952 -----RLILPYRTHvttelVGTLGYIPPEY------GQAWVATLRGDVYSFGVVMLEL 998
Cdd:cd14220  151 nsdtnEVDVPLNTR-----VGTKRYMAPEVldeslnKNHFQAYIMADIYSFGLIIWEM 203
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
811-1008 3.39e-10

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: 61.99  E-value: 3.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  811 CGGFGLVYKATLDNgTKLAVKKLTGDYGMMEKEFK-------AEVEVLSRAKHENLVALQGYCVH---DSARILIYSFME 880
Cdd:cd14012    6 SGTFYLVYEVVLDN-SKKPGKFLTSQEYFKTSNGKkqiqlleKELESLKKLRHPNLVSYLAFSIErrgRSDGWKVYLLTE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 --NGSLdywLHENPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLD---GNFKAYVADFGLSRLIL 955
Cdd:cd14012   85 yaPGGS---LSELLDSVGSVPLDTARRWTLQLLEALEYLH---RNGVVHKSLHAGNVLLDrdaGTGIVKLTDYSLGKTLL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425  956 PYRTHVTTELVGTLGYIPPEYGQ-AWVATLRGDVYSFGVVMLELLTGKRPMEVF 1008
Cdd:cd14012  159 DMCSRGSLDEFKQTYWLPPELAQgSKSPTRKTDVWDLGLLFLQMLFGLDVLEKY 212
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
809-1004 3.50e-10

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: 61.86  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVK--KLtgdYGMMEKE-FKAEVEVLSRAKHENLVALqgYCVHDSAR--ILIYSFMENG 882
Cdd:cd14103    1 LGRGKFGTVYRCVeKATGKELAAKfiKC---RKAKDREdVRNEIEIMNQLRHPRLLQL--YDAFETPRemVLVMEYVAGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SL-------DYWLHENpegpaqldwpKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNIL---LDGNfKAYVADFGLSR 952
Cdd:cd14103   76 ELfervvddDFELTER----------DCILFMRQICEGVQYMHK---QGILHLDLKPENILcvsRTGN-QIKIIDFGLAR 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  953 LILPyrTHVTTELVGTLGYIPPE---YGQAWVATlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14103  142 KYDP--DKKLKVLFGTPEFVAPEvvnYEPISYAT---DMWSVGVICYVLLSGLSP 191
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
824-1000 3.52e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 63.94  E-value: 3.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   824 NGTKLAVkkltgdygmmekEFKAEVEVLSRAKHENLVALQ--------GYCVHDSARILIYSFMENGSLDYwlHENPegp 895
Cdd:PHA03210  202 AGSRAAI------------QLENEILALGRLNHENILKIEeilrseanTYMITQKYDFDLYSFMYDEAFDW--KDRP--- 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   896 aqLDWPKRlNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVGTLGYIPPE 975
Cdd:PHA03210  265 --LLKQTR-AIMKQLLCAVEYIH---DKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAFDYGWVGTVATNSPE 338
                         170       180
                  ....*....|....*....|....*..
gi 15218425   976 Y--GQAWVATLrgDVYSFGVVMLELLT 1000
Cdd:PHA03210  339 IlaGDGYCEIT--DIWSCGLILLDMLS 363
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
802-1023 3.73e-10

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: 62.76  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKefkAEVEVLSRAKHENLVAL--------QGYCVHDSAR 872
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCrKADTGKMYAMKCLDKKRIKMKQ---GETLALNERIMLSLVSTgdcpfivcMSYAFHTPDK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 I-LIYSFMENGSLDYWLHENPE-GPAQLDWPKRLNIMrgassGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGL 950
Cdd:cd14223   78 LsFILDLMNGGDLHYHLSQHGVfSEAEMRFYAAEIIL-----GLEHMHS---RFVVYRDLKPANILLDEFGHVRISDLGL 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  951 SRLILPYRTHVTtelVGTLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAWVHTM 1023
Cdd:cd14223  150 ACDFSKKKPHAS---VGTHGYMAPEVLQKGVAyDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTM 220
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
914-1069 3.84e-10

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 62.58  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  914 LAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLI----LPYRTHVTTELVGTLGYIPPE-------Ygqawva 982
Cdd:cd07852  120 LKYLHS---GGVIHRDLKPSNILLNSDCRVKLADFGLARSLsqleEDDENPVLTDYVATRWYRAPEillgstrY------ 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  983 TLRGDVYSFGVVMLELLTGK-------------RPMEVFrPKMSRELVAWVH-----TM-KRDGKPEEVFDTLLRESGNE 1043
Cdd:cd07852  191 TKGVDMWSVGCILGEMLLGKplfpgtstlnqleKIIEVI-GRPSAEDIESIQspfaaTMlESLPPSRPKSLDELFPKASP 269
                        170       180
                 ....*....|....*....|....*.
gi 15218425 1044 EAmlrvLDIACMCVNQNPMKRPNIQQ 1069
Cdd:cd07852  270 DA----LDLLKKLLVFNPNKRLTAEE 291
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
803-1006 3.85e-10

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 61.57  E-value: 3.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMME----KEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd14188    3 YCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKphqrEKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLhenpEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYR 958
Cdd:cd14188   83 CSRRSMAHIL----KARKVLTEPEVRYYLRQIVSGLKYLH---EQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425  959 THVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14188  156 HRRRT-ICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFE 202
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
809-1004 3.85e-10

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: 61.52  E-value: 3.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLD-NGTKLAVKKLTGD----YGMMEKeFKAEVEVLSRAKHENLVALqgYCVHDSAR--ILIYSFMEN 881
Cdd:cd14079   10 LGVGSFGKVKLAEHElTGHKVAVKILNRQkiksLDMEEK-IRREIQILKLFRHPHIIRL--YEVIETPTdiFMVMEYVSG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSL-DYWLHEnpegpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTH 960
Cdd:cd14079   87 GELfDYIVQK-----GRLSEDEARRFFQQIISGVEYCHR---HMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  961 VTTelVGTLGYIPPE------YGQAWVatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14079  159 KTS--CGSPNYAAPEvisgklYAGPEV-----DVWSCGVILYALLCGSLP 201
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
809-1076 4.04e-10

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 61.59  E-value: 4.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN--GTKL--AVKKLTGD----YGMMEkEFKAEVEVLSRAKHENLVALQGyCVHDSARILIYSFME 880
Cdd:cd05040    3 LGDGSFGVVRRGEWTTpsGKVIqvAVKCLKSDvlsqPNAMD-DFLKEVNAMHSLDHPNLIRLYG-VVLSSPLMMVTELAP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHEN-PEGPAQLDWPKRLNImrgaSSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRT 959
Cdd:cd05040   81 LGSLLDRLRKDqGHFLISTLCDYAVQI----ANGMAYLES---KRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNED 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  960 HVTTELVGTLGYippeygqAWVA--TLR-------GDVYSFGVVMLELLT-GKRPmevfrpkmsrelvaWV--------H 1021
Cdd:cd05040  154 HYVMQEHRKVPF-------AWCApeSLKtrkfshaSDVWMFGVTLWEMFTyGEEP--------------WLglngsqilE 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425 1022 TMKRDGK--------PEEVFDTLLResgneeamlrvldiacmCVNQNPMKRPNIQQVVDWLKN 1076
Cdd:cd05040  213 KIDKEGErlerpddcPQDIYNVMLQ-----------------CWAHKPADRPTFVALRDFLPE 258
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
800-1010 4.12e-10

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: 61.95  E-value: 4.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  800 TDNFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMmEKEFKAEVEVL-SRAKHENLVALQGYCVHDSARI---- 873
Cdd:cd06638   17 SDTWEIIETIGKGTYGKVFKVlNKKNGSKAAVKILDPIHDI-DEEIEAEYNILkALSDHPNVVKFYGMYYKKDVKNgdql 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 -LIYSFMENGSLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSR 952
Cdd:cd06638   96 wLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLH---VNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  953 LILPYRTHVTTElVGTLGYIPPEY---GQAWVATL--RGDVYSFGVVMLELLTGKRPMEVFRP 1010
Cdd:cd06638  173 QLTSTRLRRNTS-VGTPFWMAPEViacEQQLDSTYdaRCDVWSLGITAIELGDGDPPLADLHP 234
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
807-1071 4.62e-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: 61.68  E-value: 4.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKA---EVEVLSRAKHENLVALQ-GYCVHDSARILIYSFMENG 882
Cdd:cd08223    6 RVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAaeqEAKLLSKLKHPNIVSYKeSFEGEDGFLYIVMGFCEGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENPEGPAQ----LDWPKRLNImrgassGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRlILPYR 958
Cdd:cd08223   86 DLYTRLKEQKGVLLEerqvVEWFVQIAM------ALQYMH---ERNILHRDLKTQNIFLTKSNIIKVGDLGIAR-VLESS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  959 THVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKrpmEVFRPKMSRELV-----AWVHTMKRDGKPEevf 1033
Cdd:cd08223  156 SDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLK---HAFNAKDMNSLVykileGKLPPMPKQYSPE--- 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15218425 1034 dtllresgneeamlrVLDIACMCVNQNPMKRPNIQQVV 1071
Cdd:cd08223  230 ---------------LGELIKAMLHQDPEKRPSVKRIL 252
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
809-1002 5.27e-10

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: 61.90  E-value: 5.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTgdygmMEKE----FKA--EVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd07870    8 LGEGSYATVYKGiSRINGQLVALKVIS-----MKTEegvpFTAirEASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 gSLDYWLHENPEG--PAQLdwpkRLnIMRGASSGLAYMHQicePHIVHRDIKSSNILLD--GNFKayVADFGLSRL-ILP 956
Cdd:cd07870   83 -DLAQYMIQHPGGlhPYNV----RL-FMFQLLRGLAYIHG---QHILHRDLKPQNLLISylGELK--LADFGLARAkSIP 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  957 YRTHvTTELVgTLGYIPP-------EYGQAWvatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd07870  152 SQTY-SSEVV-TLWYRPPdvllgatDYSSAL------DIWGAGCIFIEMLQGQ 196
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
809-1004 6.12e-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: 61.60  E-value: 6.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAtLDNGTKLAV-------KKLTGDygmMEKEFKAEVEVLSRAKHENLV----ALQGYCVHDSARILIYS 877
Cdd:cd14030   33 IGRGSFKTVYKG-LDTETTVEVawcelqdRKLSKS---ERQRFKEEAGMLKGLQHPNIVrfydSWESTVKGKKCIVLVTE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYWLhenpegpaqldwpKRLNIM---------RGASSGLAYMHQICEPhIVHRDIKSSNILLDG-NFKAYVAD 947
Cdd:cd14030  109 LMTSGTLKTYL-------------KRFKVMkikvlrswcRQILKGLQFLHTRTPP-IIHRDLKCDNIFITGpTGSVKIGD 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  948 FGLSRLilpYRTHVTTELVGTLGYIPPE-YGQAWVATLrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14030  175 LGLATL---KRASFAKSVIGTPEFMAPEmYEEKYDESV--DVYAFGMCMLEMATSEYP 227
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
809-1002 6.89e-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: 61.93  E-value: 6.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL-DNGTKLAVKKLTGDYgmmEKEFKA-----EVEVLSRAKHENLVALQGyCVHDSARI-------LI 875
Cdd:cd07851   23 VGSGAYGQVCSAFDtKTGRKVAIKKLSRPF---QSAIHAkrtyrELRLLKHMKHENVIGLLD-VFTPASSLedfqdvyLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMengslDYWLHenpegpaQLDWPKRLN----------IMRGassgLAYMHQIcepHIVHRDIKSSNILLDGNFKAYV 945
Cdd:cd07851   99 THLM-----GADLN-------NIVKCQKLSddhiqflvyqILRG----LKYIHSA---GIIHRDLKPSNLAVNEDCELKI 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  946 ADFGLSRLIlpyrTHVTTELVGTLGYIPPE-------YGQAwvatlrGDVYSFGVVMLELLTGK 1002
Cdd:cd07851  160 LDFGLARHT----DDEMTGYVATRWYRAPEimlnwmhYNQT------VDIWSVGCIMAELLTGK 213
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
809-1004 7.09e-10

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: 60.76  E-value: 7.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTK--LAVK---KLTGDYGMMEKEFkAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd14121    3 LGSGTYATVYKAYRKSGARevVAVKcvsKSSLNKASTENLL-TEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHEN---PEGPAQldwpkrlNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAY--VADFGLSRLILPyR 958
Cdd:cd14121   82 LSRFIRSRrtlPESTVR-------RFLQQLASALQFLR---EHNISHMDLKPQNLLLSSRYNPVlkLADFGFAQHLKP-N 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425  959 THVTTeLVGTLGYIPPEY--GQAWVAtlRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14121  151 DEAHS-LRGSPLYMAPEMilKKKYDA--RVDLWSVGVILYECLFGRAP 195
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
809-1031 7.98e-10

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 61.12  E-value: 7.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTK---LAVKKL-TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCvHDSARILIYSFMENGSL 884
Cdd:cd05115   12 LGSGNFGCVKKGVYKMRKKqidVAIKVLkQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVC-EAEALMLVMEMASGGPL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTE 964
Cdd:cd05115   91 NKFLSGKKD---EITVSNVVELMHQVSMGMKYLE---EKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKAR 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LVGT--LGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWVHTMKRDGKPEE 1031
Cdd:cd05115  165 SAGKwpLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKP---YKKMKGPEVMSFIEQGKRMDCPAE 231
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
803-1006 8.28e-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: 60.72  E-value: 8.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT-LDN----GTKLAVKKLTGDYGMMEKeFKAEVEVLSRAKHENLVALQGYCVHDSARILIYS 877
Cdd:cd14187    9 YVRGRFLGKGGFAKCYEITdADTkevfAGKIVPKSLLLKPHQKEK-MSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLdYWLHENPEGPAQldwPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIlPY 957
Cdd:cd14187   88 LCRRRSL-LELHKRRKALTE---PEARYYLRQIILGCQYLHR---NRVIHRDLKLGNLFLNDDMEVKIGDFGLATKV-EY 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15218425  958 RTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14187  160 DGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFE 208
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
809-1002 8.50e-10

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: 61.62  E-value: 8.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTG--DYGMMEKEFKAEVEVLSRAKHENLVALQGyCVHDSAR------ILIYSFM 879
Cdd:cd07858   13 IGRGAYGIVCSAKnSETNEKVAIKKIANafDNRIDAKRTLREIKLLRHLDHENVIAIKD-IMPPPHReafndvYIVYELM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 engslDYWLHENPEGPAQL--DWPKRL--NIMRGassgLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL 955
Cdd:cd07858   92 -----DTDLHQIIRSSQTLsdDHCQYFlyQLLRG----LKYIHS---ANVLHRDLKPSNLLLNANCDLKICDFGLARTTS 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425  956 PyRTHVTTELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd07858  160 E-KGDFMTEYVVTRWYRAPElllncseYTTAI------DVWSVGCIFAELLGRK 206
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
847-1005 8.58e-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: 61.18  E-value: 8.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  847 EVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYwlhenpegpaqLDWPKRLNIMRGAS-------SGLAYMHq 919
Cdd:cd07871   53 EVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDSDLKQY-----------LDNCGNLMSMHNVKifmfqllRGLSYCH- 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  920 icEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL-ILPYRTHvTTELVgTLGYIPPE--YGQAWVATlRGDVYSFGVVML 996
Cdd:cd07871  121 --KRKILHRDLKPQNLLINEKGELKLADFGLARAkSVPTKTY-SNEVV-TLWYRPPDvlLGSTEYST-PIDMWGVGCILY 195

                 ....*....
gi 15218425  997 ELLTGkRPM 1005
Cdd:cd07871  196 EMATG-RPM 203
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
852-1077 8.78e-10

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 60.58  E-value: 8.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  852 SRAKHENLVALQG------YCVHDSARILIysFMENGSLDywLHENPEgpAQLDWPKRLNIMRGASSGLAYMHQIcepHI 925
Cdd:cd13975   53 SLPKHERIVSLHGsvidysYGGGSSIAVLL--IMERLHRD--LYTGIK--AGLSLEERLQIALDVVEGIRFLHSQ---GL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  926 VHRDIKSSNILLDGNFKAYVADFGLSRlilPyRTHVTTELVGTLGYIPPEygqawvaTLRG------DVYSFGVVMLELL 999
Cdd:cd13975  124 VHRDIKLKNVLLDKKNRAKITDLGFCK---P-EAMMSGSIVGTPIHMAPE-------LFSGkydnsvDVYAFGILFWYLC 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425 1000 TGK-RPMEVFRPKMSRELVaWvHTMKRDGKPEEvfdtllresgneeamLRVLDIAC-----MCVNQNPMKRPNIQQVVDW 1073
Cdd:cd13975  193 AGHvKLPEAFEQCASKDHL-W-NNVRKGVRPER---------------LPVFDEECwnlmeACWSGDPSQRPLLGIVQPK 255

                 ....
gi 15218425 1074 LKNI 1077
Cdd:cd13975  256 LQGI 259
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
796-1017 8.81e-10

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: 61.19  E-value: 8.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  796 LLKATDnFSQANIIGCGGFGLVYKAT-LDNGTKL----AVKKLTGDYG-MMEKEFKAEVEVLSRAKHENLVALQGYCVHD 869
Cdd:cd05109    3 ILKETE-LKKVKVLGSGAFGTVYKGIwIPDGENVkipvAIKVLRENTSpKANKEILDEAYVMAGVGSPYVCRLLGICLTS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  870 SARiLIYSFMENGSLDYWLHENPEGPAQLDWpkrLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd05109   82 TVQ-LVTQLMPYGCLLDYVRENKDRIGSQDL---LNWCVQIAKGMSYLEEV---RLVHRDLAARNVLVKSPNHVKITDFG 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  950 LSRLIlpyrTHVTTELVGTLGYIPPEygqaWVA---------TLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELV 1017
Cdd:cd05109  155 LARLL----DIDETEYHADGGKVPIK----WMAlesilhrrfTHQSDVWSYGVTVWELMTfGAKPYDGIPAREIPDLL 224
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
809-998 9.32e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 61.22  E-value: 9.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLdNGTKLAVKKLtgdYGMMEKEFKAEVEVLSRA--KHENLValqGYCVHD-------SARILIYSFM 879
Cdd:cd14219   13 IGKGRYGEVWMGKW-RGEKVAVKVF---FTTEEASWFRETEIYQTVlmRHENIL---GFIAADikgtgswTQLYLITDYH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSLDYWLHENpegpaQLDWPKRLNIMRGASSGLAYMHQIC-----EPHIVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd14219   86 ENGSLYDYLKST-----TLDTKAMLKLAYSSVSGLCHLHTEIfstqgKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKF 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  955 LPYRTHVTTEL---VGTLGYIPPE---------YGQAWVAtlrGDVYSFGVVMLEL 998
Cdd:cd14219  161 ISDTNEVDIPPntrVGTKRYMPPEvldeslnrnHFQSYIM---ADMYSFGLILWEV 213
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
784-1002 1.00e-09

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: 61.46  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  784 SRYEVKDlTIFELLKatdNFSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYG--MMEKEFKAEVEVLSRAKHENLV 860
Cdd:cd07879    2 YREEVNK-TVWELPE---RYTSLKQVGSGAYGSVCSAIdKRTGEKVAIKKLSRPFQseIFAKRAYRELTLLKHMQHENVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  861 ALQGycVHDSARI--------LIYSFMENGSLDYWLHENPEGPAQLdwpkrlnIMRGASSGLAYMHQicePHIVHRDIKS 932
Cdd:cd07879   78 GLLD--VFTSAVSgdefqdfyLVMPYMQTDLQKIMGHPLSEDKVQY-------LVYQMLCGLKYIHS---AGIIHRDLKP 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  933 SNILLDGNFKAYVADFGLSRlilpyrtHVTTELVG---TLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLTGK 1002
Cdd:cd07879  146 GNLAVNEDCELKILDFGLAR-------HADAEMTGyvvTRWYRAPEVILNWMHyNQTVDIWSVGCIMAEMLTGK 212
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
925-1071 1.02e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 62.34  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   925 IVHRDIKSSNILLDGNFKAYVADFGLSRlilPYRTHVT----TELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT 1000
Cdd:PTZ00267  190 MMHRDLKSANIFLMPTGIIKLGDFGFSK---QYSDSVSldvaSSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLT 266
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  1001 GKRPmevFRPKMSRELVAWVHTMKRDGKPEEVFDTLlresgneEAMLRVLdiacmcVNQNPMKRPNIQQVV 1071
Cdd:PTZ00267  267 LHRP---FKGPSQREIMQQVLYGKYDPFPCPVSSGM-------KALLDPL------LSKNPALRPTTQQLL 321
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
801-1004 1.05e-09

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 61.21  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE----FKAEVEVLSRAKHENLVALQgycvhdsariliY 876
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAetacFREERDVLVNGDRRWITKLH------------Y 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSL----DYWL----------HEN--PEGPAQLdwpkRLNIMRGASSGLaymHQIcepHIVHRDIKSSNILLDGN 940
Cdd:cd05597   69 AFQDENYLylvmDYYCggdlltllskFEDrlPEEMARF----YLAEMVLAIDSI---HQL---GYVHRDIKPDNVLLDRN 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  941 FKAYVADFGLSRLILPYRTHVTTELVGTLGYIPPEYGQAwVATLRG------DVYSFGVVMLELLTGKRP 1004
Cdd:cd05597  139 GHIRLADFGSCLKLREDGTVQSSVAVGTPDYISPEILQA-MEDGKGrygpecDWWSLGVCMYEMLYGETP 207
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
809-949 1.19e-09

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 57.45  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAK-HE-NLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd13968    1 MGEGASAKVFWAeGECTTIGVAVKIGDDVNNEEGEDLESEMDILRRLKgLElNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  886 YWLHENPEGPAQLDwpkrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd13968   81 AYTQEEELDEKDVE-----SIMYQLAECMRLLHSF---HLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
801-1016 1.19e-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: 61.23  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKefkAEVEVLSRAKHENLVAL--------QGYCVHDSA 871
Cdd:cd05633    5 NDFSVHRIIGRGGFGEVYGCrKADTGKMYAMKCLDKKRIKMKQ---GETLALNERIMLSLVSTgdcpfivcMTYAFHTPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  872 RI-LIYSFMENGSLDYWLHENPEGPAQLdwpkrlniMRGASS----GLAYMHQicePHIVHRDIKSSNILLDGNFKAYVA 946
Cdd:cd05633   82 KLcFILDLMNGGDLHYHLSQHGVFSEKE--------MRFYATeiilGLEHMHN---RFVVYRDLKPANILLDEHGHVRIS 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  947 DFGLSRLILPYRTHVTtelVGTLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLTGKRPMEVFRPKMSREL 1016
Cdd:cd05633  151 DLGLACDFSKKKPHAS---VGTHGYMAPEVLQKGTAyDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEI 218
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
806-1077 1.38e-09

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 60.41  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  806 ANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd14153    5 GELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHenpEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDgNFKAYVADFGL-------------SR 952
Cdd:cd14153   85 SVVR---DAKVVLDVNKTRQIAQEIVKGMGYLHA---KGILHKDLKSKNVFYD-NGKVVITDFGLftisgvlqagrreDK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  953 LILP--YRTHVTTELVGTLGyipPEYGQAWVA-TLRGDVYSFGVVMLELLTGKRPMEVfRPKmsrELVAWvhTMKRDGKP 1029
Cdd:cd14153  158 LRIQsgWLCHLAPEIIRQLS---PETEEDKLPfSKHSDVFAFGTIWYELHAREWPFKT-QPA---EAIIW--QVGSGMKP 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425 1030 eevfdtLLRESGNEEamlRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14153  229 ------NLSQIGMGK---EISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
808-1079 1.41e-09

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 60.60  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSR-AKHENLVALQGYCV-------HDSARILIYSF 878
Cdd:cd14036    7 VIAEGGFAFVYEAQdVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKlSGHPNIVQFCSAASigkeesdQGQAEYLLLTE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSL-DYWLHENPEGPAQLDwpKRLNIMRGASSGLAYMHQIcEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPY 957
Cdd:cd14036   87 LCKGQLvDFVKKVEAPGPFSPD--TVLKIFYQTCRAVQHMHKQ-SPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  958 ---------RTHVTTEL--VGTLGYIPPEYGQAWV---ATLRGDVYSFGVVMLELLTGKRPmevFRPKMSRELVAWVHTM 1023
Cdd:cd14036  164 pdyswsaqkRSLVEDEItrNTTPMYRTPEMIDLYSnypIGEKQDIWALGCILYLLCFRKHP---FEDGAKLRIINAKYTI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425 1024 KRDGKPEEVFDTLLResgneeAMLRVldiacmcvnqNPMKRPNIQQVVDWLKNIEA 1079
Cdd:cd14036  241 PPNDTQYTVFHDLIR------STLKV----------NPEERLSITEIVEQLQELAA 280
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
801-1004 1.51e-09

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: 60.04  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKK--LTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVhdsARILIYSF 878
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkfLKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFE---TRKEYFIF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSldywlhenpeGPAQLDW---------PKRLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDG---NFKAYVA 946
Cdd:cd14088   78 LELAT----------GREVFDWildqgyyseRDTSNVIRQVLEAVAYLHSLK---IVHRNLKLENLVYYNrlkNSKIVIS 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  947 DFGLSRLilpyRTHVTTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14088  145 DFHLAKL----ENGLIKEPCGTPEYLAPEvvgrqrYGRPV------DCWAIGVIMYILLSGNPP 198
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
784-1072 1.56e-09

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: 60.27  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  784 SRYevkdLTIFELLKatdnfsqanIIGCGGFGLVYKA--TLDNGTkLAVKK-LTGDYGMMEKEFKAEVEVLSRAKHENLV 860
Cdd:cd14048    2 SRF----LTDFEPIQ---------CLGRGGFGVVFEAknKVDDCN-YAVKRiRLPNNELAREKVLREVRALAKLDHPGIV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  861 AL---------QGYCVHDSArILIYSFME---NGSLDYWLHENPEGPAQlDWPKRLNIMRGASSGLAYMHqicEPHIVHR 928
Cdd:cd14048   68 RYfnawlerppEGWQEKMDE-VYLYIQMQlcrKENLKDWMNRRCTMESR-ELFVCLNIFKQIASAVEYLH---SKGLIHR 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  929 DIKSSNIL--LDGNFKayVADFGLS-------------RLILPYRTHvtTELVGTLGYIPPEYGQAWVATLRGDVYSFGV 993
Cdd:cd14048  143 DLKPSNVFfsLDDVVK--VGDFGLVtamdqgepeqtvlTPMPAYAKH--TGQVGTRLYMSPEQIHGNQYSEKVDIFALGL 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  994 VMLELLTGkrpmevFRPKMSRelvawVHTMK--RDGKpeevFDTLLRESGNEEAMLrVLDIacmcVNQNPMKRPNIQQVV 1071
Cdd:cd14048  219 ILFELIYS------FSTQMER-----IRTLTdvRKLK----FPALFTNKYPEERDM-VQQM----LSPSPSERPEAHEVI 278

                 .
gi 15218425 1072 D 1072
Cdd:cd14048  279 E 279
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
802-1004 1.70e-09

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: 59.93  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT-LDNGTKLAVKkLTGDYGMMEKEFKA-EVEVLSRAKHENLVALQGYCVHDSARILIYSFM 879
Cdd:cd14190    5 SIHSKEVLGGGKFGKVHTCTeKRTGLKLAAK-VINKQNSKDKEMVLlEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  880 ENGSLDYWLHENPEGPAQLDwpkRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL--DGNFKAYVADFGLSRLILPy 957
Cdd:cd14190   84 EGGELFERIVDEDYHLTEVD---AMVFVRQICEGIQFMHQM---RVLHLDLKPENILCvnRTGHQVKIIDFGLARRYNP- 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425  958 RTHVTTELvGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14190  157 REKLKVNF-GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSP 202
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
812-948 1.82e-09

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 60.39  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  812 GGFGLVYKATlDNGTKLAVKKLTGDYGMME--KEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWLH 889
Cdd:cd08216   13 GGVVHLAKHK-PTNTLVAVKKINLESDSKEdlKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLLK 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  890 EN-PEGpaqldWPKRL--NIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADF 948
Cdd:cd08216   92 THfPEG-----LPELAiaFILRDVLNALEYIHSK---GYIHRSVKASHILISGDGKVVLSGL 145
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
801-1004 1.91e-09

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: 60.04  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQaniIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVAL-QGYCVHDSARIlIYSF 878
Cdd:cd06657   23 DNFIK---IGEGSTGIVCIATVKSSGKLvAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMyNSYLVGDELWV-VMEF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSL-DYWLHenpegpaqldwpKRLNIMRGASSGLAYMHQICEPH---IVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd06657   99 LEGGALtDIVTH------------TRMNEEQIAAVCLAVLKALSVLHaqgVIHRDIKSDSILLTHDGRVKLSDFGFCAQV 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  955 ---LPYRthvtTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd06657  167 skeVPRR----KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPP 215
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
809-1015 1.92e-09

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: 59.56  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-----LDNGTKLAVKKLTGDYGMMEKEFK--AEVEVLSRA---KHENLVALQGYCVHDSARILIysf 878
Cdd:cd14005    8 LGKGGFGTVYSGVrirdgLPVAVKFVPKSRVTEWAMINGPVPvpLEIALLLKAskpGVPGVIRLLDWYERPDGFLLI--- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGS-----LDYWLHENP--EGPAQldwpkrlNIMRGAssgLAYMHQICEPHIVHRDIKSSNILLD---GNFKayVADF 948
Cdd:cd14005   85 MERPEpcqdlFDFITERGAlsENLAR-------IIFRQV---VEAVRHCHQRGVLHRDIKDENLLINlrtGEVK--LIDF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  949 GLSRLIlpyRTHVTTELVGTLGYIPPEYGQ-----AWVATlrgdVYSFGVVMLELLTGKRPME----------VFRPKMS 1013
Cdd:cd14005  153 GCGALL---KDSVYTDFDGTRVYSPPEWIRhgryhGRPAT----VWSLGILLYDMLCGDIPFEndeqilrgnvLFRPRLS 225

                 ..
gi 15218425 1014 RE 1015
Cdd:cd14005  226 KE 227
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
794-1004 2.15e-09

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: 59.90  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  794 FELLKatdnfsqanIIGCGGFGLVYKA-TLDNGTKLAVKkltgdygMMEKE----------FKAEVEVLSRAKHENLVAL 862
Cdd:cd05580    3 FEFLK---------TLGTGSFGRVRLVkHKDSGKYYALK-------ILKKAkiiklkqvehVLNEKRILSEVRHPFIVNL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  863 QGYCVHDSARILIYSFMENGSLDYWLHEN---PEGPAQLdwpkrlnimrGASS---GLAYMHQIcepHIVHRDIKSSNIL 936
Cdd:cd05580   67 LGSFQDDRNLYMVMEYVPGGELFSLLRRSgrfPNDVAKF----------YAAEvvlALEYLHSL---DIVYRDLKPENLL 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  937 LD--GNFKayVADFGLSRlILPYRTHVtteLVGTLGYIPPE------YGQAwvatlrGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05580  134 LDsdGHIK--ITDFGFAK-RVKDRTYT---LCGTPEYLAPEiilskgHGKA------VDWWALGILIYEMLAGYPP 197
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
826-1071 2.44e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. 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. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 59.42  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  826 TKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSArILIYSFMENGSLDYWLHENPEGPAqLDWpkRLN 905
Cdd:cd05037   31 VEVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVADEN-IMVQEYVRYGPLDKYLRRMGNNVP-LSW--KLQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  906 IMRGASSGLAYMHqicEPHIVHRDIKSSNILL-----DGN--FkAYVADFGLSRLILPyrthvTTELVGTLGYIPPEY-- 976
Cdd:cd05037  107 VAKQLASALHYLE---DKKLIHGNVRGRNILLareglDGYppF-IKLSDPGVPITVLS-----REERVDRIPWIAPEClr 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  977 GQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRPkmSRELvawvhtmkrdgkpeevfdtLLRESGNEEAMLRVLDIACM 1055
Cdd:cd05037  178 NLQANLTIAADKWSFGTTLWEICSgGEEPLSALSS--QEKL-------------------QFYEDQHQLPAPDCAELAEL 236
                        250
                 ....*....|....*....
gi 15218425 1056 ---CVNQNPMKRPNIQQVV 1071
Cdd:cd05037  237 imqCWTYEPTKRPSFRAIL 255
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
801-1004 2.46e-09

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: 59.67  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQaniIGCGGFGLVYKATLDN-GTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVAL-QGYCVHDSARILIySF 878
Cdd:cd06658   25 DSFIK---IGEGSTGIVCIATEKHtGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMyNSYLVGDELWVVM-EF 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSL-DYWLHE--NPEGPAQLdwpkRLNIMRGassgLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLI- 954
Cdd:cd06658  101 LEGGALtDIVTHTrmNEEQIATV----CLSVLRA----LSYLHN---QGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVs 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  955 --LPYRthvtTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd06658  170 keVPKR----KSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPP 217
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
801-1019 2.70e-09

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 60.96  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   801 DNFSQANIIGCGGFGLVYKATLDN-----GTKLAVKKLTgDYGmmekefKAEVEVLSRAKHenlvALQGYCVHdsariLI 875
Cdd:PLN03225  132 DDFVLGKKLGEGAFGVVYKASLVNkqskkEGKYVLKKAT-EYG------AVEIWMNERVRR----ACPNSCAD-----FV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   876 YSFMENGSLD----YWLHENPEGPAQL----------------------DWPK---RLN-----IMRGASSGLAYMHQIc 921
Cdd:PLN03225  196 YGFLEPVSSKkedeYWLVWRYEGESTLadlmqskefpynvepyllgkvqDLPKgleRENkiiqtIMRQILFALDGLHST- 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   922 epHIVHRDIKSSNILLD---GNFKayVADFGlsrlilpyrthVTTELVGTLGYIP---------------------PEYG 977
Cdd:PLN03225  275 --GIVHRDVKPQNIIFSegsGSFK--IIDLG-----------AAADLRVGINYIPkeflldpryaapeqyimstqtPSAP 339
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425   978 QAWVATL------------RGDVYSFGVVMLEL----LTGKRPMEVFRPKMSR---ELVAW 1019
Cdd:PLN03225  340 SAPVATAlspvlwqlnlpdRFDIYSAGLIFLQMafpnLRSDSNLIQFNRQLKRndyDLVAW 400
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
803-1072 3.02e-09

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: 58.86  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT-LDNGTKLAVKK----LTGDYGMMEKefKAEVEvlsraKHENLvALQGYCVH------DSA 871
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRsREDGKLYAVKRsrsrFRGEKDRKRK--LEEVE-----RHEKL-GEHPNCVRfikaweEKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  872 RILIYSFMENGSLDYWLHENPEGPAQLDWpkrlNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL--DGNFKayVADFG 949
Cdd:cd14050   75 ILYIQTELCDTSLQQYCEETHSLPESEVW----NILLDLLKGLKHLH---DHGLIHLDIKPANIFLskDGVCK--LGDFG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  950 LsrLILPYRTHVTTELVGTLGYIPPEYGQAwVATLRGDVYSFGVVMLELLTGkrpMEVfrPKmsrELVAWvHTMKRDGKP 1029
Cdd:cd14050  146 L--VVELDKEDIHDAQEGDPRYMAPELLQG-SFTKAADIFSLGITILELACN---LEL--PS---GGDGW-HQLRQGYLP 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 15218425 1030 EEVFDTLLREsgneeamLRVLdIACMcVNQNPMKRPNIQQVVD 1072
Cdd:cd14050  214 EEFTAGLSPE-------LRSI-IKLM-MDPDPERRPTAEDLLA 247
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
809-1009 3.16e-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: 59.28  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTK-LAVKKL---TGDYGMMEKEFKaEVEVLSRAK---HENLVALQGYCV-----HDSARILI 875
Cdd:cd07862    9 IGEGAYGKVFKArDLKNGGRfVALKRVrvqTGEEGMPLSTIR-EVAVLRHLEtfeHPNVVRLFDVCTvsrtdRETKLTLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENgSLDYWLHENPEGPAQLDWPKrlNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRlIL 955
Cdd:cd07862   88 FEHVDQ-DLTTYLDKVPEPGVPTETIK--DMMFQLLRGLDFLHS---HRVVHRDLKPQNILVTSSGQIKLADFGLAR-IY 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  956 PYRThVTTELVGTLGYIPPE-YGQAWVATlRGDVYSFGVVMLELLTgKRPMevFR 1009
Cdd:cd07862  161 SFQM-ALTSVVVTLWYRAPEvLLQSSYAT-PVDLWSVGCIFAEMFR-RKPL--FR 210
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
856-1080 3.60e-09

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 59.00  E-value: 3.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  856 HENLVALQGYCVHDSAR-ILIYSFMENGSLDYWLHENPEGPAQ----LDWPKRLNIMRGASSGLAYMHQIcepHIVHRDI 930
Cdd:cd05043   66 HQNLLPILHVCIEDGEKpMVLYPYMNWGNLKLFLQQCRLSEANnpqaLSTQQLVHMALQIACGMSYLHRR---GVIHKDI 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  931 KSSNILLDGNFKAYVADFGLSRLILPYRTHvttelvgTLG--------YIPPEYGQAWVATLRGDVYSFGVVMLELLT-G 1001
Cdd:cd05043  143 AARNCVIDDELQVKITDNALSRDLFPMDYH-------CLGdnenrpikWMSLESLVNKEYSSASDVWSFGVLLWELMTlG 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425 1002 KRPMEVFRPKmsrELVAWVhtmkRDGK--------PEEVFdtllresgneEAMlrvldiACmCVNQNPMKRPNIQQVVDW 1073
Cdd:cd05043  216 QTPYVEIDPF---EMAAYL----KDGYrlaqpincPDELF----------AVM------AC-CWALDPEERPSFQQLVQC 271

                 ....*..
gi 15218425 1074 LKNIEAE 1080
Cdd:cd05043  272 LTDFHAQ 278
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
795-1004 3.80e-09

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: 58.79  E-value: 3.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  795 ELLKATDNFSQANIIGCGGFGLVYKAT-LDNGTKLAVKkltgdygMMEKEFKA---------EVEVLSRAKhENLVALQG 864
Cdd:cd14197    3 EPFQERYSLSPGRELGRGKFAVVRKCVeKDSGKEFAAK-------FMRKRRKGqdcrmeiihEIAVLELAQ-ANPWVINL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  865 YCVHDSAR--ILIYSFMENGSL-DYWLHENPEGPAQLDwPKRLniMRGASSGLAYMHQicePHIVHRDIKSSNILLD--- 938
Cdd:cd14197   75 HEVYETASemILVLEYAAGGEIfNQCVADREEAFKEKD-VKRL--MKQILEGVSFLHN---NNVVHLDLKPQNILLTses 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  939 --GNFKayVADFGLSRLIlpYRTHVTTELVGTLGYIPPE---YGQAWVATlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14197  149 plGDIK--IVDFGLSRIL--KNSEELREIMGTPEYVAPEilsYEPISTAT---DMWSIGVLAYVMLTGISP 212
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
854-1006 3.82e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 58.71  E-value: 3.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   854 AKHENLVALQgYCVH-DSARILIYSFMENGSL-DYWLHENPegpaqLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIK 931
Cdd:PHA03390   66 KDNPNFIKLY-YSVTtLKGHVLIMDYIKDGDLfDLLKKEGK-----LSEAEVKKIIRQLVEALNDLHKH---NIIHNDIK 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   932 SSNILLDGN-FKAYVADFGLSRLIlpyrtHVTTELVGTLGYIPPEygqawvaTLRGDVY--SF-----GVVMLELLTGKR 1003
Cdd:PHA03390  137 LENVLYDRAkDRIYLCDYGLCKII-----GTPSCYDGTLDYFSPE-------KIKGHNYdvSFdwwavGVLTYELLTGKH 204

                  ...
gi 15218425  1004 PME 1006
Cdd:PHA03390  205 PFK 207
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
803-1017 4.64e-09

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: 58.91  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVY----KATldnGTKLAVKKLtgdygmmEK--------EFKA--EVEVLSRAKHENLVALQ-GYCV 867
Cdd:cd05605    2 FRQYRVLGKGGFGEVCacqvRAT---GKMYACKKL-------EKkrikkrkgEAMAlnEKQILEKVNSRFVVSLAyAYET 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  868 HDsARILIYSFMENGSLDYWLHEnpEGPAQLDwPKRLnIMRGA--SSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYV 945
Cdd:cd05605   72 KD-ALCLVLTIMNGGDLKFHIYN--MGNPGFE-EERA-VFYAAeiTCGLEHLHS---ERIVYRDLKPENILLDDHGHVRI 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  946 ADFGLSRLILPYRThvTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELV 1017
Cdd:cd05605  144 SDLGLAVEIPEGET--IRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEV 213
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
913-1004 5.25e-09

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: 58.95  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  913 GLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILpYRTHVTTELVGTLGYIPPEygqawVATLRG-----D 987
Cdd:cd05582  109 ALDHLHSL---GIIYRDLKPENILLDEDGHIKLTDFGLSKESI-DHEKKAYSFCGTVEYMAPE-----VVNRRGhtqsaD 179
                         90
                 ....*....|....*..
gi 15218425  988 VYSFGVVMLELLTGKRP 1004
Cdd:cd05582  180 WWSFGVLMFEMLTGSLP 196
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
808-1004 5.37e-09

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: 58.42  E-value: 5.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVK-----KLTGDYGMMEkefkAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd14185    7 TIGDGNFAVVKECRhWNENQEYAMKiidksKLKGKEDMIE----SEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHEN---PEGPAQLdwpkrlnIMRGASSGLAYMHqicEPHIVHRDIKSSNILL----DGNFKAYVADFGLSRLI 954
Cdd:cd14185   83 GDLFDAIIESvkfTEHDAAL-------MIIDLCEALVYIH---SKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYV 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 lpyrTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14185  153 ----TGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPP 198
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
807-1004 5.47e-09

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 58.29  E-value: 5.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDYGMMEkefkaEVEVLSRAKHENLValQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd14109   10 EDEKRAAQGAPFHVTeRSTGRNFLAQLRYGDPFLMR-----EVDIHNSLDHPNIV--QMHDAYDDEKLAVTVIDNLASTI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YWLHENpeGPAQLDWPKRLNI---MRGASSGLAYMHqicEPHIVHRDIKSSNILL-DGNFKayVADFGLSRLILpyRTHV 961
Cdd:cd14109   83 ELVRDN--LLPGKDYYTERQVavfVRQLLLALKHMH---DLGIAHLDLRPEDILLqDDKLK--LADFGQSRRLL--RGKL 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15218425  962 TTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14109  154 TTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISP 196
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
809-1031 5.60e-09

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: 58.24  E-value: 5.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKkltgdygmMEKEFKA------EVEVLSRakhenlvaLQG---------YCVHDSAR 872
Cdd:cd14016    8 IGSGSFGEVYLGIdLKTGEEVAIK--------IEKKDSKhpqleyEAKVYKL--------LQGgpgiprlywFGQEGDYN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 ILIYSFMenG-SLDYwlhenpegpaQLDWPKR-------LNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKA- 943
Cdd:cd14016   72 VMVMDLL--GpSLED----------LFNKCGRkfslktvLMLADQMISRLEYLHSK---GYIHRDIKPENFLMGLGKNSn 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  944 --YVADFGLSRlilPYRTHVTTE---------LVGTLGYippeygqAWVATLRG-------DVYSFGVVMLELLTGKRPM 1005
Cdd:cd14016  137 kvYLIDFGLAK---KYRDPRTGKhipyregksLTGTARY-------ASINAHLGieqsrrdDLESLGYVLIYFLKGSLPW 206
                        250       260
                 ....*....|....*....|....*.
gi 15218425 1006 EVFRPKMSRELVAWVHTMKRDGKPEE 1031
Cdd:cd14016  207 QGLKAQSKKEKYEKIGEKKMNTSPEE 232
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
809-949 5.74e-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: 5.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN------GTKLAVKKLTgDYGMMEKEFKaevEVLSRAKHENLVALQGYCVHDSARIL-------- 874
Cdd:cd14013    3 LGEGGFGTVYKGSLLQkdpggeKRRVVLKKAK-EYGEVEIWMN---ERVRRACPSSCAEFVGAFLDTTSKKFtkpslwlv 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 --------IYSFMENGSLDYWLHE--------NPEGPAQlDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL- 937
Cdd:cd14013   79 wkyegdatLADLMQGKEFPYNLEPiifgrvliPPRGPKR-ENVIIKSIMRQILVALRKLHST---GIVHRDVKPQNIIVs 154
                        170
                 ....*....|....
gi 15218425  938 --DGNFKayVADFG 949
Cdd:cd14013  155 egDGQFK--IIDLG 166
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
803-1004 6.03e-09

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: 58.91  E-value: 6.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE--FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFME 880
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKEssIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHEN---PEGPAQldwpkrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL---DGNFKAYVADFGLSRli 954
Cdd:cd14168   92 GGELFDRIVEKgfyTEKDAS-------TLIRQVLDAVYYLHRM---GIVHRDLKPENLLYfsqDEESKIMISDFGLSK-- 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 LPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14168  160 MEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPP 209
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
802-1014 6.70e-09

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: 58.60  E-value: 6.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKAT--LDNGTKLAVK-----KLTGD--YGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSAR 872
Cdd:cd14096    2 NYRLINKIGEGAFSNVYKAVplRNTGKPVAIKvvrkaDLSSDnlKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 ILIYSFMENGSLdywLHEnpegPAQL-----DWPKrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLD--------- 938
Cdd:cd14096   82 YIVLELADGGEI---FHQ----IVRLtyfseDLSR--HVITQVASAVKYLHEI---GVVHRDIKPENLLFEpipfipsiv 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  939 --------------GNF----------KAYVADFGLSRLILPYRTHVTtelVGTLGYIPPEYGQAWVATLRGDVYSFGVV 994
Cdd:cd14096  150 klrkadddetkvdeGEFipgvggggigIVKLADFGLSKQVWDSNTKTP---CGTVGYTAPEVVKDERYSKKVDMWALGCV 226
                        250       260
                 ....*....|....*....|....*
gi 15218425  995 MLELLTGKRP-----MEVFRPKMSR 1014
Cdd:cd14096  227 LYTLLCGFPPfydesIETLTEKISR 251
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
803-1075 6.90e-09

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: 57.94  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGD----YGMMEKEFKAEVEVL------SRAKHENLVAL-------QG 864
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGhRISDGLQVAIKQISRNrvqqWSKLPGVNPVPNEVAllqsvgGGPGHRGVIRLldwfeipEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  865 YCV----HDSARILIYSFMENGSLdywlhenPEGPAQLDWpkrlnimrgassgLAYMHQICEPH---IVHRDIKSSNILL 937
Cdd:cd14101   82 FLLvlerPQHCQDLFDYITERGAL-------DESLARRFF-------------KQVVEAVQHCHskgVVHRDIKDENILV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  938 D---GNFKayVADFGLSRLIlpyRTHVTTELVGTLGYIPPEygqaWVAT-----LRGDVYSFGVVMLELLTGKRPMEvfr 1009
Cdd:cd14101  142 DlrtGDIK--LIDFGSGATL---KDSMYTDFDGTRVYSPPE----WILYhqyhaLPATVWSLGILLYDMVCGDIPFE--- 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425 1010 pkMSRELVAwvhtmkrdGKPEevFDTllRESGNEEAMLrvldiaCMCVNQNPMKRPNIQQVV--DWLK 1075
Cdd:cd14101  210 --RDTDILK--------AKPS--FNK--RVSNDCRSLI------RSCLAYNPSDRPSLEQILlhPWMM 257
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
808-1004 7.06e-09

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: 58.83  E-value: 7.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLD-NGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRA-KHENLVALQgYCVHDSARI-LIYSFMEN 881
Cdd:cd05603    2 VIGKGSFGKVLLAKRKcDGKFYAVKVLQKKTILKKKEQNhimAERNVLLKNlKHPFLVGLH-YSFQTSEKLyFVLDYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRL-ILPYRTh 960
Cdd:cd05603   81 GELFFHLQRE----RCFLEPRARFYAAEVASAIGYLHSL---NIIYRDLKPENILLDCQGHVVLTDFGLCKEgMEPEET- 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15218425  961 vTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05603  153 -TSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPP 195
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
841-1065 7.12e-09

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 58.01  E-value: 7.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  841 EKEFKAEVEVLSRAKHENLVALQGYCV---HDSAR-ILIYSFMENGSLDYWLHENPEGPAQLD---WpKR--LNIMrgas 911
Cdd:cd14035   39 EDKIKTMFENLTLVDHPNIVKFHKYWLdvkDNHARvVFITEYVSSGSLKQFLKKTKKNHKTMNaraW-KRwcTQIL---- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  912 SGLAYMHQiCEPHIVHRDIKSSNILLDGN---------FKAYVADFGLSRLILPYRTHvtTELVGTLGYIPPEYGQAWVA 982
Cdd:cd14035  114 SALSYLHS-CEPPIIHGNLTSDTIFIQHNglikigsvwHRLFVNVLPEGGVRGPLRQE--REELRNLHFFPPEYGSCEDG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  983 TLRgDVYSFGVVMLElltgkrpMEVFRPKMSRELVAWVHTMKRDGKPEEvfDTLLREsgneeamlrvldIACMCVNQNPM 1062
Cdd:cd14035  191 TAV-DIFSFGMCALE-------MAVLEIQANGDTRVSEEAIARARHSLE--DPNMRE------------FILSCLRHNPC 248

                 ...
gi 15218425 1063 KRP 1065
Cdd:cd14035  249 KRP 251
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
808-1016 7.28e-09

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: 58.22  E-value: 7.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVY---KAtlDNGTKLAVKKLTGDYGMMEKefkAEVEVLSRAKHENLVALQG---------YCVHDSARI-L 874
Cdd:cd05606    1 IIGRGGFGEVYgcrKA--DTGKMYAMKCLDKKRIKMKQ---GETLALNERIMLSLVSTGGdcpfivcmtYAFQTPDKLcF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYWLHEN-----PEgpaqldwpkrlniMRGASS----GLAYMHQICephIVHRDIKSSNILLDGNFKAYV 945
Cdd:cd05606   76 ILDLMNGGDLHYHLSQHgvfseAE-------------MRFYAAevilGLEHMHNRF---IVYRDLKPANILLDEHGHVRI 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  946 ADFGLSRLILPYRTHVTtelVGTLGYIPPEYGQAWVA-TLRGDVYSFGVVMLELLTGKRPMEVFRPKMSREL 1016
Cdd:cd05606  140 SDLGLACDFSKKKPHAS---VGTHGYMAPEVLQKGVAyDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEI 208
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
809-1077 7.28e-09

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 58.88  E-value: 7.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL--------DNGTKLAVKKLTGDYGMME-KEFKAEVEVLSR-AKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd05100   20 LGEGCFGQVVMAEAigidkdkpNKPVTVAVKMLKDDATDKDlSDLVSEMEMMKMiGKHKNIINLLGACTQDGPLYVLVEY 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSL-DYWLHENPEG-----------PAQLDWPKRLNIMRGASSGLAYM-HQICephiVHRDIKSSNILLDGNFKAYV 945
Cdd:cd05100  100 ASKGNLrEYLRARRPPGmdysfdtcklpEEQLTFKDLVSCAYQVARGMEYLaSQKC----IHRDLAARNVLVTEDNVMKI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  946 ADFGLSRLI--LPYRTHVTTELVgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRPKMSRELVAWVHT 1022
Cdd:cd05100  176 ADFGLARDVhnIDYYKKTTNGRL-PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLLKEGHR 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425 1023 MKRDGKPEEVFDTLLREsgneeamlrvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05100  255 MDKPANCTHELYMIMRE----------------CWHAVPSQRPTFKQLVEDLDRV 293
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
801-1076 7.51e-09

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: 58.32  E-value: 7.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKAT-LDNGTKLAVK-----KLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARIL 874
Cdd:cd14094    3 DVYELCEVIGKGPFSVVRRCIhRETGQQFAVKivdvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYwlhenpegpaqldwpkrlNIMRGASSGLA--------YMHQICEP-------HIVHRDIKSSNILL-- 937
Cdd:cd14094   83 VFEFMDGADLCF------------------EIVKRADAGFVyseavashYMRQILEAlrychdnNIIHRDVKPHCVLLas 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  938 -DGNFKAYVADFGLSRLiLPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSREL 1016
Cdd:cd14094  145 kENSAPVKLGGFGVAIQ-LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGI 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425 1017 VAWVHTMKRDGKPEevfdtlLRESGNEEAMlRVLdiacmcvNQNPMKRPNIQQVVD--WLKN 1076
Cdd:cd14094  224 IKGKYKMNPRQWSH------ISESAKDLVR-RML-------MLDPAERITVYEALNhpWIKE 271
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
806-1004 8.60e-09

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: 58.12  E-value: 8.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  806 ANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAK-HENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd14174    7 DELLGEGAYAKVQGCvSLQNGKEYAVKIIEKNAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRGGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAY---VADFGLSRLI------ 954
Cdd:cd14174   87 ILAHIQKR----KHFNEREASRVVRDIASALDFLHT---KGIAHRDLKPENILCESPDKVSpvkICDFDLGSGVklnsac 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  955 LPYRTHVTTELVGTLGYIPPEYGQAWV--ATL---RGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14174  160 TPITTPELTTPCGSAEYMAPEVVEVFTdeATFydkRCDLWSLGVILYIMLSGYPP 214
PHA02988 PHA02988
hypothetical protein; Provisional
817-1074 1.04e-08

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 57.83  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   817 VYKATLDNgTKLAVKKLT---GDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWLHENPE 893
Cdd:PHA02988   36 IYKGIFNN-KEVIIRTFKkfhKGHKVLIDITENEIKNLRRIDSNNILKIYGFIIDIVDDLPRLSLILEYCTRGYLREVLD 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   894 GPAQLDWPKRLNIMRGASSGLAYMHQ-ICEPHivhRDIKSSNILLDGNFKAYVADFGLSRLIL--PYRThvttelVGTLG 970
Cdd:PHA02988  115 KEKDLSFKTKLDMAIDCCKGLYNLYKyTNKPY---KNLTSVSFLVTENYKLKIICHGLEKILSspPFKN------VNFMV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   971 YIPP--------EYgqawvaTLRGDVYSFGVVMLELLTGKRPMEVFRPKmsrelvawvhtmkrdgkpeEVFDTLLRESGN 1042
Cdd:PHA02988  186 YFSYkmlndifsEY------TIKDDIYSLGVVLWEIFTGKIPFENLTTK-------------------EIYDLIINKNNS 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15218425  1043 E----EAMLRVLDIACMCVNQNPMKRPNIQQVVDWL 1074
Cdd:PHA02988  241 LklplDCPLEIKCIVEACTSHDSIKRPNIKEILYNL 276
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
809-1006 1.07e-08

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: 57.39  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVykatldngtKLAVKKLTGD---YGMMEKE--------FKAEVEVLSRAKHENLVALQGYCVHDSARILIYS 877
Cdd:cd14078   11 IGSGGFAKV---------KLATHILTGEkvaIKIMDKKalgddlprVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSL-DYWLHENpegpaQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILP 956
Cdd:cd14078   82 YCPGGELfDYIVAKD-----RLSEDEARVFFRQIVSAVAYVH---SQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  957 YRTHVTTELVGTLGYIPPEY--GQAWVATlRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14078  154 GMDHHLETCCGSPAYAAPELiqGKPYIGS-EADVWSMGVLLYALLCGFLPFD 204
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
801-1004 1.11e-08

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: 57.80  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVykatldngtKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHenlvalqgycVHDSARIL------ 874
Cdd:cd14209    1 DDFDRIKTLGTGSFGRV---------MLVRHKETGNYYAMKILDKQKVVKLKQVEH----------TLNEKRILqainfp 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 -----IYSFMENGSLDYWLHENPEGP--AQLDWPKRLN----IMRGASSGLA--YMHQIcepHIVHRDIKSSNILLDGNF 941
Cdd:cd14209   62 flvklEYSFKDNSNLYMVMEYVPGGEmfSHLRRIGRFSephaRFYAAQIVLAfeYLHSL---DLIYRDLKPENLLIDQQG 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  942 KAYVADFGLSRLIlpyRTHVTTeLVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14209  139 YIKVTDFGFAKRV---KGRTWT-LCGTPEYLAPEiilskgYNKAV------DWWALGVLIYEMAAGYPP 197
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
802-1001 1.14e-08

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 58.89  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   802 NFSQANIIGCGGFGLVYKAT-LDNGTKLAVKKLTGDygmmeKEFK-AEVEVLSRAKHENLVALQGYCVHDSAR-----IL 874
Cdd:PTZ00036   67 SYKLGNIIGNGSFGVVYEAIcIDTSEKVAIKKVLQD-----PQYKnRELLIMKNLNHINIIFLKDYYYTECFKkneknIF 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   875 IYSFME------NGSLDYWLHENPEGPAQLDWPKRLNIMRgassGLAYMHQicePHIVHRDIKSSNILLDGNFKAY-VAD 947
Cdd:PTZ00036  142 LNVVMEfipqtvHKYMKHYARNNHALPLFLVKLYSYQLCR----ALAYIHS---KFICHRDLKPQNLLIDPNTHTLkLCD 214
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425   948 FGLSRLILPYRTHVTteLVGTLGYIPPEYG-QAWVATLRGDVYSFGVVMLELLTG 1001
Cdd:PTZ00036  215 FGSAKNLLAGQRSVS--YICSRFYRAPELMlGATNYTTHIDLWSLGCIIAEMILG 267
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
809-1006 1.17e-08

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: 57.42  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLtgDYGMMEKEFKA----EVEVLSRAKHENLVALqgYCVHDSARILiYSFMENGS 883
Cdd:cd14074   11 LGRGHFAVVKLARhVFTGEKVAVKVI--DKTKLDDVSKAhlfqEVRCMKLVQHPNVVRL--YEVIDTQTKL-YLILELGD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 ----LDYWL-HENpegpaQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFK-AYVADFGLSRLILPY 957
Cdd:cd14074   86 ggdmYDYIMkHEN-----GLNEDLARKYFRQIVSAISYCHKL---HVVHRDLKPENVVFFEKQGlVKLTDFGFSNKFQPG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425  958 RTHVTTelVGTLGYIPPE--YGQAWVATlRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14074  158 EKLETS--CGSLAYSAPEilLGDEYDAP-AVDIWSLGVILYMLVCGQPPFQ 205
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
807-1004 1.22e-08

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: 57.59  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKATLDNGTKLAV------KKLTGDYGMMEKEfkaeVEVLSRAKHENLVALQGYCVHDSARILIYSFME 880
Cdd:cd14169    9 EKLGEGAFSEVVLAQERGSQRLVAlkcipkKALRGKEAMVENE----IAVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHEN---PEGPAQldwpkrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNF---KAYVADFGLSRLi 954
Cdd:cd14169   85 GGELFDRIIERgsyTEKDAS-------QLIGQVLQAVKYLHQL---GIVHRDLKPENLLYATPFedsKIMISDFGLSKI- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  955 lpYRTHVTTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14169  154 --EAQGMLSTACGTPGYVAPElleqkpYGKAV------DVWAIGVISYILLCGYPP 201
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
801-1004 1.31e-08

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: 57.35  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVyKATLD--NGTKLAVK-----KLTGDYGMMEKEfkaeVEVLSRAKHENLVALQGYCVHDSARI 873
Cdd:cd14184    1 EKYKIGKVIGDGNFAVV-KECVErsTGKEFALKiidkaKCCGKEHLIENE----VSILRRVKHPNIIMLIEEMDTPAELY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 LIYSFMENGSLDYWLHENPEGPAQLDWPKRLNImrgaSSGLAYMHQICephIVHRDIKSSNILL----DGNFKAYVADFG 949
Cdd:cd14184   76 LVMELVKGGDLFDAITSSTKYTERDASAMVYNL----ASALKYLHGLC---IVHRDIKPENLLVceypDGTKSLKLGDFG 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  950 LSRLIL-PYRThvtteLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14184  149 LATVVEgPLYT-----VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPP 199
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
809-1068 1.59e-08

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: 56.95  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDN-GTKLAVKKL------TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd14194   13 LGSGQFAVVKKCREKStGLQYAAKFIkkrrtkSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNI-LLDGNF---KAYVADFGLSrlilpY 957
Cdd:cd14194   93 GELFDFLAEK----ESLTEEEATEFLKQILNGVYYLHSL---QIAHFDLKPENImLLDRNVpkpRIKIIDFGLA-----H 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  958 RTHVTTE---LVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPmevFRPKMSRELVAWVHTMKRDGKpEEVFD 1034
Cdd:cd14194  161 KIDFGNEfknIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP---FLGDTKQETLANVSAVNYEFE-DEYFS 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15218425 1035 tllresgNEEAMLRvlDIACMCVNQNPMKRPNIQ 1068
Cdd:cd14194  237 -------NTSALAK--DFIRRLLVKDPKKRMTIQ 261
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
802-1004 1.77e-08

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: 57.72  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEFK---AEVEVLSR-AKHENLVALQgYCVHDSARI-LI 875
Cdd:cd05602    8 DFHFLKVIGKGSFGKVLLARHKSDEKFyAVKVLQKKAILKKKEEKhimSERNVLLKnVKHPFLVGLH-FSFQTTDKLyFV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHENPegpAQLDwPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRL-I 954
Cdd:cd05602   87 LDYINGGELFYHLQRER---CFLE-PRARFYAAEIASALGYLHSL---NIVYRDLKPENILLDSQGHIVLTDFGLCKEnI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  955 LPYRThvTTELVGTLGYIPPE--YGQAWVATLrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05602  160 EPNGT--TSTFCGTPEYLAPEvlHKQPYDRTV--DWWCLGAVLYEMLYGLPP 207
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
836-998 1.77e-08

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 57.06  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  836 DYGMMEKEFKAEVEVLSRAKHENLVALQGYCV---HDSAR-ILIYSFMENGSLDYWLHENPEGPAQLDWPKRLNIMRGAS 911
Cdd:cd14034   49 NFKLQEEKVKAVFDNLIQLEHLNIVKFHKYWAdvkENRARvIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQIL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  912 SGLAYMHQiCEPHIVHRDIKSSNILLDGNfkayvadfGLSRL--ILP--YRTHVTT--ELVGTLGYIPPEYGQAWVATLR 985
Cdd:cd14034  129 SALSYLHS-CDPPIIHGNLTCDTIFIQHN--------GLIKIgsVAPdtINNHVKTcrEEQKNLHFFAPEYGEVANVTTA 199
                        170
                 ....*....|...
gi 15218425  986 GDVYSFGVVMLEL 998
Cdd:cd14034  200 VDIYSFGMCALEM 212
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
801-1004 1.77e-08

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: 57.38  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKA-TLDNGTKLAVK--KLTGDYGMMEKEFK-----AEVEVLSRAKHENLVALQGYCVHDSAR 872
Cdd:cd14041    6 DRYLLLHLLGRGGFSEVYKAfDLTEQRYVAVKihQLNKNWRDEKKENYhkhacREYRIHKELDHPRIVKLYDYFSLDTDS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 I-LIYSFMENGSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQIcEPHIVHRDIKSSNILLD-----GNFKayVA 946
Cdd:cd14041   86 FcTVLEYCEGNDLDFYLKQH----KLMSEKEARSIIMQIVNALKYLNEI-KPPIIHYDLKPGNILLVngtacGEIK--IT 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  947 DFGLSRLIL--PYRT----HVTTELVGTLGYIPPEY----GQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14041  159 DFGLSKIMDddSYNSvdgmELTSQGAGTYWYLPPECfvvgKEPPKISNKVDVWSVGVIFYQCLYGRKP 226
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
809-1004 1.81e-08

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: 56.73  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVK-----KLTGD-YGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd14105   13 LGSGQFAVVKKCrEKSTGLEYAAKfikkrRSKASrRGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVLILELVAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNI-LLDGNF---KAYVADFGLSRLILPy 957
Cdd:cd14105   93 GELFDFLAEK----ESLSEEEATEFLKQILDGVNYLHTK---NIAHFDLKPENImLLDKNVpipRIKLIDFGLAHKIED- 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15218425  958 rTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14105  165 -GNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP 210
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
808-1004 2.03e-08

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: 57.04  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKA-TLDNGTKLAVKkltgdygMMEKE--------FKaEVEVLSRAK-HENLVALQGYCVHDSARILIYS 877
Cdd:cd14090    9 LLGEGAYASVQTCiNLYTGKEYAVK-------IIEKHpghsrsrvFR-EVETLHQCQgHPNILQLIEYFEDDERFYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLdywLHeNPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAY---VADFGLS--- 951
Cdd:cd14090   81 KMRGGPL---LS-HIEKRVHFTEQEASLVVRDIASALDFLH---DKGIAHRDLKPENILCESMDKVSpvkICDFDLGsgi 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  952 RLILPYRTHVTT-EL---VGTLGYIPPEYGQAWV--ATL---RGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14090  154 KLSSTSMTPVTTpELltpVGSAEYMAPEVVDAFVgeALSydkRCDLWSLGVILYIMLCGYPP 215
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
808-1040 2.18e-08

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: 56.52  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAT-LDNGTKLAVKKLTGD----YGMMEKEFKAEVEVLSRAKhenlvALQGYcvhdSARILIYSFMENG 882
Cdd:cd14100    7 LLGSGGFGSVYSGIrVADGAPVAIKHVEKDrvseWGELPNGTRVPMEIVLLKK-----VGSGF----RGVIRLLDWFERP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENPEgPAQ--LDW-------PKRL--NIMRGASSGLAYMHQIcepHIVHRDIKSSNILLD---GNFKayVADF 948
Cdd:cd14100   78 DSFVLVLERPE-PVQdlFDFitergalPEELarSFFRQVLEAVRHCHNC---GVLHRDIKDENILIDlntGELK--LIDF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  949 GLSRLIlpyRTHVTTELVGTLGYIPPEygqaWVATLR-----GDVYSFGVVMLELLTGKRPME----------VFRPKMS 1013
Cdd:cd14100  152 GSGALL---KDTVYTDFDGTRVYSPPE----WIRFHRyhgrsAAVWSLGILLYDMVCGDIPFEhdeeiirgqvFFRQRVS 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 15218425 1014 RE---LVAWVHTMKRDGKPEevFDTLLRES 1040
Cdd:cd14100  225 SEcqhLIKWCLALRPSDRPS--FEDIQNHP 252
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
808-1025 2.34e-08

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 56.88  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   808 IIGCGGFGLVYK---ATLDNGTKLAVKKLTGdygMMEKEFKAEVEVLSRAKHENLVALQGYcVHDSARILIYSFMENGSL 884
Cdd:PHA02882   19 LIGCGGFGCVYEtqcASDHCINNQAVAKIEN---LENETIVMETLVYNNIYDIDKIALWKN-IHNIDHLGIPKYYGCGSF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   885 DY-------------WLHENPEGPAQLDWPKRL--NIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:PHA02882   95 KRcrmyyrfilleklVENTKEIFKRIKCKNKKLikNIMKDMLTTLEYIH---EHGISHGDIKPENIMVDGNNRGYIIDYG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   950 LSRLILPYRTHVTTEL------VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAWVHTM 1023
Cdd:PHA02882  172 IASHFIIHGKHIEYSKeqkdlhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHNGNLIHAAKCDFI 251

                  ..
gi 15218425  1024 KR 1025
Cdd:PHA02882  252 KR 253
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
917-1004 2.40e-08

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: 56.61  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  917 MHQICEPH-IVHRDIKSSNILLD--GNFKayVADFGLSRLILPYRTHvtTELVGTLGYIPPE---------YgqawvaTL 984
Cdd:cd06618  127 LHYLKEKHgVIHRDVKPSNILLDesGNVK--LCDFGISGRLVDSKAK--TRSAGCAAYMAPEridppdnpkY------DI 196
                         90       100
                 ....*....|....*....|
gi 15218425  985 RGDVYSFGVVMLELLTGKRP 1004
Cdd:cd06618  197 RADVWSLGISLVELATGQFP 216
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
801-1001 2.75e-08

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: 56.62  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLD-NGTKLAVKKLTgdygMMEKE---FKA--EVEVLSRAKHENLVALQGYCVHDSARIL 874
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKvNGKLVALKVIR----LQEEEgtpFTAirEASLLKGLKHANIVLLHDIIHTKETLTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 IYSFMENGSLDYwLHENPEGPAqldwPKRLNI-MRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd07869   81 VFEYVHTDLCQY-MDKHPGGLH----PENVKLfLFQLLRGLSYIHQ---RYILHRDLKPQNLLISDTGELKLADFGLARA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15218425  954 -ILPyrTHVTTELVGTLGYIPPE--YGQAWVATLRgDVYSFGVVMLELLTG 1001
Cdd:cd07869  153 kSVP--SHTYSNEVVTLWYRPPDvlLGSTEYSTCL-DMWGVGCIFVEMIQG 200
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
847-1006 2.98e-08

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: 56.21  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  847 EVEVLSRAKHENLVALQgYCVHDSAR---ILIYSFMENGSLdywLHENPEGPAQLDWPKRlnIMRGASSGLAYMHQiceP 923
Cdd:cd14118   64 EIAILKKLDHPNVVKLV-EVLDDPNEdnlYMVFELVDKGAV---MEVPTDNPLSEETARS--YFRDIVLGIEYLHY---Q 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  924 HIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTElVGTLGYIPPEYGQAWVATLRG---DVYSFGVVMLELLT 1000
Cdd:cd14118  135 KIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSST-AGTPAFMAPEALSESRKKFSGkalDIWAMGVTLYCFVF 213

                 ....*.
gi 15218425 1001 GKRPME 1006
Cdd:cd14118  214 GRCPFE 219
PLN03150 PLN03150
hypothetical protein; Provisional
255-339 3.21e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 57.90  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   255 GFNN--LSGEIPKEIYNLPELEQLFLPVNRLSGKIDNGITRLTKLTLLELYSNHIEGEIPKDIGKLSKLSSLQLHVNNLM 332
Cdd:PLN03150  424 GLDNqgLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLS 503

                  ....*..
gi 15218425   333 GSIPVSL 339
Cdd:PLN03150  504 GRVPAAL 510
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
912-1004 3.45e-08

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: 56.60  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  912 SGLAYMHqicEPHIVHRDIKSSNILLD--GNFKayVADFGLSRLILPYrTHVTTELVGTLGYIPPE------YGQAWvat 983
Cdd:cd05571  106 LALGYLH---SQGIVYRDLKLENLLLDkdGHIK--ITDFGLCKEEISY-GATTKTFCGTPEYLAPEvledndYGRAV--- 176
                         90       100
                 ....*....|....*....|.
gi 15218425  984 lrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05571  177 ---DWWGLGVVMYEMMCGRLP 194
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
905-1075 3.59e-08

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: 56.54  E-value: 3.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  905 NIMRGASSGLAYMHQIcepHIVHRDIKSSNILL---DGNFKAYVADFGLSRLiLPYRTHVTTElVGTLGYIPPE------ 975
Cdd:cd14092  103 RIMRQLVSAVSFMHSK---GVVHRDLKPENLLFtdeDDDAEIKIVDFGFARL-KPENQPLKTP-CFTLPYAAPEvlkqal 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  976 ----YGQAWvatlrgDVYSFGVVMLELLTGKRPmevFRPKMSRELVAwvHTMKRDGKPEEVFDTLLRESGNEEA------ 1045
Cdd:cd14092  178 stqgYDESC------DLWSLGVILYTMLSGQVP---FQSPSRNESAA--EIMKRIKSGDFSFDGEEWKNVSSEAksliqg 246
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15218425 1046 MLRVldiacmcvnqNPMKRPNIQQVV--DWLK 1075
Cdd:cd14092  247 LLTV----------DPSKRLTMSELRnhPWLQ 268
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
809-1002 3.91e-08

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: 56.71  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAtLDN--GTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVAL------QGYCVHDSARIL-----I 875
Cdd:cd07854   13 LGCGSNGLVFSA-VDSdcDKRVAVKKIVLTDPQSVKHALREIKIIRRLDHDNIVKVyevlgpSGSDLTEDVGSLtelnsV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFME--NGSLDYWLHENP--EGPAQLdwpkrlnIMRGASSGLAYMHQicePHIVHRDIKSSNILLDG-NFKAYVADFGL 950
Cdd:cd07854   92 YIVQEymETDLANVLEQGPlsEEHARL-------FMYQLLRGLKYIHS---ANVLHRDLKPANVFINTeDLVLKIGDFGL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  951 SRLILPYRTH--VTTELVGTLGYIPPE-------YGQAwvatlrGDVYSFGVVMLELLTGK 1002
Cdd:cd07854  162 ARIVDPHYSHkgYLSEGLVTKWYRSPRlllspnnYTKA------IDMWAAGCIFAEMLTGK 216
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
808-1006 4.67e-08

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: 56.35  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLdNGTK--LAVKKLTGDY---------GMMEKEfkaeVEVLSrAKHENLVALQGyCVHDSARIL-I 875
Cdd:cd05591    2 VLGKGSFGKVMLAER-KGTDevYAIKVLKKDVilqdddvdcTMTEKR----ILALA-AKHPFLTALHS-CFQTKDRLFfV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQicepH-IVHRDIKSSNILLDGNFKAYVADFGLSRL- 953
Cdd:cd05591   75 MEYVNGGDLMFQIQRA----RKFDEPRARFYAAEVTLALMFLHR----HgVIYRDLKLDNILLDAEGHCKLADFGMCKEg 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  954 ILPYRThvTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd05591  147 ILNGKT--TTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFE 197
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
809-1072 4.73e-08

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: 55.76  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVAL-QGYCVHDSARILIySFMENGSLDY 886
Cdd:cd06659   29 IGEGSTGVVCIArEKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMyKSYLVGEELWVLM-EYLQGGALTD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENPEGPAQLDwpkrlNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLI---LPYRthvtT 963
Cdd:cd06659  108 IVSQTRLNEEQIA-----TVCEAVLQALAYLHS---QGVIHRDIKSDSILLTLDGRVKLSDFGFCAQIskdVPKR----K 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  964 ELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPMEVFRPkmsrelvawVHTMK--RDGKPEEvfdtlLRESG 1041
Cdd:cd06659  176 SLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSP---------VQAMKrlRDSPPPK-----LKNSH 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 15218425 1042 NEEAMLRvlDIACMCVNQNPMKRPNIQQVVD 1072
Cdd:cd06659  242 KASPVLR--DFLERMLVRDPQERATAQELLD 270
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
809-1020 6.53e-08

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 55.34  E-value: 6.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATL---DNGTKLAVKKLTGDYGMME-KEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd14206    5 IGNGWFGKVILGEIfsdYTPAQVVVKELRVSAGPLEqRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLGDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWL--HENPEGPAQlDWPKR--LNIMRGA---SSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLS------ 951
Cdd:cd14206   85 KRYLraQRKADGMTP-DLPTRdlRTLQRMAyeiTLGLLHLH---KNNYIHSDLALRNCLLTSDLTVRIGDYGLShnnyke 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  952 -------RLILPYRtHVTTELVGTLgyippeYGQAWVA--TLRGDVYSFGVVMLELLT-GKRPmevFRPKMSRELVAWV 1020
Cdd:cd14206  161 dyyltpdRLWIPLR-WVAPELLDEL------HGNLIVVdqSKESNVWSLGVTIWELFEfGAQP---YRHLSDEEVLTFV 229
pknD PRK13184
serine/threonine-protein kinase PknD;
808-1017 6.77e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 57.09  E-value: 6.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   808 IIGCGGFGLVYKAtLDN--GTKLAVKKLTGD---YGMMEKEFKAEVEVLSRAKHENLVALqgYCVHDSARILIYS--FME 880
Cdd:PRK13184    9 LIGKGGMGEVYLA-YDPvcSRRVALKKIREDlseNPLLKKRFLREAKIAADLIHPGIVPV--YSICSDGDPVYYTmpYIE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   881 NGSLDYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHQICEP----H---IVHRDIKSSNILLdGNF-KAYVADFGLS- 951
Cdd:PRK13184   86 GYTLKSLLKSVWQ---KESLSKELAEKTSVGAFLSIFHKICATieyvHskgVLHRDLKPDNILL-GLFgEVVILDWGAAi 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   952 ----------------RLILPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPmevFRPKMSRE 1015
Cdd:PRK13184  162 fkkleeedlldidvdeRNICYSSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFP---YRRKKGRK 238

                  ..
gi 15218425  1016 LV 1017
Cdd:PRK13184  239 IS 240
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
801-1002 6.88e-08

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: 55.39  E-value: 6.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMME-KEFK-AEVEVLSRAKHENLVALQGYCVHDSARILIYS 877
Cdd:cd07848    1 NKFEVLGVVGEGAYGVVLKCRHKETKEIvAIKKFKDSEENEEvKETTlRELKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYwLHENPEGPAqldwPKRLNimrgassglAYMHQICEP-------HIVHRDIKSSNILLDGNFKAYVADFGL 950
Cdd:cd07848   81 YVEKNMLEL-LEEMPNGVP----PEKVR---------SYIYQLIKAihwchknDIVHRDIKPENLLISHNDVLKLCDFGF 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  951 SRLILPYRTHVTTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGK 1002
Cdd:cd07848  147 ARNLSEGSNANYTEYVATRWYRSPElllgapYGKAV------DMWSVGCILGELSDGQ 198
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
807-1004 6.91e-08

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: 55.45  E-value: 6.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVYKA-TLDNGTKLAVK--KLTGDYGMMEKEFK-----AEVEVLSRAKHENLVALQGYCVHDSARI-LIYS 877
Cdd:cd14040   12 HLLGRGGFSEVYKAfDLYEQRYAAVKihQLNKSWRDEKKENYhkhacREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQIcEPHIVHRDIKSSNILL-DGNF--KAYVADFGLSRLI 954
Cdd:cd14040   92 YCEGNDLDFYLKQH----KLMSEKEARSIVMQIVNALRYLNEI-KPPIIHYDLKPGNILLvDGTAcgEIKITDFGLSKIM 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  955 LPYRTHV-----TTELVGTLGYIPPEY----GQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14040  167 DDDSYGVdgmdlTSQGAGTYWYLPPECfvvgKEPPKISNKVDVWSVGVIFFQCLYGRKP 225
PLN03150 PLN03150
hypothetical protein; Provisional
462-539 6.94e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 56.75  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   462 KDFLRSD--GFPSLQIFGIGACRLTGEIPAWLIKLQRVEVMDLSMNRFVGTIPGWLGTLPDLFYLDLSDNFLTGELPKEL 539
Cdd:PLN03150  431 RGFIPNDisKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAAL 510
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
801-1010 7.03e-08

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 55.76  E-value: 7.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   801 DNFSQANIIGCGGFGLVYKATLDNGT--KLAVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLVALQGYCVHDSARILI 875
Cdd:PTZ00426   30 EDFNFIRTLGTGSFGRVILATYKNEDfpPVAIKRFEKSKIIKQKQVDhvfSERKILNYINHPFCVNLYGSFKDESYLYLV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   876 YSFMENGSLDYWLHENPEgpaqldWPKRLNIMRGASSGLAYMHqICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRlIL 955
Cdd:PTZ00426  110 LEFVIGGEFFTFLRRNKR------FPNDVGCFYAAQIVLIFEY-LQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAK-VV 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425   956 PYRTHVtteLVGTLGYIPPE------YGQAwvatlrGDVYSFGVVMLELLTGKRPMEVFRP 1010
Cdd:PTZ00426  182 DTRTYT---LCGTPEYIAPEillnvgHGKA------ADWWTLGIFIYEILVGCPPFYANEP 233
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
808-1004 7.45e-08

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: 55.40  E-value: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVY----KATldnGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLVALQgYCVHDSARILIYSFME 880
Cdd:cd05595    2 LLGKGTFGKVIlvreKAT---GRYYAMKILRKEVIIAKDEVAhtvTESRVLQNTRHPFLTALK-YAFQTHDRLCFVMEYA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSlDYWLHENPEGPAQLDWPKrlniMRGAS--SGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYR 958
Cdd:cd05595   78 NGG-ELFFHLSRERVFTEDRAR----FYGAEivSALEYLHS---RDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  959 THVTTeLVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05595  150 ATMKT-FCGTPEYLAPEvledndYGRAV------DWWGLGVVMYEMMCGRLP 194
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
925-1034 7.74e-08

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: 54.58  E-value: 7.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  925 IVHRDIKSSNILLD---GNFKayVADFGLSRLIlpyRTHVTTELVGTLGYIPPEygqaWVATLR-----GDVYSFGVVML 996
Cdd:cd14102  126 VVHRDIKDENLLVDlrtGELK--LIDFGSGALL---KDTVYTDFDGTRVYSPPE----WIRYHRyhgrsATVWSLGVLLY 196
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  997 ELLTGKRPME----------VFRPKMSRE---LVAWVHTMKRDGKP--EEVFD 1034
Cdd:cd14102  197 DMVCGDIPFEqdeeilrgrlYFRRRVSPEcqqLIKWCLSLRPSDRPtlEQIFD 249
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
847-1004 8.45e-08

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: 54.93  E-value: 8.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  847 EVEVLSRAKHE-NLVALQGYCVHDSARILIYSFMENGSLdyWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHI 925
Cdd:cd14198   57 EIAVLELAKSNpRVVNLHEVYETTSEIILILEYAAGGEI--FNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQ---NNI 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  926 VHRDIKSSNILLD-----GNFKayVADFGLSRLIlpyrTHVTT--ELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLEL 998
Cdd:cd14198  132 VHLDLKPQNILLSsiyplGDIK--IVDFGMSRKI----GHACElrEIMGTPEYLAPEILNYDPITTATDMWNIGVIAYML 205

                 ....*.
gi 15218425  999 LTGKRP 1004
Cdd:cd14198  206 LTHESP 211
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
796-1010 1.04e-07

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 54.58  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  796 LLKATDnFSQANIIGCGGFGLVYKAT-LDNGTKL----AVKKLTGDYGmmEKEFKAEVE---VLSRAKHENLVALQGYCV 867
Cdd:cd05111    3 IFKETE-LRKLKVLGSGVFGTVHKGIwIPEGDSIkipvAIKVIQDRSG--RQSFQAVTDhmlAIGSLDHAYIVRLLGICP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  868 HDSARiLIYSFMENGSLDYWL--HENPEGPAQLdwpkrLNIMRGASSGLAYMHQICephIVHRDIKSSNILLDGNFKAYV 945
Cdd:cd05111   80 GASLQ-LVTQLLPLGSLLDHVrqHRGSLGPQLL-----LNWCVQIAKGMYYLEEHR---MVHRNLAARNVLLKSPSQVQV 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  946 ADFGLSRLILP-YRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMEVFRP 1010
Cdd:cd05111  151 ADFGVADLLYPdDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfGAEPYAGMRL 217
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
809-1006 1.07e-07

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: 55.05  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGdygMMEKEFKAEVEVLSRAK-HENLVALQGyCVHDSAR-ILIYSFMENGSLd 885
Cdd:cd14179   15 LGEGSFSICRKCLhKKTNQEYAVKIVSK---RMEANTQREIAALKLCEgHPNIVKLHE-VYHDQLHtFLVMELLKGGEL- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 ywlHENPEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL---DGNFKAYVADFGLSRLILPYRTHVT 962
Cdd:cd14179   90 ---LERIKKKQHFSETEASHIMRKLVSAVSHMHDV---GVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQPLK 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15218425  963 TELVgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14179  164 TPCF-TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQ 206
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
784-1004 1.09e-07

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: 55.08  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  784 SRYEVKDLTIFELLKATDNFSQANIIGCGGFGLV----YKATldngTKLAVKKLTGDYGMMEKE----FKAEVEVLSRAK 855
Cdd:cd05596    9 NRYEKPVNEITKLRMNAEDFDVIKVIGRGAFGEVqlvrHKST----KKVYAMKLLSKFEMIKRSdsafFWEERDIMAHAN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  856 HENLVALQgYCVHDSARI-LIYSFMENGSLdYWLHENpegpaqLDWPKRLNIMRGASSGLAyMHQICEPHIVHRDIKSSN 934
Cdd:cd05596   85 SEWIVQLH-YAFQDDKYLyMVMDYMPGGDL-VNLMSN------YDVPEKWARFYTAEVVLA-LDAIHSMGFVHRDVKPDN 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  935 ILLDGNFKAYVADFGLS-RLILPYRTHVTTElVGTLGYIPPEY----GQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05596  156 MLLDASGHLKLADFGTCmKMDKDGLVRSDTA-VGTPDYISPEVlksqGGDGVYGRECDWWSVGVFLYEMLVGDTP 229
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
802-1051 1.18e-07

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: 55.01  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLVALQGYCVHDSARI-LIY 876
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELyAVKILKKDVVIQDDDVEctmVEKRVLALSGKPPFLTQLHSCFQTMDRLyFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHEnpegPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILp 956
Cdd:cd05616   81 EYVNGGDLMYHIQQ----VGRFKEPHAVFYAAEIAIGLFFLQS---KGIIYRDLKLDNVMLDSEGHIKIADFGMCKENI- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  957 YRTHVTTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRPME---------------VFRPK-MSR 1014
Cdd:cd05616  153 WDGVTTKTFCGTPDYIAPEiiayqpYGKSV------DWWAFGVLLYEMLAGQAPFEgededelfqsimehnVAYPKsMSK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15218425 1015 ELVAWV------HTMKRDG-KPEEVFDTllresgNEEAMLRVLD 1051
Cdd:cd05616  227 EAVAICkglmtkHPGKRLGcGPEGERDI------KEHAFFRYID 264
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
104-311 1.28e-07

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  104 LSGN----LPSSVLDLQRLSRLDLSHNRLSgPLPPGfLSALDQLLVLDLSYNSFKgELPlqQSFGNGSNgifpIQTVDLS 179
Cdd:COG4886  166 LSNNqltdLPEELGNLTNLKELDLSNNQIT-DLPEP-LGNLTNLEELDLSGNQLT-DLP--EPLANLTN----LETLDLS 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  180 SNLLegeilSSSVFLQGAFNLTSFNVSNNSFTgSIPSfmCTASPQLTKLDFSYNDFSGDLSQELSRCSRLSVLRAGFNNL 259
Cdd:COG4886  237 NNQL-----TDLPELGNLTNLEELDLSNNQLT-DLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425  260 SGEIPKEIYNLPELEQLFLPVNRLSGKIDNGITRLTKLTLLELYSNHIEGEI 311
Cdd:COG4886  309 NLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLS 360
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
116-383 1.28e-07

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 55.57  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  116 QRLSRLDLSHNRLSGPLPP-----GFLSALDQLLVLDLSYNSFKGEL------PLQQSFGNGSNGIFPIQTVDLSSNLL- 183
Cdd:COG5238  114 TPPPDLRRIMAKTLEDSLIlylalPRRINLIQVLKDPLGGNAVHLLGlaarlgLLAAISMAKALQNNSVETVYLGCNQIg 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  184 -EGEILSSSVFLQGAfNLTSFNVSNNSFTGS-IPSF--MCTASPQLTKLDFSYNDFSGD----LSQELSRCSRLSVLRAG 255
Cdd:COG5238  194 dEGIEELAEALTQNT-TVTTLWLKRNPIGDEgAEILaeALKGNKSLTTLDLSNNQIGDEgviaLAEALKNNTTVETLYLS 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  256 FNNLSGE----IPKEIYNLPELEQLFLPVNRLSGK----IDNGITRLTKLTLLELYSNHIEGE----IPKDIGKLSKLSS 323
Cdd:COG5238  273 GNQIGAEgaiaLAKALQGNTTLTSLDLSVNRIGDEgaiaLAEGLQGNKTLHTLNLAYNGIGAQgaiaLAKALQENTTLHS 352
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  324 LQLHVNNL----MGSIPVSLANCTKLVKLNLRVNQLG--GTLSAIDFSRFQSLSILDLGNNSFTGE 383
Cdd:COG5238  353 LDLSDNQIgdegAIALAKYLEGNTTLRELNLGKNNIGkqGAEALIDALQTNRLHTLILDGNLIGAE 418
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
809-1002 1.31e-07

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


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 55.06  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAtLDNGT--KLAVKKLTGDYGMM--EKEFKAEVEVLSRAKHENLVALQGYCVHDSArilIYSFMEngsl 884
Cdd:cd07878   23 VGSGAYGSVCSA-YDTRLrqKVAVKKLSRPFQSLihARRTYRELRLLKHMKHENVIGLLDVFTPATS---IENFNE---- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 dYWLHENPEGpAQLDwpkrlNIMRGAS--------------SGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGL 950
Cdd:cd07878   95 -VYLVTNLMG-ADLN-----NIVKCQKlsdehvqfliyqllRGLKYIHS---AGIIHRDLKPSNVAVNEDCELRILDFGL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15218425  951 SRlilpYRTHVTTELVGTLGYIPPEYGQAWVATLRG-DVYSFGVVMLELLTGK 1002
Cdd:cd07878  165 AR----QADDEMTGYVATRWYRAPEIMLNWMHYNQTvDIWSVGCIMAELLKGK 213
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
809-1005 1.35e-07

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: 54.31  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTgdygmMEKE----FKA--EVEVLSRAKHENLVALQGyCVH-DSARILIYSFME 880
Cdd:cd07844    8 LGEGSYATVYKGrSKLTGQLVALKEIR-----LEHEegapFTAirEASLLKDLKHANIVTLHD-IIHtKKTLTLVFEYLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NgSLDYWLHENPEG--PAQLdwpkRL---NIMRGassgLAYMHQicePHIVHRDIKSSNILLD--GNFKayVADFGLSRL 953
Cdd:cd07844   82 T-DLKQYMDDCGGGlsMHNV----RLflfQLLRG----LAYCHQ---RRVLHRDLKPQNLLISerGELK--LADFGLARA 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  954 -ILPYRTHvTTELVgTLGYIPP-------EYgqawvaTLRGDVYSFGVVMLELLTGkRPM 1005
Cdd:cd07844  148 kSVPSKTY-SNEVV-TLWYRPPdvllgstEY------STSLDMWGVGCIFYEMATG-RPL 198
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
809-1028 1.44e-07

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: 54.49  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTGdygMMEKEFKAEVEVLSRAK-HENLVALQGyCVHDSARI-LIYSFMENGSLd 885
Cdd:cd14180   14 LGEGSFSVCRKCRhRQSGQEYAVKIISR---RMEANTQREVAALRLCQsHPNIVALHE-VLHDQYHTyLVMELLRGGEL- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 ywlHENPEGPAQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDG---NFKAYVADFGLSRLILPYRTHVT 962
Cdd:cd14180   89 ---LDRIKKKARFSESEASQLMRSLVSAVSFMH---EAGVVHRDLKPENILYADesdGAVLKVIDFGFARLRPQGSRPLQ 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  963 TELVgTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRPMEVFRPKMSRELVAWVHTMKRDGK 1028
Cdd:cd14180  163 TPCF-TLQYAAPElfsnqgYDESC------DLWSLGVILYTMLSGQVPFQSKRGKMFHNHAADIMHKIKEGD 227
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
801-1070 1.53e-07

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, 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 CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 54.85  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATL------DNGTKLAVKKLTGDYGMMEKE-FKAEVEVLSR-AKHENLVALQGYCVHDSAR 872
Cdd:cd05106   38 DNLQFGKTLGAGAFGKVVEATAfglgkeDNVLRVAVKMLKASAHTDEREaLMSELKILSHlGQHKNIVNLLGACTHGGPV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 ILIYSFMENGSLDYWLHENPEG--------PAQLDWP---KRLNI---------------------MRGASSG------- 913
Cdd:cd05106  118 LVITEYCCYGDLLNFLRKKAETflnfvmalPEISETSsdyKNITLekkyirsdsgfssqgsdtyveMRPVSSSssqssds 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  914 -----------------LAYMHQICE-------PHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTelvGT- 968
Cdd:cd05106  198 kdeedtedswpldlddlLRFSSQVAQgmdflasKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYVVK---GNa 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  969 ---LGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMsreLV-AWVHTMKRDGkpeevfdtlLRESGNE 1043
Cdd:cd05106  275 rlpVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSlGKSPY----PGI---LVnSKFYKMVKRG---------YQMSRPD 338
                        330       340
                 ....*....|....*....|....*..
gi 15218425 1044 EAMLRVLDIACMCVNQNPMKRPNIQQV 1070
Cdd:cd05106  339 FAPPEIYSIMKMCWNLEPTERPTFSQI 365
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
800-1004 1.53e-07

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: 54.23  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  800 TDNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE--FKAEVEVLSRAKHENLVALQGYCVHDSARILIYS 877
Cdd:cd14183    5 SERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhmIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSL-------DYWLHENPEGpaqldwpkrlnIMRGASSGLAYMHQIcepHIVHRDIKSSNILL----DGNFKAYVA 946
Cdd:cd14183   85 LVKGGDLfdaitstNKYTERDASG-----------MLYNLASAIKYLHSL---NIVHRDIKPENLLVyehqDGSKSLKLG 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  947 DFGLSRLI-LPYRThvtteLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14183  151 DFGLATVVdGPLYT-----VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPP 204
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
500-667 1.57e-07

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.94  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  500 MDLSMNRFVGTIPGWLGTLPDLFYLDLSDNFLTGELPKELFQLRALMSQKAYDATERNYLELPVFVNPNNVTTNQQYNQL 579
Cdd:COG4886   13 LLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  580 SSLPPtiyIKRNNLTGTIpvEVGQLKVLHILELLGNNFSgSIPDELSNLTNLERLDLSNNNLSgRIPWSLTGLHFLSYFN 659
Cdd:COG4886   93 GDLTN---LTELDLSGNE--ELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DLPEPLGNLTNLKSLD 165

                 ....*...
gi 15218425  660 VANNTLSG 667
Cdd:COG4886  166 LSNNQLTD 173
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
850-1006 1.64e-07

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: 53.79  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  850 VLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWLHENPEgpaQLDWPKRLNIMRGASSGLAYMHqicEPHIVHRD 929
Cdd:cd05077   61 MMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKSD---VLTTPWKFKVAKQLASALSYLE---DKDLVHGN 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  930 IKSSNILL-----DGNFKAYVAdfgLSRLILPYRTHVTTELVGTLGYIPPE-YGQAWVATLRGDVYSFGVVMLEL-LTGK 1002
Cdd:cd05077  135 VCTKNILLaregiDGECGPFIK---LSDPGIPITVLSRQECVERIPWIAPEcVEDSKNLSIAADKWSFGTTLWEIcYNGE 211

                 ....
gi 15218425 1003 RPME 1006
Cdd:cd05077  212 IPLK 215
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
809-1005 1.88e-07

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: 54.24  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT---LDNGTKLAVKKLTGDYGMMEKEFKaEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLD 885
Cdd:cd07873   10 LGEGTYATVYKGRsklTDNLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 YwlhenpegpaqLDWPKRLNIMRGAS-------SGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRL-ILPY 957
Cdd:cd07873   89 Y-----------LDDCGNSINMHNVKlflfqllRGLAYCHR---RKVLHRDLKPQNLLINERGELKLADFGLARAkSIPT 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  958 RTHvTTELVgTLGYIPPE--YGQAWVATlRGDVYSFGVVMLELLTGkRPM 1005
Cdd:cd07873  155 KTY-SNEVV-TLWYRPPDilLGSTDYST-QIDMWGVGCIFYEMSTG-RPL 200
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
801-1004 2.14e-07

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: 53.44  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNF----SQANIIGCGGFGLVYKATlDNGTKLAVK-KLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILI 875
Cdd:cd14113    3 DNFdsfySEVAELGRGRFSVVKKCD-QRGTKRAVAtKFVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSL-DY---WlhenpegpAQLDWPKRLNIMRGASSGLAYMHQiCEphIVHRDIKSSNILLDGNFKA---YVADF 948
Cdd:cd14113   82 LEMADQGRLlDYvvrW--------GNLTEEKIRFYLREILEALQYLHN-CR--IAHLDLKPENILVDQSLSKptiKLADF 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  949 GLS-RLILPYRTHvttELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14113  151 GDAvQLNTTYYIH---QLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSP 204
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
809-1004 2.15e-07

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: 53.55  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVyKATLDNGT--KLAVKKL--------TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSF 878
Cdd:cd14084   14 LGSGACGEV-KLAYDKSTckKVAIKIInkrkftigSRREINKPRNIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLEL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGSLDYWLHEN---PEGPAQLdwpkrlnIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGN-----FKayVADFGL 950
Cdd:cd14084   93 MEGGELFDRVVSNkrlKEAICKL-------YFYQMLLAVKYLH---SNGIIHRDLKPENVLLSSQeeeclIK--ITDFGL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  951 SRlILPYRTHVTTeLVGTLGYIPPE----YGQAwVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14084  161 SK-ILGETSLMKT-LCGTPTYLAPEvlrsFGTE-GYTRAVDCWSLGVILFICLSGYPP 215
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
809-1078 2.26e-07

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: 53.97  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVK-----KLTG-DYGMMEKEfkaeVEVLSRAKHENLVALQGYCVHDSARILIYSFMEN 881
Cdd:cd14086    9 LGKGAFSVVRRCVqKSTGQEFAAKiintkKLSArDHQKLERE----ARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSL--DYWLHEN-PEGPAQldwpkrlNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFK-AYV--ADFGLSrLIL 955
Cdd:cd14086   85 GELfeDIVAREFySEADAS-------HCIQQILESVNHCHQ---NGIVHRDLKPENLLLASKSKgAAVklADFGLA-IEV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  956 PYRTHVTTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRPmevFRPKMSRELVAWVHTMKRDGKP 1029
Cdd:cd14086  154 QGDQQAWFGFAGTPGYLSPEvlrkdpYGKPV------DIWACGVILYILLVGYPP---FWDEDQHRLYAQIKAGAYDYPS 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15218425 1030 EEvFDTLLRESGNE-EAMLRVldiacmcvnqNPMKRPNIQQVVD--WLKNIE 1078
Cdd:cd14086  225 PE-WDTVTPEAKDLiNQMLTV----------NPAKRITAAEALKhpWICQRD 265
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
913-1004 2.29e-07

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: 53.45  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  913 GLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLI-----LPYRTHVTTE----------LVGTLGYIPPEYG 977
Cdd:cd14010  106 GLHYIH---SKGIIYCDLKPSNILLDGNGTLKLSDFGLARREgeilkELFGQFSDEGnvnkvskkqaKRGTPYYMAPELF 182
                         90       100
                 ....*....|....*....|....*..
gi 15218425  978 QAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14010  183 QGGVHSFASDLWALGCVLYEMFTGKPP 209
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
809-1077 2.39e-07

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 53.65  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT------LDNGTKLAVKKLTgdYGMMEKEFKA---EVEVLSR-AKHENLVALQGYCVHDSARIL-IYS 877
Cdd:cd05054   15 LGRGAFGKVIQASafgidkSATCRTVAVKMLK--EGATASEHKAlmtELKILIHiGHHLNVVNLLGACTKPGGPLMvIVE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYWL-----------------HENPEGPAQL-DWPKRLNIMRGASSGLAY-MHQICEPHIVHRDIKSSNILLD 938
Cdd:cd05054   93 FCKFGNLSNYLrskreefvpyrdkgardVEEEEDDDELyKEPLTLEDLICYSFQVARgMEFLASRKCIHRDLAARNILLS 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  939 GNFKAYVADFGLSRLILP---YRTHVTTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrP--KM 1012
Cdd:cd05054  173 ENNVVKICDFGLARDIYKdpdYVRKGDARL--PLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPY----PgvQM 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425 1013 SRELVAWVHTMKRDGKPEEVFDTLLResgneeamlrvldIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05054  247 DEEFCRRLKEGTRMRAPEYTTPEIYQ-------------IMLDCWHGEPKERPTFSELVEKLGDL 298
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
807-1004 2.61e-07

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: 53.26  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  807 NIIGCGGFGLVY------KATLDNGTKLAVKK-LTGDYGMMEKEFKA--EVEVLSRAKHENLVALQGYCVHDSARILIYS 877
Cdd:cd14076    7 RTLGEGEFGKVKlgwplpKANHRSGVQVAIKLiRRDTQQENCQTSKImrEINILKGLTHPNIVRLLDVLKTKKYIGIVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSL-DYWLH----ENPEGP---AQLdwpkrlnimrgaSSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFG 949
Cdd:cd14076   87 FVSGGELfDYILArrrlKDSVACrlfAQL------------ISGVAYLHK---KGVVHRDLKLENLLLDKNRNLVITDFG 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  950 LSRLILPYRTHVTTELVGTLGYIPPEY---GQAWVATlRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14076  152 FANTFDHFNGDLMSTSCGSPCYAAPELvvsDSMYAGR-KADIWSCGVILYAMLAGYLP 208
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
808-1002 2.74e-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: 54.02  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKAtLDN--GTKLAVKKLTGDYGMMEKEFKA--EVEVLSRAKHENLVALQGYCVHDSAR-----ILIYSF 878
Cdd:cd07859    7 VIGKGSYGVVCSA-IDThtGEKVAIKKINDVFEHVSDATRIlrEIKLLRLLRHPDIVEIKHIMLPPSRRefkdiYVVFEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  879 MENGsldywLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLIL--P 956
Cdd:cd07859   86 MESD-----LHQVIKANDDLTPEHHQFFLYQLLRALKYIHT---ANVFHRDLKPKNILANADCKLKICDFGLARVAFndT 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15218425  957 YRTHVTTELVGTLGYIPPEYGQAWVA--TLRGDVYSFGVVMLELLTGK 1002
Cdd:cd07859  158 PTAIFWTDYVATRWYRAPELCGSFFSkyTPAIDIWSIGCIFAEVLTGK 205
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
808-1004 2.77e-07

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: 53.86  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEFK---AEVEVL-SRAKHENLVALQgycvhdsariliYSFMENG 882
Cdd:cd05575    2 VIGKGSFGKVLLARHKAEGKLyAVKVLQKKAILKRNEVKhimAERNVLlKNVKHPFLVGLH------------YSFQTKD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SL----DY------WLHENPEgpaqldwpKRLNIMRG------ASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVA 946
Cdd:cd05575   70 KLyfvlDYvnggelFFHLQRE--------RHFPEPRArfyaaeIASALGYLHSL---NIIYRDLKPENILLDSQGHVVLT 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  947 DFGLSRLILPyRTHVTTELVGTLGYIPPEY--GQAWVATLrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05575  139 DFGLCKEGIE-PSDTTSTFCGTPEYLAPEVlrKQPYDRTV--DWWCLGAVLYEMLYGLPP 195
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
801-1004 2.90e-07

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: 53.08  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKL------TGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARI 873
Cdd:cd14195    5 DHYEMGEELGSGQFAIVRKCrEKGTGKEYAAKFIkkrrlsSSRRGVSREEIEREVNILREIQHPNIITLHDIFENKTDVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  874 LIYSFMENGSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNI-LLDGNF---KAYVADFG 949
Cdd:cd14195   85 LILELVSGGELFDFLAEK----ESLTEEEATQFLKQILDGVHYLHS---KRIAHFDLKPENImLLDKNVpnpRIKLIDFG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  950 LSRLIlpYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14195  158 IAHKI--EAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASP 210
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
912-1006 3.30e-07

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: 52.85  E-value: 3.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  912 SGLAYMH--QICephivHRDIKSSNILLDGNF--KAYVADFGLSRLILPYRTHVTTelVGTLGYIPPEygqawVATLR-- 985
Cdd:cd14662  107 SGVSYCHsmQIC-----HRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQPKST--VGTPAYIAPE-----VLSRKey 174
                         90       100
                 ....*....|....*....|....*
gi 15218425  986 ----GDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14662  175 dgkvADVWSCGVTLYVMLVGAYPFE 199
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
809-1076 3.31e-07

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: 53.41  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVY----KATldnGTKLAVKkltgdygMMEKEFK---AEVEVLSR-AKHENLVALQGycVHDSARiLIYSFME 880
Cdd:cd14091    8 IGKGSYSVCKrcihKAT---GKEYAVK-------IIDKSKRdpsEEIEILLRyGQHPNIITLRD--VYDDGN-SVYLVTE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 --NGS--LDYWLHEN--PEGPAQldwpkrlNIMRGASSGLAYMHQicePHIVHRDIKSSNILL---DGNFKAY-VADFGL 950
Cdd:cd14091   75 llRGGelLDRILRQKffSEREAS-------AVMKTLTKTVEYLHS---QGVVHRDLKPSNILYadeSGDPESLrICDFGF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  951 SR--------LILP-YrthvttelvgTLGYIPPEygqawVATLRG-----DVYSFGVVMLELLTGKRPmevfrpkmsrel 1016
Cdd:cd14091  145 AKqlraenglLMTPcY----------TANFVAPE-----VLKKQGydaacDIWSLGVLLYTMLAGYTP------------ 197
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425 1017 vawvHTMKRDGKPEEVfdtLLR--------ESGNEEAmlrVLDIACMCV----NQNPMKRPNIQQVVD--WLKN 1076
Cdd:cd14091  198 ----FASGPNDTPEVI---LARigsgkidlSGGNWDH---VSDSAKDLVrkmlHVDPSQRPTAAQVLQhpWIRN 261
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
912-1006 3.60e-07

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: 52.68  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  912 SGLAYMH--QICephivHRDIKSSNILLDGNF--KAYVADFGLSRLILPYRTHVTTelVGTLGYIPPEY--GQAWVATLr 985
Cdd:cd14665  107 SGVSYCHsmQIC-----HRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQPKST--VGTPAYIAPEVllKKEYDGKI- 178
                         90       100
                 ....*....|....*....|.
gi 15218425  986 GDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14665  179 ADVWSCGVTLYVMLVGAYPFE 199
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
913-1027 3.73e-07

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: 53.16  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  913 GLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRL-ILPYRThvTTELVGTLGYIPPE------YGQAWvatlr 985
Cdd:cd05587  109 GLFFLHS---KGIIYRDLKLDNVMLDAEGHIKIADFGMCKEgIFGGKT--TRTFCGTPDYIAPEiiayqpYGKSV----- 178
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  986 gDVYSFGVVMLELLTGKRPME---------------VFRPK-MSRELVAWV------HTMKRDG 1027
Cdd:cd05587  179 -DWWAYGVLLYEMLAGQPPFDgededelfqsimehnVSYPKsLSKEAVSICkglltkHPAKRLG 241
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
809-1004 3.83e-07

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: 53.34  E-value: 3.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRAKHEN---LVALQGYCVHDSARILIYSFMEN 881
Cdd:cd05586    1 IGKGTFGQVYQVrKKDTRRIYAMKVLSKKVIVAKKEVAhtiGERNILVRTALDEspfIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLdYWlHENPEGPAQLDWPKrlniMRGASSGLAYMHqICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRThV 961
Cdd:cd05586   81 GEL-FW-HLQKEGRFSEDRAK----FYIAELVLALEH-LHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNK-T 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  962 TTELVGTLGYIPPE-------YGQawvatlRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05586  153 TNTFCGTTEYLAPEvlldekgYTK------MVDFWSLGVLVFEMCCGWSP 196
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
801-1023 4.42e-07

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: 53.52  E-value: 4.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKEFKAEVevlsRAKHENLVALQGYCVHDsariLIYSFME 880
Cdd:cd05627    2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHI----RAERDILVEADGAWVVK----MFYSFQD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHENPEGPAQLDWPKRLNIMRGASS--------GLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGL-S 951
Cdd:cd05627   74 KRNLYLIMEFLPGGDMMTLLMKKDTLSEEATQfyiaetvlAIDAIHQL---GFIHRDIKPDNLLLDAKGHVKLSDFGLcT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  952 RLILPYRTHVTTEL---------------------------------VGTLGYIPPEYGQAWVATLRGDVYSFGVVMLEL 998
Cdd:cd05627  151 GLKKAHRTEFYRNLthnppsdfsfqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEM 230
                        250       260
                 ....*....|....*....|....*.
gi 15218425  999 LTGKRPMEVFRPKMS-RELVAWVHTM 1023
Cdd:cd05627  231 LIGYPPFCSETPQETyRKVMNWKETL 256
LRRNT_2 pfam08263
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
49-87 4.48e-07

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


Pssm-ID: 462411 [Multi-domain]  Cd Length: 41  Bit Score: 47.29  E-value: 4.48e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 15218425     49 NLQDRDSLLWFSGNVSSPVSPL-HWN-SSIDCCSWEGISCD 87
Cdd:pfam08263    1 LNDDGQALLAFKSSLNDPPGALsSWNsSSSDPCSWTGVTCD 41
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
801-1073 4.48e-07

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: 53.34  E-value: 4.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEK----EFKAEVEVLSRAKHENLVALQgYCVHDSARI-LI 875
Cdd:cd05610    4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKnmvhQVQAERDALALSKSPFIVHLY-YSLQSANNVyLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  876 YSFMENGSLDYWLHENpegpAQLDWPKRLNIMRGASSGLAYMHQicepH-IVHRDIKSSNILLDGNFKAYVADFGLSRLI 954
Cdd:cd05610   83 MEYLIGGDVKSLLHIY----GYFDEEMAVKYISEVALALDYLHR----HgIIHRDLKPDNMLISNEGHIKLTDFGLSKVT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  955 L------------------------------------------PYRT---------HVTTE-LVGTLGYIPPE--YGQAW 980
Cdd:cd05610  155 LnrelnmmdilttpsmakpkndysrtpgqvlslisslgfntptPYRTpksvrrgaaRVEGErILGTPDYLAPEllLGKPH 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  981 VATLrgDVYSFGVVMLELLTGKRPMEvfrpkmsrelvawvhtmkrDGKPEEVFDTLLRES-----GNEEAMLRVLDIACM 1055
Cdd:cd05610  235 GPAV--DWWALGVCLFEFLTGIPPFN-------------------DETPQQVFQNILNRDipwpeGEEELSVNAQNAIEI 293
                        330       340
                 ....*....|....*....|....*.
gi 15218425 1056 CVNQNPMKRPNIQQV--------VDW 1073
Cdd:cd05610  294 LLTMDPTKRAGLKELkqhplfhgVDW 319
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
809-1005 4.83e-07

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: 53.18  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT---LDNGTKLAVKKLTGDYG--MMEKEFKAEVEVLSRAK-HENLVALQGY-CVHDSARILIYSFMEn 881
Cdd:cd07857    8 LGQGAYGIVCSARnaeTSEEETVAIKKITNVFSkkILAKRALRELKLLRHFRgHKNITCLYDMdIVFPGNFNELYLYEE- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 gSLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHV 961
Cdd:cd07857   87 -LMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHS---ANVLHRDLKPGNLLVNADCELKICDFGLARGFSENPGEN 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15218425  962 T---TELVGTLGYIPPE-------YGQAWvatlrgDVYSFGVVMLELLtGKRPM 1005
Cdd:cd07857  163 AgfmTEYVATRWYRAPEimlsfqsYTKAI------DVWSVGCILAELL-GRKPV 209
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
913-1026 4.92e-07

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: 52.52  E-value: 4.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  913 GLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFG 992
Cdd:cd14111  111 GLEYLHG---RRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIG 187
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15218425  993 VVMLELLTGKRPMEVFRPkmsRELVAWVHTMKRD 1026
Cdd:cd14111  188 VLTYIMLSGRSPFEDQDP---QETEAKILVAKFD 218
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
802-1004 5.00e-07

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: 52.41  E-value: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVY----KATldnGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLVALqgYCVHDSARIL 874
Cdd:cd05609    1 DFETIKLISNGAYGAVYlvrhRET---RQRFAMKKINKQNLILRNQIQqvfVERDILTFAENPFVVSM--YCSFETKRHL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  875 --IYSFMENGSLDYWLHENpeGPAQLDWPKrlniMRGASSGLA--YMHQIcepHIVHRDIKSSNILLD--GNFKayVADF 948
Cdd:cd05609   76 cmVMEYVEGGDCATLLKNI--GPLPVDMAR----MYFAETVLAleYLHSY---GIVHRDLKPDNLLITsmGHIK--LTDF 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  949 GLSRLILPYRT--------------HVTTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05609  145 GLSKIGLMSLTtnlyeghiekdtreFLDKQVCGTPEYIAPEvilrqgYGKPV------DWWAMGIILYEFLVGCVP 214
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
797-1027 5.11e-07

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: 53.08  E-value: 5.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  797 LKATDnFSQANIIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLVALQGYCVHDSAR 872
Cdd:cd05615    7 VRLTD-FNFLMVLGKGSFGKVMLAERKGSDELyAIKILKKDVVIQDDDVEctmVEKRVLALQDKPPFLTQLHSCFQTVDR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 I-LIYSFMENGSLDYWLHEnpegPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLS 951
Cdd:cd05615   86 LyFVMEYVNGGDLMYHIQQ----VGKFKEPQAVFYAAEISVGLFFLHK---KGIIYRDLKLDNVMLDSEGHIKIADFGMC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  952 RLILpYRTHVTTELVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRPM------EVFRPKMSRElVAW 1019
Cdd:cd05615  159 KEHM-VEGVTTRTFCGTPDYIAPEiiayqpYGRSV------DWWAYGVLLYEMLAGQPPFdgededELFQSIMEHN-VSY 230

                 ....*...
gi 15218425 1020 VHTMKRDG 1027
Cdd:cd05615  231 PKSLSKEA 238
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
809-999 5.16e-07

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 52.56  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTKLA---VKKLTGDYGMMEKE-FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL 884
Cdd:cd05086    5 IGNGWFGKVLLGEIYTGTSVArvvVKELKASANPKEQDdFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWL---HENPEGPAQLDWPKRLNIMRGAssGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGlsrlILPYR--- 958
Cdd:cd05086   85 KTYLanqQEKLRGDSQIMLLQRMACEIAA--GLAHMHKH---NFLHSDLALRNCYLTSDLTVKVGDYG----IGFSRyke 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15218425  959 --THVTTELVGTLGYIPPE-----YGQAWVA--TLRGDVYSFGVVMLELL 999
Cdd:cd05086  156 dyIETDDKKYAPLRWTAPElvtsfQDGLLAAeqTKYSNIWSLGVTLWELF 205
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
784-1004 5.59e-07

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: 53.08  E-value: 5.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  784 SRYEVKDLTIFELLKATDNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE----FKAEVEVLSRAKHENL 859
Cdd:cd05621   35 NRYEKIVNKIRELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSdsafFWEERDIMAFANSPWV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  860 VALqgYCVHDSARIL--IYSFMENGSLDYWLhenpegpAQLDWPKRLNIMRGASSGLAyMHQICEPHIVHRDIKSSNILL 937
Cdd:cd05621  115 VQL--FCAFQDDKYLymVMEYMPGGDLVNLM-------SNYDVPEKWAKFYTAEVVLA-LDAIHSMGLIHRDVKPDNMLL 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  938 DGNFKAYVADFGLS-RLILPYRTHVTTElVGTLGYIPPE----------YGQawvatlRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05621  185 DKYGHLKLADFGTCmKMDETGMVHCDTA-VGTPDYISPEvlksqggdgyYGR------ECDWWSVGVFLFEMLVGDTP 255
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
825-1074 6.20e-07

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: 52.13  E-value: 6.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  825 GTKLAVK----KLTGDYGMMEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWLHENpegpAQLDW 900
Cdd:cd14070   27 GEKVAIKvidkKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGNLMHRIYDK----KRLEE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  901 PKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVADFGLSRL--ILPYRTHVTTElVGTLGYIPPE--- 975
Cdd:cd14070  103 REARRYIRQLVSAVEHLHR---AGVVHRDLKIENLLLDENDNIKLIDFGLSNCagILGYSDPFSTQ-CGSPAYAAPElla 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  976 ---YGQawvatlRGDVYSFGVVMLELLTGKRPMEVfRPKMSRELvawvHTMKRDGKPEEVFDTLlrESGNEEAMLRVLDi 1052
Cdd:cd14070  179 rkkYGP------KVDVWSIGVNMYAMLTGTLPFTV-EPFSLRAL----HQKMVDKEMNPLPTDL--SPGAISFLRSLLE- 244
                        250       260
                 ....*....|....*....|....
gi 15218425 1053 acmcvnQNPMKRPNIQQVV--DWL 1074
Cdd:cd14070  245 ------PDPLKRPNIKQALanRWL 262
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
809-1000 6.50e-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: 52.56  E-value: 6.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLD-NGTKLAVKKLTGD----YGMMEKEFKAEVEVLSRakHENLVALQgYCV-----------HDSAR 872
Cdd:cd13977    8 VGRGSYGVVYEAVVRrTGARVAVKKIRCNapenVELALREFWALSSIQRQ--HPNVIQLE-ECVlqrdglaqrmsHGSSK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 ILIY--------------------------SFMENGSLD-YWLHENPEgpaqldwpKRLN--IMRGASSGLAYMHQiceP 923
Cdd:cd13977   85 SDLYlllvetslkgercfdprsacylwfvmEFCDGGDMNeYLLSRRPD--------RQTNtsFMLQLSSALAFLHR---N 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  924 HIVHRDIKSSNILLD---GNFKAYVADFGLSRLI----------LPYRTHVTTELVGTLGYIPPEygqAWVA--TLRGDV 988
Cdd:cd13977  154 QIVHRDLKPDNILIShkrGEPILKVADFGLSKVCsgsglnpeepANVNKHFLSSACGSDFYMAPE---VWEGhyTAKADI 230
                        250
                 ....*....|....*
gi 15218425  989 YSFGVV---MLELLT 1000
Cdd:cd13977  231 FALGIIiwaMVERIT 245
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
809-1014 6.56e-07

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: 51.95  E-value: 6.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVyKATLDNGT--KLAVKKLtgDYGMMEKEFK----AEVEVLSRAKHENLVALqgY-CVHDSARI-LIYSFME 880
Cdd:cd14075   10 LGSGNFSQV-KLGIHQLTkeKVAIKIL--DKTKLDQKTQrllsREISSMEKLHHPNIIRL--YeVVETLSKLhLVMEYAS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  881 NGSLDYWLHEN---PEGPAQldwpkrlNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPY 957
Cdd:cd14075   85 GGELYTKISTEgklSESEAK-------PLFAQIVSAVKHMHEN---NIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218425  958 RTHVTteLVGTLGYIPPE------YGQAWVatlrgDVYSFGVVMLELLTGKRPmevFR----PKMSR 1014
Cdd:cd14075  155 ETLNT--FCGSPPYAAPElfkdehYIGIYV-----DIWALGVLLYFMVTGVMP---FRaetvAKLKK 211
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
802-1007 6.99e-07

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: 52.73  E-value: 6.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  802 NFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE----FKAEVEVLSRAK-HENLVALQGYCVHDSARILIY 876
Cdd:cd05618   21 DFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEdidwVQTEKHVFEQASnHPFLVGLHSCFQTESRLFFVI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHEN---PEGPAQLdwpkrlnIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL 953
Cdd:cd05618  101 EYVNGGDLMFHMQRQrklPEEHARF-------YSAEISLALNYLH---ERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKE 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  954 IL-PYRThvTTELVGTLGYIPPEygqawvaTLRGDVYSF-------GVVMLELLTGKRPMEV 1007
Cdd:cd05618  171 GLrPGDT--TSTFCGTPNYIAPE-------ILRGEDYGFsvdwwalGVLMFEMMAGRSPFDI 223
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
926-1024 7.34e-07

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: 52.32  E-value: 7.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  926 VHRDIKSSNILLD--GNFKayVADFGLSRlilPYR-TH-----VTTELVGTLGYIPPE------YGQAWvatlrgDVYSF 991
Cdd:cd05598  123 IHRDIKPDNILIDrdGHIK--LTDFGLCT---GFRwTHdskyyLAHSLVGTPNYIAPEvllrtgYTQLC------DWWSV 191
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15218425  992 GVVMLELLTGKRPMEVFRPKMSRE-LVAWVHTMK 1024
Cdd:cd05598  192 GVILYEMLVGQPPFLAQTPAETQLkVINWRTTLK 225
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
809-1001 7.51e-07

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a 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. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 51.87  E-value: 7.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAtldngtklaVKKLTGDYGMMEK-----------------EFKAEVEVLSRAKHENLVALQGYCVHDSA 871
Cdd:cd05078    7 LGQGTFTKIFKG---------IRREVGDYGQLHEtevllkvldkahrnyseSFFEAASMMSQLSHKHLVLNYGVCVCGDE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  872 RILIYSFMENGSLDYWLHENPEGpaqldwpkrLNIMRG--ASSGLAY-MHQICEPHIVHRDIKSSNILL-------DGNF 941
Cdd:cd05078   78 NILVQEYVKFGSLDTYLKKNKNC---------INILWKleVAKQLAWaMHFLEEKTLVHGNVCAKNILLireedrkTGNP 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218425  942 K-AYVADFGLSRLILPYRThvtteLVGTLGYIPPE-YGQAWVATLRGDVYSFGVVMLELLTG 1001
Cdd:cd05078  149 PfIKLSDPGISITVLPKDI-----LLERIPWVPPEcIENPKNLSLATDKWSFGTTLWEICSG 205
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
801-1004 7.83e-07

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: 52.72  E-value: 7.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYkatldngtkLAVKKLTGDYGMMeKEFKAEV--------------EVLSRAKHENLVALQgYC 866
Cdd:cd05594   25 NDFEYLKLLGKGTFGKVI---------LVKEKATGRYYAM-KILKKEVivakdevahtltenRVLQNSRHPFLTALK-YS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  867 VHDSARILIYSFMENGSlDYWLHENPEGPAQLDWPKrlniMRGAS--SGLAYMHQicEPHIVHRDIKSSNILLDGNFKAY 944
Cdd:cd05594   94 FQTHDRLCFVMEYANGG-ELFFHLSRERVFSEDRAR----FYGAEivSALDYLHS--EKNVVYRDLKLENLMLDKDGHIK 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  945 VADFGLSRLILPYRTHVTTeLVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05594  167 ITDFGLCKEGIKDGATMKT-FCGTPEYLAPEvledndYGRAV------DWWGLGVVMYEMMCGRLP 225
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
809-1002 8.09e-07

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 52.38  E-value: 8.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGT---KLAVKKLTGDYGMMEKefKAEVEVLSRAKHENLVALQGYCVHDSAR--ILIYSFMENgs 883
Cdd:cd07867   10 VGRGTYGHVYKAKRKDGKdekEYALKQIEGTGISMSA--CREIALLRELKHPNVIALQKVFLSHSDRkvWLLFDYAEH-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 lDYW----LHENPEG---PAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGN----FKAYVADFGLSR 952
Cdd:cd07867   86 -DLWhiikFHRASKAnkkPMQLPRSMVKSLLYQILDGIHYLHA---NWVLHRDLKPANILVMGEgperGRVKIADMGFAR 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  953 LI-LPYRTHVTTE-LVGTLGYIPPEY---GQAWVATLrgDVYSFGVVMLELLTGK 1002
Cdd:cd07867  162 LFnSPLKPLADLDpVVVTFWYRAPELllgARHYTKAI--DIWAIGCIFAELLTSE 214
PLN03150 PLN03150
hypothetical protein; Provisional
173-271 9.10e-07

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 52.90  E-value: 9.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   173 IQTVDLSSNLLEGEILSSSVFLQgafNLTSFNVSNNSFTGSIPSFMCTASpQLTKLDFSYNDFSGDLSQELSRCSRLSVL 252
Cdd:PLN03150  420 IDGLGLDNQGLRGFIPNDISKLR---HLQSINLSGNSIRGNIPPSLGSIT-SLEVLDLSYNSFNGSIPESLGQLTSLRIL 495
                          90
                  ....*....|....*....
gi 15218425   253 RAGFNNLSGEIPKEIYNLP 271
Cdd:PLN03150  496 NLNGNSLSGRVPAALGGRL 514
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
808-1004 9.22e-07

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: 52.19  E-value: 9.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTKL-AVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGS 883
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIyALKTIRKAHIVSRSEVThtlAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  884 LDYwlHENPEGpaqldwpkRLNIMRG---ASSGLAYMHQICEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPyRTH 960
Cdd:cd05585   81 LFH--HLQREG--------RFDLSRArfyTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMK-DDD 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15218425  961 VTTELVGTLGYIPPEY--GQAWVATLrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05585  150 KTNTFCGTPEYLAPELllGHGYTKAV--DWWTLGVLLYEMLTGLPP 193
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
914-1006 1.01e-06

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 51.90  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  914 LAYMHqicEPHIVHRDIKSSNILLDGNF---KAYVADFGLSrlilpYRTHVTTELV-----------GTLGYIPPEYGQA 979
Cdd:cd14015  140 LEYIH---ENGYVHADIKASNLLLGFGKnkdQVYLVDYGLA-----SRYCPNGKHKeykedprkahnGTIEFTSRDAHKG 211
                         90       100
                 ....*....|....*....|....*..
gi 15218425  980 WVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14015  212 VAPSRRGDLEILGYNMLQWLCGKLPWE 238
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
800-1004 1.01e-06

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: 51.75  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  800 TDNFSQANIIGCGGFGLVYKATLDNGTK-LAVKKL--TGDygmmEKEFKAEVEVLSRAKHENLVALQGYCVHDSARILIY 876
Cdd:cd14085    2 EDFFEIESELGRGATSVVYRCRQKGTQKpYAVKKLkkTVD----KKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLHEN---PEGPAQldwpkrlNIMRGASSGLAYMHqicEPHIVHRDIKSSNILL-----DGNFKayVADF 948
Cdd:cd14085   78 ELVTGGELFDRIVEKgyySERDAA-------DAVKQILEAVAYLH---ENGIVHRDLKPENLLYatpapDAPLK--IADF 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  949 GLSRLIlpyRTHVTTELV-GTLGYIPPEygqawvaTLRG-------DVYSFGVVMLELLTGKRP 1004
Cdd:cd14085  146 GLSKIV---DQQVTMKTVcGTPGYCAPE-------ILRGcaygpevDMWSVGVITYILLCGFEP 199
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
801-1004 1.04e-06

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: 51.77  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGdygMMEKEFKAEVEVLSRAK-HENLVALQGYCVHDSARI--LIY 876
Cdd:cd14132   18 DDYEIIRKIGRGKYSEVFEGiNIGNNEKVVIKVLKP---VKKKKIKREIKILQNLRgGPNIVKLLDVVKDPQSKTpsLIF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  877 SFMENGSLDYWLhenpegpAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILLDGNF-KAYVADFGLSRLIL 955
Cdd:cd14132   95 EYVNNTDFKTLY-------PTLTDYDIRYYMYELLKALDYCHSK---GIMHRDVKPHNIMIDHEKrKLRLIDWGLAEFYH 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218425  956 P---YRTHvttelVGTLGYIPPE---------YGQawvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14132  165 PgqeYNVR-----VASRYYKGPEllvdyqyydYSL--------DMWSLGCMLASMIFRKEP 212
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
914-1004 1.06e-06

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: 52.02  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  914 LAYMHQIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRLILpYRTHVTTELVGTLGYIPPEygqawVATLRG-----DV 988
Cdd:cd05584  113 LGHLHSL---GIIYRDLKPENILLDAQGHVKLTDFGLCKESI-HDGTVTHTFCGTIEYMAPE-----ILTRSGhgkavDW 183
                         90
                 ....*....|....*.
gi 15218425  989 YSFGVVMLELLTGKRP 1004
Cdd:cd05584  184 WSLGALMYDMLTGAPP 199
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
801-1072 1.15e-06

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: 52.21  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATL------DNGTKLAVKKLTGDYGMMEKE-FKAEVEVLSR-AKHENLVALQGYCVHDSAR 872
Cdd:cd05104   35 DRLRFGKTLGAGAFGKVVEATAyglakaDSAMTVAVKMLKPSAHSTEREaLMSELKVLSYlGNHINIVNLLGACTVGGPT 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 ILIYSFMENGSL--------DYW------------LHEN------PEGPAQLDW-----------PKRLNIMRGASSG-- 913
Cdd:cd05104  115 LVITEYCCYGDLlnflrrkrDSFicpkfedlaeaaLYRNllhqreMACDSLNEYmdmkpsvsyvvPTKADKRRGVRSGsy 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  914 ----------------------LAYMHQICE-------PHIVHRDIKSSNILLDGNFKAYVADFGLSRLIlpyRTHVTTE 964
Cdd:cd05104  195 vdqdvtseileedelaldtedlLSFSYQVAKgmeflasKNCIHRDLAARNILLTHGRITKICDFGLARDI---RNDSNYV 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  965 LVGT----LGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKRPMevfrPKMSRElvAWVHTMKRDGkpeevfdtlLRE 1039
Cdd:cd05104  272 VKGNarlpVKWMAPESIFECVYTFESDVWSYGILLWEIFSlGSSPY----PGMPVD--SKFYKMIKEG---------YRM 336
                        330       340       350
                 ....*....|....*....|....*....|...
gi 15218425 1040 SGNEEAMLRVLDIACMCVNQNPMKRPNIQQVVD 1072
Cdd:cd05104  337 DSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQ 369
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
847-1005 1.35e-06

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: 51.53  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  847 EVEVLSRAKHENLVALQGYCVHDSARILIYSFMENgSLDYWLHENPEGPAQLDWPKRL-NIMRGassgLAYMHQicePHI 925
Cdd:cd07872   54 EVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDK-DLKQYMDDCGNIMSMHNVKIFLyQILRG----LAYCHR---RKV 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  926 VHRDIKSSNILLDGNFKAYVADFGLSRL-ILPYRTHvTTELVgTLGYIPPE--YGQAWVATlRGDVYSFGVVMLELLTGk 1002
Cdd:cd07872  126 LHRDLKPQNLLINERGELKLADFGLARAkSVPTKTY-SNEVV-TLWYRPPDvlLGSSEYST-QIDMWGVGCIFFEMASG- 201

                 ...
gi 15218425 1003 RPM 1005
Cdd:cd07872  202 RPL 204
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
916-1015 1.41e-06

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: 51.95  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  916 YMHQIC-------EPHIVHRDIKSSNILLDGNFKAYVADFGLSRL-ILPYRThvTTELVGTLGYIPPEygqawvaTLRGD 987
Cdd:cd05617  121 YAAEICialnflhERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEgLGPGDT--TSTFCGTPNYIAPE-------ILRGE 191
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15218425  988 VYSF-------GVVMLELLTGKRPMEVF--RPKMSRE 1015
Cdd:cd05617  192 EYGFsvdwwalGVLMFEMMAGRSPFDIItdNPDMNTE 228
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
798-1004 1.42e-06

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: 51.62  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  798 KATDNFSQANIIGCGGFGLVY----KATldnGTKLAVKKLTGDYGMMEKEFK---AEVEVLSRAKHENLVALQgYCVHDS 870
Cdd:cd05593   12 KTMNDFDYLKLLGKGTFGKVIlvreKAS---GKYYAMKILKKEVIIAKDEVAhtlTESRVLKNTRHPFLTSLK-YSFQTK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  871 ARI-LIYSFMENGSLdyWLHENPEGPAQLDWPKrlniMRGAS--SGLAYMHQicePHIVHRDIKSSNILLDGNFKAYVAD 947
Cdd:cd05593   88 DRLcFVMEYVNGGEL--FFHLSRERVFSEDRTR----FYGAEivSALDYLHS---GKIVYRDLKLENLMLDKDGHIKITD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218425  948 FGLSRLILPYRTHVTTeLVGTLGYIPPE------YGQAWvatlrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd05593  159 FGLCKEGITDAATMKT-FCGTPEYLAPEvledndYGRAV------DWWGLGVVMYEMMCGRLP 214
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
809-1070 1.54e-06

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: 51.10  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKATLDNGTK------LAVKKLTGDYGM----------------------MEKEFKaEVEVLSRAKHENLV 860
Cdd:cd14200    8 IGKGSYGVVKLAYNESDDKyyamkvLSKKKLLKQYGFprrppprgskaaqgeqakplapLERVYQ-EIAILKKLDHVNIV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  861 ALQgYCVHDSAR---ILIYSFMENGSLDYWLHENPEGPAQldwpKRLnIMRGASSGLAYMHqiCEpHIVHRDIKSSNILL 937
Cdd:cd14200   87 KLI-EVLDDPAEdnlYMVFDLLRKGPVMEVPSDKPFSEDQ----ARL-YFRDIVLGIEYLH--YQ-KIVHRDIKPSNLLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  938 --DGNFKayVADFGLSRLILPYRTHVTTElVGTLGYIPPEY----GQAWVATLRgDVYSFGVVMLELLTGKRPmevfrpk 1011
Cdd:cd14200  158 gdDGHVK--IADFGVSNQFEGNDALLSST-AGTPAFMAPETlsdsGQSFSGKAL-DVWAMGVTLYCFVYGKCP------- 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425 1012 MSRELVAWVHTmKRDGKPEEVFDTLLRESGNEEAMLRVLDiacmcvnQNPMKRPNIQQV 1070
Cdd:cd14200  227 FIDEFILALHN-KIKNKPVEFPEEPEISEELKDLILKMLD-------KNPETRITVPEI 277
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
844-1071 1.59e-06

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: 51.06  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  844 FKAEVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSLDYWLHENpEGPAQLDWpkRLNIMRGASSGLAYMHqicEP 923
Cdd:cd05076   62 FFETASLMSQVSHTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLRKE-KGHVPMAW--KFVVARQLASALSYLE---NK 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  924 HIVHRDIKSSNIL-----LDGNFKAYV--ADFGLSRLILPYRthvttELVGTLGYIPPEY--GQAWVATlRGDVYSFGVV 994
Cdd:cd05076  136 NLVHGNVCAKNILlarlgLEEGTSPFIklSDPGVGLGVLSRE-----ERVERIPWIAPECvpGGNSLST-AADKWGFGAT 209
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425  995 MLEL-LTGKRPMEvfrpkmSRELVAWVHTMKRDGKpeevfdtlLRESGNEEamlrVLDIACMCVNQNPMKRPNIQQVV 1071
Cdd:cd05076  210 LLEIcFNGEAPLQ------SRTPSEKERFYQRQHR--------LPEPSCPE----LATLISQCLTYEPTQRPSFRTIL 269
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
913-1007 1.63e-06

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: 51.27  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  913 GLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRL-ILPYRThvTTELVGTLGYIPPEygqawvaTLRGDVYSF 991
Cdd:cd05588  108 ALNFLH---EKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEgLRPGDT--TSTFCGTPNYIAPE-------ILRGEDYGF 175
                         90       100
                 ....*....|....*....|...
gi 15218425  992 -------GVVMLELLTGKRPMEV 1007
Cdd:cd05588  176 svdwwalGVLMFEMLAGRSPFDI 198
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
808-1006 1.96e-06

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: 50.61  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATLDNGTK-LAVKKLTGDYGMMEKeFKAEVEVLSRAKHENLVALQGycVHDSA-RILIYSFMENGSld 885
Cdd:cd14087    8 LIGRGSFSRVVRVEHRVTRQpYAIKMIETKCRGREV-CESELNVLRRVRHTNIIQLIE--VFETKeRVYMVMELATGG-- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  886 yWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQIcepHIVHRDIKSSNILL---DGNFKAYVADFGLSRLILPYRTHVT 962
Cdd:cd14087   83 -ELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGL---GITHRDLKPENLLYyhpGPDSKIMITDFGLASTRKKGPNCLM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15218425  963 TELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRPME 1006
Cdd:cd14087  159 KTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFD 202
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
809-1004 2.05e-06

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: 50.34  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAtLDNGTK--LAVKKLTGDygMMEKEFKA-EVEVLSRAKHENLVALQGYCVHDSARILIYSFMENGSL- 884
Cdd:cd14115    1 IGRGRFSIVKKC-LHKATRkdVAVKFVSKK--MKKKEQAAhEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLl 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  885 DYWLHENpegpaQLDWPKRLNIMRGASSGLAYMHQiCEphIVHRDIKSSNILLDGNF---KAYVADFGLS-RLILPYRTH 960
Cdd:cd14115   78 DYLMNHD-----ELMEEKVAFYIRDIMEALQYLHN-CR--VAHLDIKPENLLIDLRIpvpRVKLIDLEDAvQISGHRHVH 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15218425  961 vttELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14115  150 ---HLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSP 190
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
847-999 2.93e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 50.64  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   847 EVEVLSRAKHENLVALQGYCVHDSARILI--------YSFMENGSldywlhenpeGPAQLDwpKRLNIMRGASSGLAYMH 918
Cdd:PHA03209  107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVlphyssdlYTYLTKRS----------RPLPID--QALIIEKQILEGLRYLH 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   919 QIcepHIVHRDIKSSNILLDGNFKAYVADFGLSRliLPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLEL 998
Cdd:PHA03209  175 AQ---RIIHRDVKTENIFINDVDQVCIGDLGAAQ--FPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEM 249

                  .
gi 15218425   999 L 999
Cdd:PHA03209  250 L 250
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
802-1004 3.47e-06

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 50.20  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   802 NFSQANIIGCGGFGLVykatldngtKLAVKKLTGDYGMMEKEFKAEVEVLSRAKHENLVA--LQGYCvHDSARILIYSFM 879
Cdd:PTZ00263   19 DFEMGETLGTGSFGRV---------RIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKsiLMELS-HPFIVNMMCSFQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   880 ENGSLdYWLHENPEGPAQLD-------WPKRLNIMRGASSGLA--YMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGL 950
Cdd:PTZ00263   89 DENRV-YFLLEFVVGGELFThlrkagrFPNDVAKFYHAELVLAfeYLH---SKDIIYRDLKPENLLLDNKGHVKVTDFGF 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15218425   951 SRLIlPYRTHVtteLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:PTZ00263  165 AKKV-PDRTFT---LCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPP 214
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
808-1004 4.05e-06

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: 49.72  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  808 IIGCGGFGLVYKATL-DNGTKLAVK---KLTGDYgMMEKEFKAEVEVLSRAKHENLVALQGYCvhdSARILIYSFME--N 881
Cdd:cd14082   10 VLGSGQFGIVYGGKHrKTGRDVAIKvidKLRFPT-KQESQLRNEVAILQQLSHPGVVNLECMF---ETPERVFVVMEklH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  882 GSLDYWLHENPEGpaqldwpkRLN------IMRGASSGLAYMHqicEPHIVHRDIKSSNILL--DGNF-KAYVADFGLSR 952
Cdd:cd14082   86 GDMLEMILSSEKG--------RLPeritkfLVTQILVALRYLH---SKNIVHCDLKPENVLLasAEPFpQVKLCDFGFAR 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  953 LI--LPYRTHVttelVGTLGYIPPEY--GQAWVATLrgDVYSFGVVMLELLTGKRP 1004
Cdd:cd14082  155 IIgeKSFRRSV----VGTPAYLAPEVlrNKGYNRSL--DMWSVGVIIYVSLSGTFP 204
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
784-1004 4.40e-06

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: 50.39  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  784 SRYEVKDLTIFELLKATDNFSQANIIGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE----FKAEVEVLSRAKHENL 859
Cdd:cd05622   56 SRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSdsafFWEERDIMAFANSPWV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  860 VALQGYCVHDSARILIYSFMENGSLDYWLhenpegpAQLDWPKRLNIMRGASSGLAyMHQICEPHIVHRDIKSSNILLDG 939
Cdd:cd05622  136 VQLFYAFQDDRYLYMVMEYMPGGDLVNLM-------SNYDVPEKWARFYTAEVVLA-LDAIHSMGFIHRDVKPDNMLLDK 207
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  940 NFKAYVADFGLSRLILPYRTHVTTELVGTLGYIPPE----------YGQawvatlRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05622  208 SGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEvlksqggdgyYGR------ECDWWSVGVFLYEMLVGDTP 276
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
801-1031 4.60e-06

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: 49.83  E-value: 4.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYKATLDNGTKL-AVKKLTGDygmMEKE-----FKAEVEVLSRAKHENLVA--LQGYCVHDSAR 872
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLvALKKTRLE---MEEEgvpstALREVSLLQMLSQSIYIVrlLDVEHVEENGK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  873 ILIYSFME--NGSLDYWLHENPEGPAQ-LDWPKRLNIMRGASSGLAYMHQicepH-IVHRDIKSSNILLD---GNFKayV 945
Cdd:cd07837   78 PLLYLVFEylDTDLKKFIDSYGRGPHNpLPAKTIQSFMYQLCKGVAHCHS----HgVMHRDLKPQNLLVDkqkGLLK--I 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  946 ADFGLSR-LILPYRTHvTTELVgTLGYIPPE--YGQAWVATlRGDVYSFGVVMLELLtgkRPMEVFrPKMSrELVAWVHT 1022
Cdd:cd07837  152 ADLGLGRaFTIPIKSY-THEIV-TLWYRAPEvlLGSTHYST-PVDMWSVGCIFAEMS---RKQPLF-PGDS-ELQQLLHI 223

                 ....*....
gi 15218425 1023 MKRDGKPEE 1031
Cdd:cd07837  224 FRLLGTPNE 232
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
781-1002 5.13e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 50.06  E-value: 5.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  781 FGNSRYEVKDLTIFELLKatdnfsqaniIGCGGFGLVYKATLDNGTK---LAVKKLTGDYGMMEKefKAEVEVLSRAKHE 857
Cdd:cd07868    7 LTGERERVEDLFEYEGCK----------VGRGTYGHVYKAKRKDGKDdkdYALKQIEGTGISMSA--CREIALLRELKHP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  858 NLVALQG-YCVHDSARI-LIYSFMENgslDYW----LHENPEG---PAQLDWPKRLNIMRGASSGLAYMHQicePHIVHR 928
Cdd:cd07868   75 NVISLQKvFLSHADRKVwLLFDYAEH---DLWhiikFHRASKAnkkPVQLPRGMVKSLLYQILDGIHYLHA---NWVLHR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  929 DIKSSNILLDGN----FKAYVADFGLSRLI-LPYRTHVTTE-LVGTLGYIPPEY---GQAWVATLrgDVYSFGVVMLELL 999
Cdd:cd07868  149 DLKPANILVMGEgperGRVKIADMGFARLFnSPLKPLADLDpVVVTFWYRAPELllgARHYTKAI--DIWAIGCIFAELL 226

                 ...
gi 15218425 1000 TGK 1002
Cdd:cd07868  227 TSE 229
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
926-1077 5.15e-06

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 49.98  E-value: 5.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  926 VHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTT-ELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-GKR 1003
Cdd:cd05103  201 IHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKgDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSlGAS 280
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218425 1004 PMEVFrpKMSRELVAWVHTMKRDGKPE----EVFDTLLResgneeamlrvldiacmCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd05103  281 PYPGV--KIDEEFCRRLKEGTRMRAPDyttpEMYQTMLD-----------------CWHGEPSQRPTFSELVEHLGNL 339
PLN03150 PLN03150
hypothetical protein; Provisional
237-316 5.92e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 50.20  E-value: 5.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   237 GDLSQELSRCSRLSVLRAGFNNLSGEIPKEIYNLPELEQLFLPVNRLSGKIDNGITRLTKLTLLELYSNHIEGEIPKDIG 316
Cdd:PLN03150  432 GFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAALG 511
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
926-1077 8.96e-06

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 49.23  E-value: 8.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  926 VHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHV---TTELvgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLT-G 1001
Cdd:cd14207  202 IHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVrkgDARL--PLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSlG 279
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425 1002 KRPMevfrPKMSRElvawvhtmkrdgkpEEVFDTL---LRESGNEEAMLRVLDIACMCVNQNPMKRPNIQQVVDWLKNI 1077
Cdd:cd14207  280 ASPY----PGVQID--------------EDFCSKLkegIRMRAPEFATSEIYQIMLDCWQGDPNERPRFSELVERLGDL 340
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
801-1004 1.13e-05

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: 48.59  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  801 DNFSQANIIGCGGFGLVYkatldngtkLAVKKLTGDYGMM-------------EKEFKAEVEVLSRAKHENLVALqgYCV 867
Cdd:cd05612    1 DDFERIKTIGTGTFGRVH---------LVRDRISEHYYALkvmaipevirlkqEQHVHNEKRVLKEVSHPFIIRL--FWT 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  868 HDSARIL--IYSFMENGSLDYWLHENpegpaqldwpKRLNIMRG---AS---SGLAYMHQIcepHIVHRDIKSSNILLDG 939
Cdd:cd05612   70 EHDQRFLymLMEYVPGGELFSYLRNS----------GRFSNSTGlfyASeivCALEYLHSK---EIVYRDLKPENILLDK 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425  940 NFKAYVADFGLSRLILPyRTHVtteLVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd05612  137 EGHIKLTDFGFAKKLRD-RTWT---LCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPP 197
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
913-1008 1.25e-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: 48.45  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  913 GLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTTeLVGTLGYIPPEYGQAWVATLRGDVYSFG 992
Cdd:cd05589  113 GLQFLH---EHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTST-FCGTPEFLAPEVLTDTSYTRAVDWWGLG 188
                         90       100
                 ....*....|....*....|..
gi 15218425  993 VVMLELLTGKRPM------EVF 1008
Cdd:cd05589  189 VLIYEMLVGESPFpgddeeEVF 210
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
805-1004 1.25e-05

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: 48.48  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  805 QANIIGCGGFGLVYKA-TLDNGTKLAVKKLTGDYGMMEKEFKAEVEVLSRAK-HENLVALQGYCVHDSARILIYSFMENG 882
Cdd:cd14173    6 QEEVLGEGAYARVQTCiNLITNKEYAVKIIEKRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  883 SLDYWLHENP---EGPAQLdwpkrlnIMRGASSGLAYMHQicePHIVHRDIKSSNILLDGNFK---AYVADFGLSRLI-- 954
Cdd:cd14173   86 SILSHIHRRRhfnELEASV-------VVQDIASALDFLHN---KGIAHRDLKPENILCEHPNQvspVKICDFDLGSGIkl 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15218425  955 ----LPYRTHVTTELVGTLGYIPPEYGQAW-----VATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14173  156 nsdcSPISTPELLTPCGSAEYMAPEVVEAFneeasIYDKRCDLWSLGVILYIMLSGYPP 214
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
913-1001 1.37e-05

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: 48.34  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  913 GLAYMHQICepHIVHRDIKSSNILLD-GNFKAYVADFGLSRLIlpYRtHVTTElVGTLGYIPPE--YGQAWVATlrGDVY 989
Cdd:cd14136  131 GLDYLHTKC--GIIHTDIKPENVLLCiSKIEVKIADLGNACWT--DK-HFTED-IQTRQYRSPEviLGAGYGTP--ADIW 202
                         90
                 ....*....|..
gi 15218425  990 SFGVVMLELLTG 1001
Cdd:cd14136  203 STACMAFELATG 214
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
809-1004 1.50e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 49.35  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   809 IGCGGFGLVYKATLDNGTKLAVKKLTGDYGMMEKE---FKAEVEVLSRAKHENLVALQGYCVHDSARIL--IYSFMENGS 883
Cdd:PTZ00266   21 IGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREksqLVIEVNVMRELKHKNIVRYIDRFLNKANQKLyiLMEFCDAGD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   884 LDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQICE----PHIVHRDIKSSNIL-----------------LDGNFK 942
Cdd:PTZ00266  101 LSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNLKDgpngERVLHRDLKPQNIFlstgirhigkitaqannLNGRPI 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218425   943 AYVADFGLSRLI-LPYRTHvttELVGTLGYIPPEYGQAWVATL--RGDVYSFGVVMLELLTGKRP 1004
Cdd:PTZ00266  181 AKIGDFGLSKNIgIESMAH---SCVGTPYYWSPELLLHETKSYddKSDMWALGCIIYELCSGKTP 242
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
787-1001 1.51e-05

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: 48.49  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  787 EVKDLTiFELLKatdNFSQANIIGCGGFGLVYKAtLDN--GTKLAVKKLTGDYGMMEKEFKA--EVEVLSRAKHENLVAL 862
Cdd:cd07876   11 QVADST-FTVLK---RYQQLKPIGSGAQGIVCAA-FDTvlGINVAVKKLSRPFQNQTHAKRAyrELVLLKCVNHKNIISL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  863 QGycVHDSARIL-----IYSFME--NGSLDYWLHenpegpAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNI 935
Cdd:cd07876   86 LN--VFTPQKSLeefqdVYLVMElmDANLCQVIH------MELDHERMSYLLYQMLCGIKHLHS---AGIIHRDLKPSNI 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218425  936 LLDGNFKAYVADFGLSRliLPYRTHVTTELVGTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTG 1001
Cdd:cd07876  155 VVKSDCTLKILDFGLAR--TACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKG 218
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
809-1004 1.81e-05

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: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  809 IGCGGFGLVYKAT-LDNGTKLAVKKLTgdygmMEKEFKAEVEVLSRAKHENLVALQGyCVHDSARILIY-SFMENGSLDY 886
Cdd:cd13991   14 IGRGSFGEVHRMEdKQTGFQCAVKKVR-----LEVFRAEELMACAGLTSPRVVPLYG-AVREGPWVNIFmDLKEGGSLGQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  887 WLHENPEGPAQLdwpkRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILL--DGNfKAYVADFGLSRLILP---YRTHV 961
Cdd:cd13991   88 LIKEQGCLPEDR----ALHYLGQALEGLEYLHS---RKILHGDVKADNVLLssDGS-DAFLCDFGHAECLDPdglGKSLF 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15218425  962 TTELV-GTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd13991  160 TGDYIpGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHP 203
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
803-937 2.35e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 47.23  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  803 FSQANIIGCGGFGLVYKAT--LDnGTKLAVKKLTGDYGMMEKEFKAEVEVLSRA---KHENLVALQGYCVHDSARILIYS 877
Cdd:cd14139    2 FLELEKIGVGEFGSVYKCIkrLD-GCVYAIKRSMRPFAGSSNEQLALHEVYAHAvlgHHPHVVRYYSAWAEDDHMIIQNE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  878 FMENGSLDYWLHENPEGPAQLDWPKRLNIMRGASSGLAYMHQicePHIVHRDIKSSNILL 937
Cdd:cd14139   81 YCNGGSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHN---SGLVHLDIKPSNIFI 137
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
834-1077 2.73e-05

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 47.71  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  834 TGDY-GMMEKEFKAEVEVLSRAKHENLVALQGyCVHDsaRILIYSFMENGSLDYWLHEN-PEGPAQLDWpkrLNIMRGAS 911
Cdd:cd05105  174 KGDYmDMKQADTTQYVPMLEIKEASKYSDIQR-SNYD--RPASYKGSNDSEVKNLLSDDgSEGLTTLDL---LSFTYQVA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  912 SGLAYMhqiCEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLILPYRTHVTT-ELVGTLGYIPPEYGQAWVATLRGDVYS 990
Cdd:cd05105  248 RGMEFL---ASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKgSTFLPVKWMAPESIFDNLYTTLSDVWS 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  991 FGVVMLELLT---GKRPMEVFRPKMSRELVAWVHTMKRDGKPEEVFDTLLResgneeamlrvldiacmCVNQNPMKRPNI 1067
Cdd:cd05105  325 YGILLWEIFSlggTPYPGMIVDSTFYNKIKSGYRMAKPDHATQEVYDIMVK-----------------CWNSEPEKRPSF 387
                        250
                 ....*....|
gi 15218425 1068 QQVVDWLKNI 1077
Cdd:cd05105  388 LHLSDIVESL 397
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
826-1005 2.83e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 47.92  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   826 TKLAVKKLTGDygmmeKEFKAEVEVLSRAKHENLVALqgycVHD-SARILIYSFMENGSLDYWLHENPEGPAQLDwpKRL 904
Cdd:PHA03207  120 KKVIVKAVTGG-----KTPGREIDILKTISHRAIINL----IHAyRWKSTVCMVMPKYKCDLFTYVDRSGPLPLE--QAI 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   905 NIMRGASSGLAYMHqicEPHIVHRDIKSSNILLDGNFKAYVADFGLSRLIlpyrthvttelvGTLGYIPPEYGqaWVATL 984
Cdd:PHA03207  189 TIQRRLLEALAYLH---GRGIIHRDVKTENIFLDEPENAVLGDFGAACKL------------DAHPDTPQCYG--WSGTL 251
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 15218425   985 ---------------RGDVYSFGVVMLELLTGKRPM 1005
Cdd:PHA03207  252 etnspellaldpycaKTDIWSAGLVLFEMSVKNVTL 287
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
797-1004 3.12e-05

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: 47.32  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  797 LKATDNFSQANIIGCGGFGL----VYKATldnGTKLAVKKLTGDygmmEKEFKAEVEVLSR-AKHENLVALQGycVHDSA 871
Cdd:cd14176   15 IQFTDGYEVKEDIGVGSYSVckrcIHKAT---NMEFAVKIIDKS----KRDPTEEIEILLRyGQHPNIITLKD--VYDDG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425  872 R--ILIYSFMENGSL-DYWLHEN----PEGPAQLdwpkrLNIMRGASsglaYMHQicePHIVHRDIKSSNILL---DGNF 941
Cdd:cd14176   86 KyvYVVTELMKGGELlDKILRQKffseREASAVL-----FTITKTVE----YLHA---QGVVHRDLKPSNILYvdeSGNP 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218425  942 KAY-VADFGLSRLILPYRTHVTTELVgTLGYIPPEYGQAWVATLRGDVYSFGVVMLELLTGKRP 1004
Cdd:cd14176  154 ESIrICDFGFAKQLRAENGLLMTPCY-TANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTP 216
PLN03150 PLN03150
hypothetical protein; Provisional
196-287 5.71e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.04  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218425   196 GAFNLTSFNVSNNSFTGSIPSFMcTASPQLTKLDFSYNDFSGDLSQELSRCSRLSVLRAGFNNLSGEIPKEIYNLPELEQ 275
Cdd:PLN03150  416 GKWFIDGLGLDNQGLRGFIPNDI-SKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRI 494
                          90
                  ....*....|..
gi 15218425   276 LFLPVNRLSGKI 287
Cdd:PLN03150  495 LNLNGNSLSGRV 506
 
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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