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Conserved domains on  [gi|240256081|ref|NP_567748|]
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Leucine-rich repeat 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
32-1038 5.55e-158

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: 493.98  E-value: 5.55e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   32 LLSWKSQLNISGDAFSSWHVADTSpCNWVGVKCNRRGEVSEIQLKGMDLQGSLPVTSLRslksltsltlsslnltgvipk 111
Cdd:PLN00113   34 LLSFKSSINDPLKYLSNWNSSADV-CLWQGITCNNSSRVVSIDLSGKNISGKISSAIFR--------------------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  112 eigdFTELELLDLSDNSLSGDIPVEIFRL-KKLKTLSLNTNNLEGHIPMeiGNLSGLVELMLFDNKLSGEIPRSIGELKN 190
Cdd:PLN00113   92 ----LPYIQTINLSNNQLSGPIPDDIFTTsSSLRYLNLSNNNFTGSIPR--GSIPNLETLDLSNNMLSGEIPNDIGSFSS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  191 LQVLRAGGNKnLRGELPWEIGNCENLVMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLY 270
Cdd:PLN00113  166 LKVLDLGGNV-LVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  271 QNSISGSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTI 350
Cdd:PLN00113  245 YNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  351 PEELTNCTKLTHLEIdnnlitgeipslmsnlrsltmffaWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIFGLR 430
Cdd:PLN00113  325 PVALTSLPRLQVLQL------------------------WSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSG 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  431 NLTKLLLLSNDLSGFIPPDIGNCTNLYRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLH 510
Cdd:PLN00113  381 NLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLA 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  511 TNSLSGSLLGTTLPKSLKFIDFSDNALSSTLPPGIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLLNLGENDFSGEIP 590
Cdd:PLN00113  461 RNKFFGGLPDSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIP 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  591 DELGQIPSLAiSLNLSCNRFVGEIPsrfsdlKNLGvldvshnqltgnlnvltDLQNLVSLNISYNDFSGDLPNTPFFRRL 670
Cdd:PLN00113  541 ASFSEMPVLS-QLDLSQNQLSGEIP------KNLG-----------------NVESLVQVNISHNHLHGSLPSTGAFLAI 596
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  671 PLSDLASNRGLYISNAISTRPDPTTRNSSVVRLTILILVVVTAVLVLMAVYTLV---RARAAGKQLLGEEIDSWEVTLYQ 747
Cdd:PLN00113  597 NASAVAGNIDLCGGDTTSGLPPCKRVRKTPSWWFYITCTLGAFLVLALVAFGFVfirGRNNLELKRVENEDGTWELQFFD 676
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  748 K---LDFSIDDIVKNLTSANVIGTGSSGVVYR-ITIPSGESLAVKKMwsKEESGAFNSEIKTLGSIRHRNIVRLLGWCSN 823
Cdd:PLN00113  677 SkvsKSITINDILSSLKEENVISRGKKGASYKgKSIKNGMQFVVKEI--NDVNSIPSSEIADMGKLQHPNIVKLIGLCRS 754
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  824 RNLKLLFYDYLPNGSLSSRLHGagkggcVDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLadfg 903
Cdd:PLN00113  755 EKGAYLIHEYIEGKNLSEVLRN------LSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHL---- 824
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  904 lartISGYPNT-GIDLAKPTnrppmagSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAHLVKWVR 982
Cdd:PLN00113  825 ----RLSLPGLlCTDTKCFI-------SSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADAEFGVHGSIVEWAR 893
                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  983 D-----HLaekkdpSRLLDPRLDGRTDSIMHEMLQTLAVAFLCVSNKANERPLMKDVVAML 1038
Cdd:PLN00113  894 YcysdcHL------DMWIDPSIRGDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTL 948
 
Name Accession Description Interval E-value
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
32-1038 5.55e-158

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 493.98  E-value: 5.55e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   32 LLSWKSQLNISGDAFSSWHVADTSpCNWVGVKCNRRGEVSEIQLKGMDLQGSLPVTSLRslksltsltlsslnltgvipk 111
Cdd:PLN00113   34 LLSFKSSINDPLKYLSNWNSSADV-CLWQGITCNNSSRVVSIDLSGKNISGKISSAIFR--------------------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  112 eigdFTELELLDLSDNSLSGDIPVEIFRL-KKLKTLSLNTNNLEGHIPMeiGNLSGLVELMLFDNKLSGEIPRSIGELKN 190
Cdd:PLN00113   92 ----LPYIQTINLSNNQLSGPIPDDIFTTsSSLRYLNLSNNNFTGSIPR--GSIPNLETLDLSNNMLSGEIPNDIGSFSS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  191 LQVLRAGGNKnLRGELPWEIGNCENLVMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLY 270
Cdd:PLN00113  166 LKVLDLGGNV-LVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  271 QNSISGSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTI 350
Cdd:PLN00113  245 YNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  351 PEELTNCTKLTHLEIdnnlitgeipslmsnlrsltmffaWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIFGLR 430
Cdd:PLN00113  325 PVALTSLPRLQVLQL------------------------WSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSG 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  431 NLTKLLLLSNDLSGFIPPDIGNCTNLYRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLH 510
Cdd:PLN00113  381 NLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLA 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  511 TNSLSGSLLGTTLPKSLKFIDFSDNALSSTLPPGIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLLNLGENDFSGEIP 590
Cdd:PLN00113  461 RNKFFGGLPDSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIP 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  591 DELGQIPSLAiSLNLSCNRFVGEIPsrfsdlKNLGvldvshnqltgnlnvltDLQNLVSLNISYNDFSGDLPNTPFFRRL 670
Cdd:PLN00113  541 ASFSEMPVLS-QLDLSQNQLSGEIP------KNLG-----------------NVESLVQVNISHNHLHGSLPSTGAFLAI 596
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  671 PLSDLASNRGLYISNAISTRPDPTTRNSSVVRLTILILVVVTAVLVLMAVYTLV---RARAAGKQLLGEEIDSWEVTLYQ 747
Cdd:PLN00113  597 NASAVAGNIDLCGGDTTSGLPPCKRVRKTPSWWFYITCTLGAFLVLALVAFGFVfirGRNNLELKRVENEDGTWELQFFD 676
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  748 K---LDFSIDDIVKNLTSANVIGTGSSGVVYR-ITIPSGESLAVKKMwsKEESGAFNSEIKTLGSIRHRNIVRLLGWCSN 823
Cdd:PLN00113  677 SkvsKSITINDILSSLKEENVISRGKKGASYKgKSIKNGMQFVVKEI--NDVNSIPSSEIADMGKLQHPNIVKLIGLCRS 754
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  824 RNLKLLFYDYLPNGSLSSRLHGagkggcVDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLadfg 903
Cdd:PLN00113  755 EKGAYLIHEYIEGKNLSEVLRN------LSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHL---- 824
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  904 lartISGYPNT-GIDLAKPTnrppmagSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAHLVKWVR 982
Cdd:PLN00113  825 ----RLSLPGLlCTDTKCFI-------SSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADAEFGVHGSIVEWAR 893
                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  983 D-----HLaekkdpSRLLDPRLDGRTDSIMHEMLQTLAVAFLCVSNKANERPLMKDVVAML 1038
Cdd:PLN00113  894 YcysdcHL------DMWIDPSIRGDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTL 948
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
766-1041 1.25e-85

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: 277.84  E-value: 1.25e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMwsKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd14664     1 IGRGGAGTVYKGVMPNGTLVAVKRL--KGEGTQggdhgFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHG-AGKGGCVDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgYPNTGIDLA 919
Cdd:cd14664    79 ELLHSrPESQPPLDWETRQRIALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMD-DKDSHVMSS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  920 kptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD-LPGGAHLVKWVRDHLAEKKDPSrLLDPR 998
Cdd:cd14664   158 -------VAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAfLDDGVDIVDWVRGLLEEKKVEA-LVDPD 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 240256081  999 LDGrtDSIMHEMLQTLAVAFLCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd14664   230 LQG--VYKLEEVEQVFQVALLCTQSSPMERPTMREVVRMLEGD 270
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
765-1012 7.37e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 160.95  E-value: 7.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM-----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:COG0515    14 LLGRGGMGVVYLaRDLRLGRPVALKVLrpelaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGES 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHgagKGGCVDWEARYDVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgid 917
Cdd:COG0515    94 LADLLR---RRGPLPPAEALRILAQLAEALAAAHaAG----IVHRDIKPANILLTPDGRVKLIDFGIARALGG------- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  918 lAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPggahlVKWVRDHLAEKKDPSRLLDP 997
Cdd:COG0515   160 -ATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSP-----AELLRAHLREPPPPPSELRP 233
                         250
                  ....*....|....*
gi 240256081  998 RLDGRTDSIMHEMLQ 1012
Cdd:COG0515   234 DLPPALDAIVLRALA 248
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
764-970 2.16e-36

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 138.43  E-value: 2.16e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    764 NVIGTGSSGVVYRIT-IPSGESLAVKKMWSKEESG---AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:smart00220    5 EKLGEGSFGKVYLARdKKTGKLVAIKVIKKKKIKKdreRILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDL 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    840 SSRLHgagKGGCVD-WEARYdVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARtisgypntgiDL 918
Cdd:smart00220   85 FDLLK---KRGRLSeDEARF-YLRQILSALEYLHSKG---IVHRDLKPENILLDEDGHVKLADFGLAR----------QL 147
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 240256081    919 AKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:smart00220  148 DPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGD 199
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
765-1038 1.78e-32

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: 127.23  E-value: 1.78e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   765 VIGTGSSGVVYR---ITIPSGESL--AVKKMW---SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:pfam07714    6 KLGEGAFGEVYKgtlKGEGENTKIkvAVKTLKegaDEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   837 GSLSSRLHgaGKGGCVDWEARYDVVLGVAHALAYLH-HDClptiIHGDVKAMNVLLGphfEPY---LADFGLARTIsgYP 912
Cdd:pfam07714   86 GDLLDFLR--KHKRKLTLKDLLSMALQIAKGMEYLEsKNF----VHRDLAARNCLVS---ENLvvkISDFGLSRDI--YD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   913 NTGIDLAKPTNRPPMagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLdPDLPgGAHLVKWVRDHLaekkdp 991
Cdd:pfam07714  155 DDYYRKRGGGKLPIK-----WMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPY-PGMS-NEEVLEFLEDGY------ 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 240256081   992 sRLldPRLDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAML 1038
Cdd:pfam07714  222 -RL--PQPENCPDELYDLMKQ-------CWAYDPEDRPTFSELVEDL 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
859-972 7.05e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.52  E-value: 7.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  859 DVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypNTGIdlakpTNRPPMAGSYGYMAPE 937
Cdd:NF033483  111 EIMIQILSALEHAHrNG----IVHRDIKPQNILITKDGRVKVTDFGIARALS---STTM-----TQTNSVLGTVHYLSPE 178
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 240256081  938 HASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLP 972
Cdd:NF033483  179 QARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSP 213
 
Name Accession Description Interval E-value
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
32-1038 5.55e-158

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 493.98  E-value: 5.55e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   32 LLSWKSQLNISGDAFSSWHVADTSpCNWVGVKCNRRGEVSEIQLKGMDLQGSLPVTSLRslksltsltlsslnltgvipk 111
Cdd:PLN00113   34 LLSFKSSINDPLKYLSNWNSSADV-CLWQGITCNNSSRVVSIDLSGKNISGKISSAIFR--------------------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  112 eigdFTELELLDLSDNSLSGDIPVEIFRL-KKLKTLSLNTNNLEGHIPMeiGNLSGLVELMLFDNKLSGEIPRSIGELKN 190
Cdd:PLN00113   92 ----LPYIQTINLSNNQLSGPIPDDIFTTsSSLRYLNLSNNNFTGSIPR--GSIPNLETLDLSNNMLSGEIPNDIGSFSS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  191 LQVLRAGGNKnLRGELPWEIGNCENLVMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLY 270
Cdd:PLN00113  166 LKVLDLGGNV-LVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  271 QNSISGSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTI 350
Cdd:PLN00113  245 YNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  351 PEELTNCTKLTHLEIdnnlitgeipslmsnlrsltmffaWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIFGLR 430
Cdd:PLN00113  325 PVALTSLPRLQVLQL------------------------WSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSG 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  431 NLTKLLLLSNDLSGFIPPDIGNCTNLYRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLH 510
Cdd:PLN00113  381 NLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLA 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  511 TNSLSGSLLGTTLPKSLKFIDFSDNALSSTLPPGIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLLNLGENDFSGEIP 590
Cdd:PLN00113  461 RNKFFGGLPDSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIP 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  591 DELGQIPSLAiSLNLSCNRFVGEIPsrfsdlKNLGvldvshnqltgnlnvltDLQNLVSLNISYNDFSGDLPNTPFFRRL 670
Cdd:PLN00113  541 ASFSEMPVLS-QLDLSQNQLSGEIP------KNLG-----------------NVESLVQVNISHNHLHGSLPSTGAFLAI 596
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  671 PLSDLASNRGLYISNAISTRPDPTTRNSSVVRLTILILVVVTAVLVLMAVYTLV---RARAAGKQLLGEEIDSWEVTLYQ 747
Cdd:PLN00113  597 NASAVAGNIDLCGGDTTSGLPPCKRVRKTPSWWFYITCTLGAFLVLALVAFGFVfirGRNNLELKRVENEDGTWELQFFD 676
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  748 K---LDFSIDDIVKNLTSANVIGTGSSGVVYR-ITIPSGESLAVKKMwsKEESGAFNSEIKTLGSIRHRNIVRLLGWCSN 823
Cdd:PLN00113  677 SkvsKSITINDILSSLKEENVISRGKKGASYKgKSIKNGMQFVVKEI--NDVNSIPSSEIADMGKLQHPNIVKLIGLCRS 754
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  824 RNLKLLFYDYLPNGSLSSRLHGagkggcVDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLadfg 903
Cdd:PLN00113  755 EKGAYLIHEYIEGKNLSEVLRN------LSWERRRKIAIGIAKALRFLHCRCSPAVVVGNLSPEKIIIDGKDEPHL---- 824
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  904 lartISGYPNT-GIDLAKPTnrppmagSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAHLVKWVR 982
Cdd:PLN00113  825 ----RLSLPGLlCTDTKCFI-------SSAYVAPETRETKDITEKSDIYGFGLILIELLTGKSPADAEFGVHGSIVEWAR 893
                         970       980       990      1000      1010      1020
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  983 D-----HLaekkdpSRLLDPRLDGRTDSIMHEMLQTLAVAFLCVSNKANERPLMKDVVAML 1038
Cdd:PLN00113  894 YcysdcHL------DMWIDPSIRGDVSVNQNEIVEVMNLALHCTATDPTARPCANDVLKTL 948
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
766-1041 1.25e-85

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: 277.84  E-value: 1.25e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMwsKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd14664     1 IGRGGAGTVYKGVMPNGTLVAVKRL--KGEGTQggdhgFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHG-AGKGGCVDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgYPNTGIDLA 919
Cdd:cd14664    79 ELLHSrPESQPPLDWETRQRIALGSARGLAYLHHDCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMD-DKDSHVMSS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  920 kptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD-LPGGAHLVKWVRDHLAEKKDPSrLLDPR 998
Cdd:cd14664   158 -------VAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAfLDDGVDIVDWVRGLLEEKKVEA-LVDPD 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 240256081  999 LDGrtDSIMHEMLQTLAVAFLCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd14664   230 LQG--VYKLEEVEQVFQVALLCTQSSPMERPTMREVVRMLEGD 270
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
766-1041 2.69e-84

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: 274.15  E-value: 2.69e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMWS---KEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTVVAVKRLNEmncAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGKGGCVDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDLAkpt 922
Cdd:cd14066    81 LHCHKGSPPLPWPQRLKIAKGIARGLEYLHEECPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTSA--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  923 nrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD--PDLPGGAHLVKWVRDHLAEKKDpsRLLDPRLd 1000
Cdd:cd14066   158 ----VKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDenRENASRKDLVEWVESKGKEELE--DILDKRL- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 240256081 1001 GRTDSIMHE-MLQTLAVAFLCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd14066   231 VDDDGVEEEeVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
766-1034 2.50e-52

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: 185.80  E-value: 2.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGEsLAVKKMwsKEES--------GAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd14159     1 IGEGGFGCVYQAVMRNTE-YAVKRL--KEDSeldwsvvkNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLhHDCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARtISGYPNTGID 917
Cdd:cd14159    78 SLEDRLHCQVSCPCLSWSQRLHVLLGTARAIQYL-HSDSPSLIHGDVKSSNILLDAALNPKLGDFGLAR-FSRRPKQPGM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  918 LAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDlpgGAHLVKWVRDHLAEKKDPSRL--- 994
Cdd:cd14159   156 SSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVD---SCSPTKYLKDLVKEEEEAQHTptt 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  995 --------------------LDPRLdGRTDSIMHEMLQTLAVAflCVSNKANERPLMKDV 1034
Cdd:cd14159   233 mthsaeaqaaqlatsicqkhLDPQA-GPCPPELGIEISQLACR--CLHRRAKKRPPMTEV 289
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
766-1038 1.46e-51

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: 181.58  E-value: 1.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIpSGESLAVKKM----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd13999     1 IGSGSFGEVYKGKW-RGTDVAIKKLkvedDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGagKGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgidlaKP 921
Cdd:cd13999    80 LLHK--KKIPLSWSLRLKIALDIARGMNYLHS---PPIIHRDLKSLNILLDENFTVKIADFGLSRIKNS---------TT 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  922 TNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPlDPDLPGGAHLVKWVRDHLAEKKDPSrlldprldg 1001
Cdd:cd13999   146 EKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVP-FKELSPIQIAAAVVQKGLRPPIPPD--------- 215
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 240256081 1002 rtdsiMHEMLQTLAVAflCVSNKANERPLMKDVVAML 1038
Cdd:cd13999   216 -----CPPELSKLIKR--CWNEDPEKRPSFSEIVKRL 245
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
764-1041 2.53e-44

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: 162.28  E-value: 2.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIpSGESLAVKKMWS------KEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd14158    21 NKLGEGGFGVVFKGYI-NDKNVAVKKLAAmvdistEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGId 917
Cdd:cd14158   100 SLLDRLACLNDTPPLSWHMRCKIAQGTANGINYLHEN---NHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTIM- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  918 lakpTNRppMAGSYGYMAPEhASMQRITEKSDVYSYGVVLLEVLTGKHPLDpdlpggahlvkwvrdhlaEKKDPSRLLDP 997
Cdd:cd14158   176 ----TER--IVGTTAYMAPE-ALRGEITPKSDIFSFGVVLLEIITGLPPVD------------------ENRDPQLLLDI 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  998 R--LDGRTDSIM------------HEMLQTLAVAFLCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd14158   231 KeeIEDEEKTIEdyvdkkmgdwdsTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
765-1012 7.37e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 160.95  E-value: 7.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM-----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:COG0515    14 LLGRGGMGVVYLaRDLRLGRPVALKVLrpelaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVEGES 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHgagKGGCVDWEARYDVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgid 917
Cdd:COG0515    94 LADLLR---RRGPLPPAEALRILAQLAEALAAAHaAG----IVHRDIKPANILLTPDGRVKLIDFGIARALGG------- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  918 lAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPggahlVKWVRDHLAEKKDPSRLLDP 997
Cdd:COG0515   160 -ATLTQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSP-----AELLRAHLREPPPPPSELRP 233
                         250
                  ....*....|....*
gi 240256081  998 RLDGRTDSIMHEMLQ 1012
Cdd:COG0515   234 DLPPALDAIVLRALA 248
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
766-959 1.19e-36

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: 137.79  E-value: 1.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMW---SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd00180     1 LGKGSFGKVYKARdKETGKKVAVKVIPkekLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGagKGGCVDWEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypNTGIDLAKP 921
Cdd:cd00180    81 LLKE--NKGPLSEEEALSILRQLLSALEYLHSNG---IIHRDLKPENILLDSDGTVKLADFGLAKDL----DSDDSLLKT 151
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 240256081  922 TNRPPMagsYGYMAPEHASMQRITEKSDVYSYGVVLLE 959
Cdd:cd00180   152 TGGTTP---PYYAPPELLGGRYYGPKVDIWSLGVILYE 186
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
764-970 2.16e-36

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 138.43  E-value: 2.16e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    764 NVIGTGSSGVVYRIT-IPSGESLAVKKMWSKEESG---AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:smart00220    5 EKLGEGSFGKVYLARdKKTGKLVAIKVIKKKKIKKdreRILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDL 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    840 SSRLHgagKGGCVD-WEARYdVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARtisgypntgiDL 918
Cdd:smart00220   85 FDLLK---KRGRLSeDEARF-YLRQILSALEYLHSKG---IVHRDLKPENILLDEDGHVKLADFGLAR----------QL 147
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 240256081    919 AKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:smart00220  148 DPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGD 199
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
765-966 1.76e-35

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: 135.73  E-value: 1.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd06606     7 LLGKGSFGSVYLaLNLDTGELMAVKEVelsgDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLhgaGKGGCVDwEA---RY--DVVLGvahaLAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypnt 914
Cdd:cd06606    87 ASLL---KKFGKLP-EPvvrKYtrQILEG----LEYLHSNG---IVHRDIKGANILVDSDGVVKLADFGCAKRLA----- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  915 giDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06606   151 --EIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPP 200
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
765-1043 5.40e-35

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: 134.64  E-value: 5.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM-----WSKEESGAFNSEIKTLGSIRHRNIVRLL--GWCSNRnlklLFY--DYL 834
Cdd:cd14014     7 LLGRGGMGEVYRaRDTLLGRPVAIKVLrpelaEDEEFRERFLREARALARLSHPNIVRVYdvGEDDGR----PYIvmEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLhgaGKGGCVDWEARYDVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypn 913
Cdd:cd14014    83 EGGSLADLL---RERGPLPPREALRILAQIADALAAAHrAG----IVHRDIKPANILLTEDGRVKLTDFGIARAL----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  914 tgiDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDpdlpgGAHLVKWVRDHLAEKKDPSR 993
Cdd:cd14014   151 ---GDSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFD-----GDSPAAVLAKHLQEAPPPPS 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  994 LLDPRLDGRTDSIMHEMLqtlavaflcvSNKANERPlmKDVVAMLTEIRH 1043
Cdd:cd14014   223 PLNPDVPPALDAIILRAL----------AKDPEERP--QSAAELLAALRA 260
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
764-1039 1.17e-34

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: 133.43  E-value: 1.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR--ITIPSGESL--AVKKMWSKEESG---AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:cd00192     1 KKLGEGAFGEVYKgkLKGGDGKTVdvAVKTLKEDASESerkDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRL------HGAGKGGCVDWEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISG 910
Cdd:cd00192    81 GDLLDFLrksrpvFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKK---FVHRDLAARNCLVGEDLVVKISDFGLSRDIYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  911 YPNTgidlAKPTNRP-PMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLdPDLPggahlVKWVRDHLaek 988
Cdd:cd00192   158 DDYY----RKKTGGKlPIR----WMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPY-PGLS-----NEEVLEYL--- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  989 KDPSRLLDPRLdgrTDSIMHEMLQTlavaflCVSNKANERPLMKDVVAMLT 1039
Cdd:cd00192   221 RKGYRLPKPEN---CPDELYELMLS------CWQLDPEDRPTFSELVERLE 262
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
766-1041 2.78e-33

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: 129.48  E-value: 2.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGEsLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHG 845
Cdd:cd14058     1 VGRGSFGVVCKARWRNQI-VAVKIIESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVLHG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  846 AGkggcVDWEARYDVVLG----VAHALAYLHHDCLPTIIHGDVKAMNVLL-GPHFEPYLADFGLARTISgypntgidlak 920
Cdd:cd14058    80 KE----PKPIYTAAHAMSwalqCAKGVAYLHSMKPKALIHRDLKPPNLLLtNGGTVLKICDFGTACDIS----------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  921 pTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDpDLpGGAHLVKWVRDHLAEKKDPSRLLDPRLd 1000
Cdd:cd14058   145 -THMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFD-HI-GGPAFRIMWAVHNGERPPLIKNCPKPI- 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 240256081 1001 grtdsimhEMLQTlavafLCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd14058   221 --------ESLMT-----RCWSKDPEKRPSMKEIVKIMSHL 248
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
760-1038 1.41e-32

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: 127.28  E-value: 1.41e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    760 LTSANVIGTGSSGVVYR--ITIPSGESL---AVKKMwsKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL 829
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKgtLKGKGDGKEvevAVKTL--KEDASEqqieeFLREARIMRKLDHPNIVKLLGVCTEEEPLMI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    830 FYDYLPNGSLSSRLHgAGKGGCVDWEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTIS 909
Cdd:smart00221   79 VMEYMPGGDLLDYLR-KNRPKELSLSDLLSFALQIARGMEYLESKN---FIHRDLAARNCLVGENLVVKISDFGLSRDLY 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    910 GYpntGIDLAKPTNRPpmagsYGYMAPEhASMQRI-TEKSDVYSYGVVLLEVLT-GKHPLdPDLPgGAHLVKWVrdhlae 987
Cdd:smart00221  155 DD---DYYKVKGGKLP-----IRWMAPE-SLKEGKfTSKSDVWSFGVLLWEIFTlGEEPY-PGMS-NAEVLEYL------ 217
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 240256081    988 kKDPSRLldPRLDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAML 1038
Cdd:smart00221  218 -KKGYRL--PKPPNCPPELYKLMLQ-------CWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
765-1038 1.78e-32

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: 127.23  E-value: 1.78e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   765 VIGTGSSGVVYR---ITIPSGESL--AVKKMW---SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:pfam07714    6 KLGEGAFGEVYKgtlKGEGENTKIkvAVKTLKegaDEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   837 GSLSSRLHgaGKGGCVDWEARYDVVLGVAHALAYLH-HDClptiIHGDVKAMNVLLGphfEPY---LADFGLARTIsgYP 912
Cdd:pfam07714   86 GDLLDFLR--KHKRKLTLKDLLSMALQIAKGMEYLEsKNF----VHRDLAARNCLVS---ENLvvkISDFGLSRDI--YD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   913 NTGIDLAKPTNRPPMagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLdPDLPgGAHLVKWVRDHLaekkdp 991
Cdd:pfam07714  155 DDYYRKRGGGKLPIK-----WMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPY-PGMS-NEEVLEFLEDGY------ 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 240256081   992 sRLldPRLDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAML 1038
Cdd:pfam07714  222 -RL--PQPENCPDELYDLMKQ-------CWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
760-1038 2.79e-32

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 126.49  E-value: 2.79e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    760 LTSANVIGTGSSGVVYR-----ITIPSGESLAVKKMwsKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL 829
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKgklkgKGGKKKVEVAVKTL--KEDASEqqieeFLREARIMRKLDHPNVVKLLGVCTEEEPLYI 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    830 FYDYLPNGSLSSRLHgaGKGGCVDWEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTIS 909
Cdd:smart00219   79 VMEYMEGGDLLSYLR--KNRPKLSLSDLLSFALQIARGMEYLESKN---FIHRDLAARNCLVGENLVVKISDFGLSRDLY 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081    910 GYpntGIDLAKPTNRPpmagsYGYMAPEhASMQRI-TEKSDVYSYGVVLLEVLT-GKHPLdPDLPgGAHLVKWVrdhlae 987
Cdd:smart00219  154 DD---DYYRKRGGKLP-----IRWMAPE-SLKEGKfTSKSDVWSFGVLLWEIFTlGEQPY-PGMS-NEEVLEYL------ 216
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 240256081    988 kKDPSRLldPRLDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAML 1038
Cdd:smart00219  217 -KNGYRL--PQPPNCPPELYDLMLQ-------CWAEDPEDRPTFSELVEIL 257
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
264-664 2.24e-31

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 128.13  E-value: 2.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  264 LQNLYLYQNSISGSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNcpELWLIDFSENLLTGTIPRSFGKLENLQELQLSV 343
Cdd:COG4886    28 LLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLL--LLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  344 NqisgtipEELTNCTKLTHLEIDNNLITgEIPSLMSNLRSLTMFFAWQNKLTgNIPQSLSQCRELQAIDLSYNSLSGsip 423
Cdd:COG4886   106 N-------EELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DLPEPLGNLTNLKSLDLSNNQLTD--- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  424 keifglrnltkllllsndlsgfIPPDIGNCTNLYRLRLNGNRLAgSIPSEIGNLKNLNFVDISENRLvGSIPPAISGCES 503
Cdd:COG4886   174 ----------------------LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQL-TDLPEPLANLTN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  504 LEFLDLHTNSLsgsllgTTLP-----KSLKFIDFSDNALSStLPPgIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLL 578
Cdd:COG4886   230 LETLDLSNNQL------TDLPelgnlTNLEELDLSNNQLTD-LPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  579 NLGENDFSGEIPDELGQIPSLAISLNLSCNRFVGEIPSRFSDLKNLGVLDVSHNQLTGNLNVLTDLQNLVSLNISYNDFS 658
Cdd:COG4886   302 LLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLT 381

                  ....*.
gi 240256081  659 GDLPNT 664
Cdd:COG4886   382 LALLLL 387
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
117-491 1.47e-30

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 125.82  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  117 TELELLDLSDNSLSGDIPVEIFRLKKLKTLSLNTNNleghipmEIGNLSGLVELMLFDNKLSgEIPRSIGELKNLQVLRA 196
Cdd:COG4886    72 LLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  197 GGNkNLRgELPWEIGNCENLVMLGLAETSLSGklpasignlkrvqtiaiytsllsgpIPDEIGYCTELQNLYLYQNSISg 276
Cdd:COG4886   144 SNN-QLT-DLPEPLGNLTNLKSLDLSNNQLTD-------------------------LPEELGNLTNLKELDLSNNQIT- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  277 SIPTTIGGLKKLQSLLLWQNNLvGKIPTELGNCPELWLIDFSENLLTgTIPrSFGKLENLQELQLSVNQISgTIPEELtN 356
Cdd:COG4886   196 DLPEPLGNLTNLEELDLSGNQL-TDLPEPLANLTNLETLDLSNNQLT-DLP-ELGNLTNLEELDLSNNQLT-DLPPLA-N 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  357 CTKLTHLEIDNNLITGEIPSLMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIFGLRNLTKLL 436
Cdd:COG4886   271 LTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALL 350
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  437 LLSNDLSGFIPPDIGNCTNLYRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLV 491
Cdd:COG4886   351 TLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTL 405
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
116-527 2.06e-30

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 125.43  E-value: 2.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  116 FTELELLDLSDNSLSGDIPVEIFRLKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGeiPRSIGELKNLQVLR 195
Cdd:COG4886    25 ILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLG--LTDLGDLTNLTELD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  196 AGGNKnlrgelpwEIGNCENLVMLGLAETSLSGklpasignlkrvqtiaiytsllsgpIPDEIGYCTELQNLYLYQNSIS 275
Cdd:COG4886   103 LSGNE--------ELSNLTNLESLDLSGNQLTD-------------------------LPEELANLTNLKELDLSNNQLT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  276 gSIPTTIGGLKKLQSLLLWQNNLVGkIPTELGNCPELWLIDFSENLLTgTIPRSFGKLENLQELQLSVNQISgTIPEELT 355
Cdd:COG4886   150 -DLPEPLGNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  356 NCTKLTHLEIDNNLITgEIPSLmSNLRSLTMFFAWQNKLTgNIPqSLSQCRELQAIDLSYNSLSGSIPKEIFGLRNLTKL 435
Cdd:COG4886   226 NLTNLETLDLSNNQLT-DLPEL-GNLTNLEELDLSNNQLT-DLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  436 LLLSNDLSGFIPPDIGNCTNLYRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLS 515
Cdd:COG4886   302 LLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLT 381
                         410
                  ....*....|..
gi 240256081  516 GSLLGTTLPKSL 527
Cdd:COG4886   382 LALLLLTLLLLL 393
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
766-1034 5.40e-30

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: 120.25  E-value: 5.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPS-GESLAVKKMWS----KEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd13978     1 LGSGGFGTVSKARHVSwFGMVAIKCLHSspncIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGagKGGCVDWEARYDVVLGVAHALAYLHHdCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTisGYPNTGIDLAK 920
Cdd:cd13978    81 SLLER--EIQDVPWSLRFRIIHEIALGMNFLHN-MDPPLLHHDLKPENILLDNHFHVKISDFGLSKL--GMKSISANRRR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  921 PTnrPPMAGSYGYMAPEHASM--QRITEKSDVYSYGVVLLEVLTGKHPLdPDLPGGAH-LVKWVRDHLAEKKDPSRLLDP 997
Cdd:cd13978   156 GT--ENLGGTPIYMAPEAFDDfnKKPTSKSDVYSFAIVIWAVLTRKEPF-ENAINPLLiMQIVSKGDRPSLDDIGRLKQI 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 240256081  998 RLDGRTDSIMHEmlqtlavaflCVSNKANERPLMKDV 1034
Cdd:cd13978   233 ENVQELISLMIR----------CWDGNPDARPTFLEC 259
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
346-663 6.28e-29

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 120.81  E-value: 6.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  346 ISGTIPEELTNCTKLTHLEIDNNLITGEIPSLMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKE 425
Cdd:COG4886     7 SLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  426 IFGLRNLTKLLLLSNDLSGfiPPDIGNCTNLYRLRLNGNRLAgSIPSEIGNLKNLNFVDISENRLvGSIPPAISGCESLE 505
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSG--NEELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQL-TDLPEPLGNLTNLK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  506 FLDLHTNSLsgsllgTTLP------KSLKFIDFSDNALSStLPPGIGLLTELTKLNLAKNRLSgEIPREISTCRSLQLLN 579
Cdd:COG4886   163 SLDLSNNQL------TDLPeelgnlTNLKELDLSNNQITD-LPEPLGNLTNLEELDLSGNQLT-DLPEPLANLTNLETLD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  580 LGENDFSgEIPdELGQIPSLAiSLNLSCNRfVGEIPSrFSDLKNLGVLDVSHNQLTG-NLNVLTDLQNLVSLNISYNDFS 658
Cdd:COG4886   235 LSNNQLT-DLP-ELGNLTNLE-ELDLSNNQ-LTDLPP-LANLTNLKTLDLSNNQLTDlKLKELELLLGLNSLLLLLLLLN 309

                  ....*
gi 240256081  659 GDLPN 663
Cdd:COG4886   310 LLELL 314
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
766-1038 2.17e-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: 115.75  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIpSGESLAVK------KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd14160     1 IGEGEIFEVYRVRI-GNRSYAVKlfkqekKMQWKKHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDLA 919
Cdd:cd14160    80 FDRLQCHGVTKPLSWHERINILIGIAKAIHYLHNSQPCTVICGNISSANILLDDQMQPKLTDFALAHFRPHLEDQSCTIN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  920 KPTNrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDlPGGAHLVKWVRDHLAEKKDPS--RLLDP 997
Cdd:cd14160   160 MTTA---LHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCKVVLDD-PKHLQLRDLLHELMEKRGLDSclSFLDL 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 240256081  998 RLDGRTDSImheMLQTLAVAFLCVSNKANERPLMKDVVAML 1038
Cdd:cd14160   236 KFPPCPRNF---SAKLFRLAGRCTATKAKLRPDMDEVLQRL 273
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
366-659 3.07e-28

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 118.88  E-value: 3.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  366 DNNLITGEIPSLMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPK-----EIFGLRNLTKLLLLSN 440
Cdd:COG4886     3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLlssllLLLSLLLLLLLSLLLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  441 DLSGFIPPDIGNCTNLYRLRLNGNRlagsipsEIGNLKNLNFVDISENRLVgSIPPAISGCESLEFLDLHTNSLsgsllg 520
Cdd:COG4886    83 SLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQL------ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  521 TTLP------KSLKFIDFSDNALSStLPPGIGLLTELTKLNLAKNRLSgEIPREISTCRSLQLLNLGENDFSgEIPDELG 594
Cdd:COG4886   149 TDLPeplgnlTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLA 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  595 QIPSLaISLNLSCNRFVgEIPSrFSDLKNLGVLDVSHNQLTgNLNVLTDLQNLVSLNISYNDFSG 659
Cdd:COG4886   226 NLTNL-ETLDLSNNQLT-DLPE-LGNLTNLEELDLSNNQLT-DLPPLANLTNLKTLDLSNNQLTD 286
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
143-555 5.71e-28

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 118.11  E-value: 5.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  143 LKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGEIPRSIGELKNLQVLRAGGNKNLRGELPWEIGNCENLVMLGLA 222
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  223 ETSLSGKLPASIGNLKRVQTIAIYtsllsgpIPDEIGYCTELQNLYLYQNSISgSIPTTIGGLKKLQSLLLWQNNLvGKI 302
Cdd:COG4886    81 LLSLLLLGLTDLGDLTNLTELDLS-------GNEELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQL-TDL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  303 PTELGNCPELWLIDFSENLLTgTIPRSFGKLENLQELQLSVNQISgTIPEELTNCTKLTHLEIDNNLITgEIPSLMSNLR 382
Cdd:COG4886   152 PEPLGNLTNLKSLDLSNNQLT-DLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANLT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  383 SLTMFFAWQNKLTgNIPqSLSQCRELQAIDLSYNSLSgSIPKEiFGLRNLTKLLLLSNDLSGFIPPDIGNCTNLYRLRLN 462
Cdd:COG4886   229 NLETLDLSNNQLT-DLP-ELGNLTNLEELDLSNNQLT-DLPPL-ANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLL 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  463 GNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLSGSLLGTTLPKSLKFIDFSDNALSSTLP 542
Cdd:COG4886   305 LLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLAL 384
                         410
                  ....*....|...
gi 240256081  543 PGIGLLTELTKLN 555
Cdd:COG4886   385 LLLTLLLLLLTTT 397
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
765-967 1.45e-26

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: 109.99  E-value: 1.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKMW--SKEESGAFNSEIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYLPNGSLS 840
Cdd:cd05122     7 KIGKGGFGVVYKaRHKKTGQIVAIKKINleSKEKKESILNEIAILKKCKHPNIVKYYGsYLKKDELWIVM-EFCSGGSLK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAGKGGCvDWEARYdVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLArtisgypntgIDLA 919
Cdd:cd05122    86 DLLKNTNKTLT-EQQIAY-VCKEVLKGLEYLHsHG----IIHRDIKAANILLTSDGEVKLIDFGLS----------AQLS 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  920 KPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05122   150 DGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPY 197
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
765-966 2.67e-26

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: 109.41  E-value: 2.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRiTIPSGESLAVKKMWSKEESGA------FNSEIKTLGSIRHRNIVRLLGWCSNR-NLKLLFyDYLPNG 837
Cdd:cd14061     1 VIGVGGFGKVYR-GIWRGEEVAVKAARQDPDEDIsvtlenVRQEARLFWMLRHPNIIALRGVCLQPpNLCLVM-EYARGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAG--KGGCVDWEARydvvlgVAHALAYLHHDCLPTIIHGDVKAMNVLLgphFEPY-----------LADFGL 904
Cdd:cd14061    79 ALNRVLAGRKipPHVLVDWAIQ------IARGMNYLHNEAPVPIIHRDLKSSNILI---LEAIenedlenktlkITDFGL 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  905 ARtisgypntgiDLAKpTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14061   150 AR----------EWHK-TTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVP 200
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
766-969 4.16e-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: 108.47  E-value: 4.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKM----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd06627     8 IGRGAFGSVYKgLNLNTGEFVAIKQIslekIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAGKGGcvdwE---ARYdvVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgiD 917
Cdd:cd06627    88 SIIKKFGKFP----EslvAVY--IYQVLEGLAYLHEQ---GVIHRDIKGANILTTKDGLVKLADFGVATKLN-------E 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  918 LAKPTNRPpmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP---LDP 969
Cdd:cd06627   152 VEKDENSV--VGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPyydLQP 204
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
764-966 4.16e-26

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: 109.01  E-value: 4.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIpSGESLAVKKMWSKEESGA----FNSEIKTLgSIRHRNIVRLLGW---CSNRNLKLLFYDYLPN 836
Cdd:cd13979     9 EPLGSGGFGSVYKATY-KGETVAVKIVRRRRKNRAsrqsFWAELNAA-RLRHENIVRVLAAetgTDFASLGLIIMEYCGN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGgcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYpntgi 916
Cdd:cd13979    87 GTLQQLIYEGSEP--LPLAHRILISLDIARALRFCHSH---GIVHLDVKPANILISEQGVCKLCDFGCSVKLGEG----- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  917 dLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd13979   157 -NEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELP 205
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
109-390 1.06e-25

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 111.18  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  109 IPKEIGDFTELELLDLSDNSLSgDIPVEIFRLKKLKTLSLNTNNLEGhIPMEIGNLSGLVELMLFDNKLSgEIPRSIGEL 188
Cdd:COG4886   128 LPEELANLTNLKELDLSNNQLT-DLPEPLGNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNL 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  189 KNLQVLRAGGNKnLRgELPWEIGNCENLVMLGLAETSLSgKLPaSIGNLKRVQTIAIYTSLLSGpIPDEiGYCTELQNLY 268
Cdd:COG4886   205 TNLEELDLSGNQ-LT-DLPEPLANLTNLETLDLSNNQLT-DLP-ELGNLTNLEELDLSNNQLTD-LPPL-ANLTNLKTLD 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  269 LYQNSISGSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISG 348
Cdd:COG4886   279 LSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNL 358
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 240256081  349 TIPEELTNCTKLTHLEIDNNLITGEIPSLMSNLRSLTMFFAW 390
Cdd:COG4886   359 LSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGV 400
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
764-968 7.97e-24

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: 102.17  E-value: 7.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRIT-IPSGESLAVK-----KMWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd05117     6 KVLGRGSFGVVRLAVhKKTGEEYAVKiidkkKLKSEDEEMLRR-EIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHgagKGGCVD-WEARyDVVLGVAHALAYLHHDClptIIHGDVKAMNVLL---GPHFEPYLADFGLARTIsgypN 913
Cdd:cd05117    85 ELFDRIV---KKGSFSeREAA-KIMKQILSAVAYLHSQG---IVHRDLKPENILLaskDPDSPIKIIDFGLAKIF----E 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  914 TGIDLAKptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd05117   154 EGEKLKT------VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFY 202
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
766-966 1.20e-23

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


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 101.03  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIpSGESLAVKKMwsKEESgafNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHG 845
Cdd:cd14059     1 LGSGAQGAVFLGKF-RGEEVAVKKV--RDEK---ETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  846 AGK---GGCVDWearydvVLGVAHALAYLHhdcLPTIIHGDVKAMNVLLGPHFEPYLADFGLARtisgypntgiDLAKPT 922
Cdd:cd14059    75 GREitpSLLVDW------SKQIASGMNYLH---LHKIIHRDLKSPNVLVTYNDVLKISDFGTSK----------ELSEKS 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 240256081  923 NRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14059   136 TKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIP 179
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
765-974 2.45e-23

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 100.74  E-value: 2.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESG---AFNSEIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYLPNGSL 839
Cdd:cd06623     8 VLGQGSSGVVYKvRHKPTGKIYALKKIHVDGDEEfrkQLLRELKTLRSCESPYVVKCYGaFYKEGEISIVL-EYMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLhgaGKGGCVDwearyDVVLG-----VAHALAYLHHDclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypNT 914
Cdd:cd06623    87 ADLL---KKVGKIP-----EPVLAyiarqILKGLDYLHTK--RHIIHRDIKPSNLLINSKGEVKIADFGISKVLE---NT 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  915 GidlakpTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGG 974
Cdd:cd06623   154 L------DQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPS 207
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
766-972 4.25e-23

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: 99.87  E-value: 4.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLH 844
Cdd:cd14065     1 LGKGFFGEVYKVThRETGKVMVMKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 GAGKGGCvdWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL---GPHFEPYLADFGLARTISGYPNTGIDLAKP 921
Cdd:cd14065    81 SMDEQLP--WSQRVSLAKDIASGMAYLHSK---NIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKTKKPDRKKR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  922 TNrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLtGKHPLDPD-LP 972
Cdd:cd14065   156 LT---VVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII-GRVPADPDyLP 203
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
765-971 4.41e-23

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: 100.30  E-value: 4.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVY-RITIPSGESLAVKKMWSKEESG-----------AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYD 832
Cdd:cd06628     7 LIGSGSFGSVYlGMNASSGELMAVKQVELPSVSAenkdrkksmldALQREIALLRELQHENIVQYLGSSSDANHLNIFLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  833 YLPNGSLSSRL--HGAGKGGCVDwearyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISG 910
Cdd:cd06628    87 YVPGGSVATLLnnYGAFEESLVR-----NFVRQILKGLNYLHNR---GIIHRDIKGANILVDNKGGIKISDFGISKKLEA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  911 ypnTGIDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLdPDL 971
Cdd:cd06628   159 ---NSLSTKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF-PDC 215
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
799-968 5.58e-23

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: 100.30  E-value: 5.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  799 FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpT 878
Cdd:cd14157    39 FQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQDRLQQQGGSHPLPWEQRLSISLGLLKAVQHLHNF---G 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHFEPYLADFGLaRTISGYPNTGIDLAKPTNrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLL 958
Cdd:cd14157   116 ILHGNIKSSNVLLDGNLLPKLGHSGL-RLCPVDKKSVYTMMKTKV---LQISLAYLPEDFVRHGQLTEKVDIFSCGVVLA 191
                         170
                  ....*....|
gi 240256081  959 EVLTGKHPLD 968
Cdd:cd14157   192 EILTGIKAMD 201
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
405-685 2.07e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.16  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  405 CRELQAIDLSYNSLSGSIPKEIFGLRNLTKLLLLSNDLSGFIPPDIGNCTNLYRLRLNGNRLAGSIPSEIGNLKNLNFVD 484
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  485 ISENRLVGsiPPAISGCESLEFLDLHTNSLSGSLlgttlpKSLKFIDFSDNALSStLPPGIGLLTELTKLNLAKNRLSgE 564
Cdd:COG4886    81 LLSLLLLG--LTDLGDLTNLTELDLSGNEELSNL------TNLESLDLSGNQLTD-LPEELANLTNLKELDLSNNQLT-D 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  565 IPREISTCRSLQLLNLGENDFSgEIPDELGQIPSLaISLNLSCNRfVGEIPSRFSDLKNLGVLDVSHNQLTGNLNVLTDL 644
Cdd:COG4886   151 LPEPLGNLTNLKSLDLSNNQLT-DLPEELGNLTNL-KELDLSNNQ-ITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANL 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 240256081  645 QNLVSLNISYNDFSgDLPNtpffrrlpLSDLASNRGLYISN 685
Cdd:COG4886   228 TNLETLDLSNNQLT-DLPE--------LGNLTNLEELDLSN 259
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
765-966 3.54e-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: 97.36  E-value: 3.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRiTIPSGESLAVKKM-WSKEESGAFNSE-----IKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd14148     1 IIGVGGFGKVYK-GLWRGEEVAVKAArQDPDEDIAVTAEnvrqeARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLhgAGKGG----CVDWEARydvvlgVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPY--------LADFGLAR 906
Cdd:cd14148    80 LNRAL--AGKKVpphvLVNWAVQ------IARGMNYLHNEAIVPIIHRDLKSSNILILEPIENDdlsgktlkITDFGLAR 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  907 TisgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14148   152 E-----------WHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVP 200
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
109-386 4.63e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.39  E-value: 4.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  109 IPKEIGDFTELELLDLSDNSLSgDIPVEIFRLKKLKTLSLNTNNLEgHIPMEIGNLSGLVELMLFDNKLSgEIPRSIGEL 188
Cdd:COG4886   151 LPEPLGNLTNLKSLDLSNNQLT-DLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLANL 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  189 KNLQVLRAGGNKNlrGELPWeIGNCENLVMLGLAETSLSGkLPASiGNLKRVQTIAIYTSLLSGpipdeigycTELQNLY 268
Cdd:COG4886   228 TNLETLDLSNNQL--TDLPE-LGNLTNLEELDLSNNQLTD-LPPL-ANLTNLKTLDLSNNQLTD---------LKLKELE 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  269 LYQNSISGSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISG 348
Cdd:COG4886   294 LLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLG 373
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 240256081  349 TIPEELTNCTKLTHLEIDNNLITGEIPSLMSNLRSLTM 386
Cdd:COG4886   374 LLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAV 411
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
761-967 7.24e-22

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: 96.74  E-value: 7.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  761 TSANVIGTGSSGVVYRITIPSGESLAVK--------KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYD 832
Cdd:cd06631     4 KKGNVLGKGAYGTVYCGLTSTGQLIAVKqveldtsdKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  833 YLPNGSLSSRLhgaGKGGCVDWEA--RY--DVVLGVahalAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLAR-- 906
Cdd:cd06631    84 FVPGGSIASIL---ARFGALEEPVfcRYtkQILEGV----AYLHNNN---VIHRDIKGNNIMLMPNGVIKLIDFGCAKrl 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  907 TISGYPNTGIDLAKptnrpPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06631   154 CINLSSGSQSQLLK-----SMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPW 209
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
802-1041 9.15e-22

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: 96.31  E-value: 9.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEARYDVVLGVAHALAYLHHDclPTIIH 881
Cdd:cd13992    46 ELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVL--LNREIKMDWMFKSSFIKDIVKGMNYLHSS--SIGYH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  882 GDVKAMNVLLGPHFEPYLADFGLARTISGypntgiDLAKPTNRPPMAGSYGYMAPEH----ASMQRITEKSDVYSYGVVL 957
Cdd:cd13992   122 GRLKSSNCLVDSRWVVKLTDFGLRNLLEE------QTNHQLDEDAQHKKLLWTAPELlrgsLLEVRGTQKGDVYSFAIIL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  958 LEVLTGKHPLDPDLPggahlVKWVRDHLAEKKDPSRlldPRLDGRTDSImHEMLQTLAVAflCVSNKANERPLMKDVVAM 1037
Cdd:cd13992   196 YEILFRSDPFALERE-----VAIVEKVISGGNKPFR---PELAVLLDEF-PPRLVLLVKQ--CWAENPEKRPSFKQIKKT 264

                  ....
gi 240256081 1038 LTEI 1041
Cdd:cd13992   265 LTEN 268
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
802-968 1.14e-21

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: 96.53  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLhHDCLPTIIH 881
Cdd:cd14026    47 EAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSLNELLHEKDIYPDVAWPLRLRILYEIALGVNYL-HNMSPPLLH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  882 GDVKAMNVLLGPHFEPYLADFGLA--RTISgypntgIDLAKPTNRPPMAGSYGYMAPEH---ASMQRITEKSDVYSYGVV 956
Cdd:cd14026   126 HDLKTQNILLDGEFHVKIADFGLSkwRQLS------ISQSRSSKSAPEGGTIIYMPPEEyepSQKRRASVKHDIYSYAII 199
                         170
                  ....*....|..
gi 240256081  957 LLEVLTGKHPLD 968
Cdd:cd14026   200 MWEVLSRKIPFE 211
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
767-1038 1.36e-21

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: 95.02  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  767 GTGSSGVVYR-ITIPSGESLAVKKMWSKEEsgafnsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHG 845
Cdd:cd14060     2 GGGSFGSVYRaIWVSQDKEVAVKKLLKIEK------EAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLNS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  846 AGKGgcvdwEARYDVVLG----VAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgidlakP 921
Cdd:cd14060    76 NESE-----EMDMDQIMTwatdIAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHS-----------H 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  922 TNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDpDLPGGAhlVKWVrdhLAEKKDpsRLLDPR-LD 1000
Cdd:cd14060   140 TTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFK-GLEGLQ--VAWL---VVEKNE--RPTIPSsCP 211
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 240256081 1001 GRTDSIMHEmlqtlavaflCVSNKANERPLMKDVVAML 1038
Cdd:cd14060   212 RSFAELMRR----------CWEADVKERPSFKQIIGIL 239
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
750-970 4.34e-21

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: 94.08  E-value: 4.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  750 DFsidDIVKNLtsanviGTGSSGVVYR-ITIPSGESLAVKKMwSKEE------SGAFNSEIKTLGSIRHRNIVRLLGWcs 822
Cdd:cd14007     1 DF---EIGKPL------GKGKFGNVYLaREKKSGFIVALKVI-SKSQlqksglEHQLRREIEIQSHLRHPNILRLYGY-- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  823 nrnlkllFYD---------YLPNGSLSSRLHGAGKGGcvDWEA-RYdvVLGVAHALAYLHHDClptIIHGDVKAMNVLLG 892
Cdd:cd14007    69 -------FEDkkriylileYAPNGELYKELKKQKRFD--EKEAaKY--IYQLALALDYLHSKN---IIHRDIKPENILLG 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  893 PHFEPYLADFGL-ARTISGYPNTgidlakptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14007   135 SNGELKLADFGWsVHAPSNRRKT------------FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESK 201
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
766-966 5.34e-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: 93.61  E-value: 5.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRitipsGE---SLAVKKMW----SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLfYDYLPNGS 838
Cdd:cd14062     1 IGSGSFGTVYK-----GRwhgDVAVKKLNvtdpTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIV-TQWCEGSS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHgagkggcVDwEARYDVVL------GVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLArTISGYP 912
Cdd:cd14062    75 LYKHLH-------VL-ETKFEMLQlidiarQTAQGMDYLHAK---NIIHRDLKSNNIFLHEDLTVKIGDFGLA-TVKTRW 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  913 NTGIDLAKPTnrppmaGSYGYMAPEHASMQRI---TEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14062   143 SGSQQFEQPT------GSILWMAPEVIRMQDEnpySFQSDVYAFGIVLYELLTGQLP 193
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
766-977 6.24e-21

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: 93.36  E-value: 6.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIpSGESLAVKK-----MWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKL-LFYDYLPNGSL 839
Cdd:cd14064     1 IGSGSFGKVYKGRC-RNKIVAIKRyrantYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFaIVTQYVSGGSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHGAGKggCVDWEARYDVVLGVAHALAYLHHDCLPtIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgIDLA 919
Cdd:cd14064    80 FSLLHEQKR--VIDLQSKLIIAVDVAKGMEYLHNLTQP-IIHRDLNSHNILLYEDGHAVVADFGESRFLQS-----LDED 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  920 KPTNRPpmaGSYGYMAPEHASM-QRITEKSDVYSYGVVLLEVLTGKHPLdpdlpggAHL 977
Cdd:cd14064   152 NMTKQP---GNLRWMAPEVFTQcTRYSIKADVFSYALCLWELLTGEIPF-------AHL 200
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
765-961 7.60e-21

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 93.90  E-value: 7.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVY----RITipsGESLAVKKMWSKEESGAFN---SEIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYLPN 836
Cdd:cd13996    13 LLGSGGFGSVYkvrnKVD---GVTYAIKKIRLTEKSSASEkvlREVKALAKLNHPNIVRYYTaWVEEPPLYIQM-ELCEG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLL-GPHFEPYLADFGLARTISGYPNTG 915
Cdd:cd13996    89 GTLRDWIDRRNSSSKNDRKLALELFKQILKGVSYIHSKG---IVHRDLKPSNIFLdNDDLQVKIGDFGLATSIGNQKREL 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  916 IDLAKPTNR-----PPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVL 961
Cdd:cd13996   166 NNLNNNNNGntsnnSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
765-966 8.63e-21

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: 93.56  E-value: 8.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIpSGESLAVKKMWSKEESGA------FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd14146     1 IIGVGGFGKVYRATW-KGQEVAVKAARQDPDEDIkataesVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGAGKGGC------------VDWEARydvvlgVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEP--------Y 898
Cdd:cd14146    80 LNRALAAANAAPGprrarripphilVNWAVQ------IARGMLYLHEEAVVPILHRDLKSSNILLLEKIEHddicnktlK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  899 LADFGLARTisgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14146   154 ITDFGLARE-----------WHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVP 210
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
764-982 1.26e-20

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: 92.86  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIPS-GESLAVK-----KMWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd08529     6 NKLGKGSFGVVYKVVRKVdGRVYALKqidisRMSRKMREEAID-EARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYAENG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHgAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgyPNTgiD 917
Cdd:cd08529    85 DLHSLIK-SQRGRPLPEDQIWKFFIQTLLGLSHLHSK---KILHRDIKSMNIFLDKGDNVKIGDLGVAKILS--DTT--N 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  918 LAKPtnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDlPGGAHLVKWVR 982
Cdd:cd08529   157 FAQT-----IVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQ-NQGALILKIVR 215
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
764-967 2.29e-20

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: 92.04  E-value: 2.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR-ITIPSGESLAVKKMwSKEESGAF----NSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd06610     7 EVIGSGATAVVYAaYCLPKKEKVAIKRI-DLEKCQTSmdelRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGAGKGGCVDwEARYDVVL-GVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGlartISGYPNTGID 917
Cdd:cd06610    86 LLDIMKSSYPRGGLD-EAIIATVLkEVLKGLEYLHSNGQ---IHRDVKAGNILLGEDGSVKIADFG----VSASLATGGD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  918 LAKPTnRPPMAGSYGYMAPEHASMQR-ITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06610   158 RTRKV-RKTFVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIELATGAAPY 207
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
748-967 2.73e-20

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 92.03  E-value: 2.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  748 KLDFSiddivkNLTSANVIGTGSSGVVYRiTIPSGESLAVKKMWSKEESG------AFNSEIKTLGSIRHRNIVRLLGWC 821
Cdd:cd14145     2 EIDFS------ELVLEEIIGIGGFGKVYR-AIWIGDEVAVKAARHDPDEDisqtieNVRQEAKLFAMLKHPNIIALRGVC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  822 SNRNLKLLFYDYLPNGSLSSRLHGAG--KGGCVDWEARydvvlgVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEP-- 897
Cdd:cd14145    75 LKEPNLCLVMEFARGGPLNRVLSGKRipPDILVNWAVQ------IARGMNYLHCEAIVPVIHRDLKSSNILILEKVENgd 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  898 ------YLADFGLARTisgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14145   149 lsnkilKITDFGLARE-----------WHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
765-960 3.37e-20

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: 92.12  E-value: 3.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIpSGESLAVKKMWSKEESGAFN-SEIKTLGSIRHRNIVRLL-GWCSNRNLK---LLFYDYLPNGSL 839
Cdd:cd13998     2 VIGKGRFGEVWKASL-KNEPVAVKIFSSRDKQSWFReKEIYRTPMLKHENILQFIaADERDTALRtelWLVTAFHPNGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDCL------PTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPN 913
Cdd:cd13998    81 *DYL----SLHTIDWVSLCRLALSVARGLAHLHSEIPgctqgkPAIAHRDLKSKNILVKNDGTCCIADFGLAVRLSPSTG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  914 TGiDLAKptnrPPMAGSYGYMAPE------HASMQRITEKSDVYSYGVVLLEV 960
Cdd:cd13998   157 EE-DNAN----NGQVGTKRYMAPEvlegaiNLRDFESFKRVDIYAMGLVLWEM 204
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
764-962 9.23e-20

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: 91.27  E-value: 9.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIpSGESLAVKkMWSKEESGAFNSE--IKTLGSIRHRNIVRLLGWCSNRNLK-----LLFYDYLPN 836
Cdd:cd14054     1 QLIGQGRYGTVWKGSL-DERPVAVK-VFPARHRQNFQNEkdIYELPLMEHSNILRFIGADERPTADgrmeyLLVLEYAPK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGagkgGCVDWEARYDVVLGVAHALAYLHHDCL------PTIIHGDVKAMNVLLGPHFEPYLADFGLARTISG 910
Cdd:cd14054    79 GSLCSYLRE----NTLDWMSSCRMALSLTRGLAYLHTDLRrgdqykPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  911 --YPNTGIDLAKPTNrPPMAGSYGYMAPE-----------HASMQRIteksDVYSYGVVLLEVLT 962
Cdd:cd14054   155 ssLVRGRPGAAENAS-ISEVGTLRYMAPEvlegavnlrdcESALKQV----DVYALGLVLWEIAM 214
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
766-966 1.87e-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: 89.69  E-value: 1.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMW--SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLfYDYLPNGSLSSRL 843
Cdd:cd14150     8 IGTGSFGTVFRGKWHGDVAVKILKVTepTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAII-TQWCEGSSLYRHL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  844 HGAGKGgcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNtgidlAKPTN 923
Cdd:cd14150    87 HVTETR--FDTMQLIDVARQTAQGMDYLHAK---NIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSG-----SQQVE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 240256081  924 RPpmAGSYGYMAPEHASMQR---ITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14150   157 QP--SGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLP 200
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
764-966 2.13e-19

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: 89.28  E-value: 2.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR-ITIPSGESLAVKKM-WSKEESGAFNS---EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd06626     6 NKIGEGTFGKVYTaVNLDTGELMAMKEIrFQDNDPKTIKEiadEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLhgagKGGCVDWEA---RYDVVLGVahALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgyPNTg 915
Cdd:cd06626    86 LEELL----RHGRILDEAvirVYTLQLLE--GLAYLHEN---GIVHRDIKPANIFLDSNGLIKLGDFGSAVKLK--NNT- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  916 iDLAKPTNRPPMAGSYGYMAPEHASMQRITEK---SDVYSYGVVLLEVLTGKHP 966
Cdd:cd06626   154 -TTMAPGEVNSLVGTPAYMAPEVITGNKGEGHgraADIWSLGCVVLEMATGKRP 206
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
766-1041 2.63e-19

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 88.69  E-value: 2.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL----S 840
Cdd:cd14155     1 IGSGFFSEVYKVRhRTSGQVMALKMNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLeqllD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHgagkggcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL---GPHFEPYLADFGLARTISGYPNTGID 917
Cdd:cd14155    81 SNEP-------LSWTVRVKLALDIARGLSYLHSK---GIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKIPDYSDGKEK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  918 LakptnrpPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLtGKHPLDPD-LPggahlvkwvrdhlaekkdpsRLLD 996
Cdd:cd14155   151 L-------AVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII-ARIQADPDyLP--------------------RTED 202
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 240256081  997 PRLDgrTDSIMHEMLQT----LAVAFLCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd14155   203 FGLD--YDAFQHMVGDCppdfLQLAFNCCNMDPKSRPSFHDIVKTLEEI 249
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
764-969 2.88e-19

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: 88.94  E-value: 2.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITI-PSGESLAVKKMWS---KEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd06605     7 GELGEGNGGVVSKVRHrPSGQIMAVKVIRLeidEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHgagKGGCVDWEARYDVVLGVAHALAYLHHDClpTIIHGDVKAMNVLLGPHFEPYLADFGlartISGYPntgIDLA 919
Cdd:cd06605    87 DKILK---EVGRIPERILGKIAVAVVKGLIYLHEKH--KIIHRDVKPSNILVNSRGQVKLCDFG----VSGQL---VDSL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  920 KPTNrppmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDP 969
Cdd:cd06605   155 AKTF----VGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPP 200
Pkinase pfam00069
Protein kinase domain;
765-967 3.42e-19

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 87.30  E-value: 3.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   765 VIGTGSSGVVYR-ITIPSGESLAVKKM----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWC-SNRNLKLLFyDYLPNGS 838
Cdd:pfam00069    6 KLGSGSFGTVYKaKHRDTGKIVAIKKIkkekIKKKKDKNILREIKILKKLNHPNIVRLYDAFeDKDNLYLVL-EYVEGGS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081   839 LSSRLHGAGkggcvdwearydvvlgvahalaylhhdclptiihgdvkamnvllgpHFEPYLADFGLARTISGypntgidL 918
Cdd:pfam00069   85 LFDLLSEKG----------------------------------------------AFSEREAKFIMKQILEG-------L 111
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 240256081   919 AKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:pfam00069  112 ESGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPF 160
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
798-966 3.72e-19

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: 88.11  E-value: 3.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  798 AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGaGKGGCVDWEARYDVVLGVAHALAYLHHDCLp 877
Cdd:cd05034    36 AFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLDYLRT-GEGRALRLPQLIDMAAQIASGMAYLESRNY- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  878 tiIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypNTGIDLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVL 957
Cdd:cd05034   114 --IHRDLAARNILVGENNVCKVADFGLARLI----EDDEYTAREGAKFPIK----WTAPEAALYGRFTIKSDVWSFGILL 183
                         170
                  ....*....|
gi 240256081  958 LEVLT-GKHP 966
Cdd:cd05034   184 YEIVTyGRVP 193
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
766-972 5.32e-19

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: 88.33  E-value: 5.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKM--WSKEESGAFNSEIKTLGSIRHRNIVRLLG-WCSNRNLKLLfYDYLPNGSLSS 841
Cdd:cd14154     1 LGKGFFGQAIKVThRETGEVMVMKELirFDEEAQRNFLKEVKVMRSLDHPNVLKFIGvLYKDKKLNLI-TEYIPGGTLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGagKGGCVDWEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTI--------SGYPN 913
Cdd:cd14154    80 VLKD--MARPLPWAQRVRFAKDIASGMAYLHSMN---IIHRDLNSHNCLVREDKTVVVADFGLARLIveerlpsgNMSPS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256081  914 TGIDLAKPTNRPP---MAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLtGKHPLDPD-LP 972
Cdd:cd14154   155 ETLRHLKSPDRKKrytVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII-GRVEADPDyLP 216
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
766-966 6.38e-19

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: 87.66  E-value: 6.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGA----FNSEIKTLGSIRHRNIVRLLGwCSNRNLKL-LFYDYLPNGSL 839
Cdd:cd14009     1 IGRGSFATVWKgRHKQTGEVVAIKEISRKKLNKKlqenLESEIAILKSIKHPNIVRLYD-VQKTEDFIyLVLEYCAGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHGagKGGCVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL---GPHFEPYLADFGLARTISgyPNTgi 916
Cdd:cd14009    80 SQYIRK--RGRLPEAVARH-FMQQLASGLKFLRSK---NIIHRDLKPQNLLLstsGDDPVLKIADFGFARSLQ--PAS-- 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  917 dlakptnrppMA----GSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14009   150 ----------MAetlcGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPP 193
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
758-1042 9.64e-19

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: 87.82  E-value: 9.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVY--RITIP---SGESLAVKKMWSKEESGA---FNSEIKTLGSIRHRNIVRLLGWC---SNRNL 826
Cdd:cd05038     4 RHLKFIKQLGEGHFGSVElcRYDPLgdnTGEQVAVKSLQPSGEEQHmsdFKREIEILRTLDHEYIVKYKGVCespGRRSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  827 KLLFyDYLPNGSLSSRLHGAGKGgcVDWEARYDVVLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLAR 906
Cdd:cd05038    84 RLIM-EYLPSGSLRDYLQRHRDQ--IDLKRLLLFASQICKGMEYLGSQRY---IHRDLAARNILVESEDLVKISDFGLAK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  907 TISgyPNTGIDLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLDP-----DLPGGAHLVKW 980
Cdd:cd05038   158 VLP--EDKEYYYVKEPGESPIF----WYAPECLRESRFSSASDVWSFGVTLYELFTyGDPSQSPpalflRMIGIAQGQMI 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  981 VRDHLAEKKDPSRLldPRLDGRTDSIMHEMLqtlavafLCVSNKANERPLMKDVVAMLTEIR 1042
Cdd:cd05038   232 VTRLLELLKSGERL--PRPPSCPDEVYDLMK-------ECWEYEPQDRPSFSDLILIIDRLR 284
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
766-970 1.00e-18

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: 87.44  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKM-WSKEESG-----------AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYD 832
Cdd:cd06629     9 IGKGTYGRVYLaMNATTGEMLAVKQVeLPKTSSDradsrqktvvdALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  833 YLPNGSLSSRLHGAGKggcvdweARYDVVLG----VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLAR-T 907
Cdd:cd06629    89 YVPGGSIGSCLRKYGK-------FEEDLVRFftrqILDGLAYLHSK---GILHRDLKADNILVDLEGICKISDFGISKkS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  908 ISGYPNTGidlakPTNrppMAGSYGYMAPE--HASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd06629   159 DDIYGNNG-----ATS---MQGSVFWMAPEviHSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDD 215
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
765-968 3.74e-18

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: 85.59  E-value: 3.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVKK-----MWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd08215     7 VIGKGSFGSAYLVRrKSDGKLYVLKEidlsnMSEKEREEALN-EVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGAGKGG-------CVDWearydvVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgy 911
Cdd:cd08215    86 LAQKIKKQKKKGqpfpeeqILDW------FVQICLALKYLHSR---KILHRDLKTQNIFLTKDGVVKLGDFGISKVLE-- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  912 pNTgIDLAKpTnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd08215   155 -ST-TDLAK-T----VVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFE 204
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
781-1042 3.82e-18

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 86.22  E-value: 3.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  781 SGESLAVKKMW--SKEESGAFNSEIKTLGSIRHRNIVRLLGWC---SNRNLKLLFyDYLPNGSLSSRLHGAGKGgcVDWE 855
Cdd:cd14205    32 TGEVVAVKKLQhsTEEHLRDFEREIEILKSLQHDNIVKYKGVCysaGRRNLRLIM-EYLPYGSLRDYLQKHKER--IDHI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  856 ARYDVVLGVAHALAYLhhdCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgyPNtgiDLAKPTNRPPMAGSYGYMA 935
Cdd:cd14205   109 KLLQYTSQICKGMEYL---GTKRYIHRDLATRNILVENENRVKIGDFGLTKVL---PQ---DKEYYKVKEPGESPIFWYA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  936 PEHASMQRITEKSDVYSYGVVLLEVLT----GKHPldP----DLPGGAHLVKWVRDHLAE-KKDPSRLldPRLDGRTDSI 1006
Cdd:cd14205   180 PESLTESKFSVASDVWSFGVVLYELFTyiekSKSP--PaefmRMIGNDKQGQMIVFHLIElLKNNGRL--PRPDGCPDEI 255
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 240256081 1007 MHEMLQtlavaflCVSNKANERPLMKDVVAMLTEIR 1042
Cdd:cd14205   256 YMIMTE-------CWNNNVNQRPSFRDLALRVDQIR 284
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
766-966 4.22e-18

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: 85.56  E-value: 4.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVK--KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRL 843
Cdd:cd05148    14 LGSGYFGEVWEGLWKNRVRVAIKilKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSLLAFL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  844 hGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypNTGIDLAKPTN 923
Cdd:cd05148    94 -RSPEGQVLPVASLIDMACQVAEGMAYLEEQ---NSIHRDLAARNILVGEDLVCKVADFGLARLI----KEDVYLSSDKK 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 240256081  924 RPpmagsYGYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05148   166 IP-----YKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVP 204
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
757-1038 7.45e-18

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: 84.73  E-value: 7.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  757 VKNLTSANVIGTGSSGVVY--RITIPSGESLAV-----KKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL 829
Cdd:cd05033     3 ASYVTIEKVIGGGEFGEVCsgSLKLPGKKEIDVaiktlKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 FYDYLPNGSLSSRL-HGAGKggcVDWEARYDVVLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLARti 908
Cdd:cd05033    83 VTEYMENGSLDKFLrENDGK---FTVTQLVGMLRGIASGMKYLSEMNY---VHRDLAARNILVNSDLVCKVSDFGLSR-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  909 sgypntGIDLAKPT-----NRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLDpDLPGgahlvkwvR 982
Cdd:cd05033   155 ------RLEDSEATyttkgGKIPIR----WTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYW-DMSN--------Q 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  983 DHLAEKKDPSRLLDPRldgRTDSIMHEMLQTlavaflCVSNKANERPLMKDVVAML 1038
Cdd:cd05033   216 DVIKAVEDGYRLPPPM---DCPSALYQLMLD------CWQKDRNERPTFSQIVSTL 262
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
764-966 7.96e-18

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: 84.51  E-value: 7.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRI-TIPSGESLAVK-----KMWSKEESgAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLF--YDYLP 835
Cdd:cd08217     6 ETIGKGSFGTVRKVrRKSDGKILVWKeidygKMSEKEKQ-QLVSEVNILRELKHPNIVRYYDRIVDRANTTLYivMEYCE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGAGK-GGCVDWEARYDVVLGVAHALAYLHHDCLP--TIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgyp 912
Cdd:cd08217    85 GGDLAQLIKKCKKeNQYIPEEFIWKIFTQLLLALYECHNRSVGggKILHRDLKPANIFLDSDNNVKLGDFGLARVL---- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  913 NTGIDLAKpTNrppmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd08217   161 SHDSSFAK-TY----VGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPP 209
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
764-966 9.27e-18

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: 84.38  E-value: 9.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR-ITIPSGESLAVKKM-------WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLP 835
Cdd:cd06632     6 QLLGSGSFGSVYEgFNGDTGDFFAVKEVslvdddkKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGAGKggcvdweARYDVVLG----VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGY 911
Cdd:cd06632    86 GGSIHKLLQRYGA-------FEEPVIRLytrqILSGLAYLHSR---NTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  912 pntgiDLAKptnrpPMAGSYGYMAPEhASMQRITE---KSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06632   156 -----SFAK-----SFKGSPYWMAPE-VIMQKNSGyglAVDIWSLGCTVLEMATGKPP 202
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
765-968 1.28e-17

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: 83.72  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVK----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd14003     7 TLGEGSFGKVKLaRHKLTGEKVAIKiidkSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLhgAGKGGCVDWEARY---DVVLGVAhalaYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTISG--YPN 913
Cdd:cd14003    87 FDYI--VNNGRLSEDEARRffqQLISAVD----YCHsNG----IVHRDLKLENILLDKNGNLKIIDFGLSNEFRGgsLLK 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  914 TgidlakptnrppMAGSYGYMAPEH-ASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14003   157 T------------FCGTPAYAAPEVlLGRKYDGPKADVWSLGVILYAMLTGYLPFD 200
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
760-1041 2.44e-17

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: 83.48  E-value: 2.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYR--ITIPSGESLAV-----KKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYD 832
Cdd:cd05063     7 ITKQKVIGAGEFGEVFRgiLKMPGRKEVAVaiktlKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  833 YLPNGSLSSRLHGagKGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYP 912
Cdd:cd05063    87 YMENGALDKYLRD--HDGEFSSYQLVGMLRGIAAGMKYLSD---MNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  913 NTgiDLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLdpdlpggahlvkW-VRDHLAEK-- 988
Cdd:cd05063   162 EG--TYTTSGGKIPIR----WTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPY------------WdMSNHEVMKai 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  989 KDPSRLLDPRldGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd05063   224 NDGFRLPAPM--DCPSAVYQLMLQ-------CWQQDRARRPRFVDIVNLLDKL 267
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
766-972 2.73e-17

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: 82.95  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMWSKE-ESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLh 844
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDvDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 gAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL--GPH-FEPYLADFGLARTISGYPntgidLAKP 921
Cdd:cd14156    80 -AREELPLSWREKVELACDISRGMVYLHSK---NIYHRDLNSKNCLIrvTPRgREAVVTDFGLAREVGEMP-----ANDP 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  922 TNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLtGKHPLDPD-LP 972
Cdd:cd14156   151 ERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIPADPEvLP 201
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
765-1040 2.94e-17

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: 83.23  E-value: 2.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGES----LAVKKMwsKEESGAFNS-----EIKTLGSIRHRNIVRLLGWCSNRNLKLLfYDYL 834
Cdd:cd05057    14 VLGSGAFGTVYKgVWIPEGEKvkipVAIKVL--REETGPKANeeildEAYVMASVDHPHLVRLLGICLSSQVQLI-TQLM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLH----GAGKGGCVDWEARydvvlgVAHALAYL--HHdclptIIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd05057    91 PLGCLLDYVRnhrdNIGSQLLLNWCVQ------IAKGMSYLeeKR-----LVHRDLAARNVLVKTPNHVKITDFGLAKLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  909 SG----YPNTGidlakptNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLDpDLPGgahlvKWVRD 983
Cdd:cd05057   160 DVdekeYHAEG-------GKVPIK----WMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYE-GIPA-----VEIPD 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  984 HLaEKKDpsRLldPRLDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAMLTE 1040
Cdd:cd05057   223 LL-EKGE--RL--PQPPICTIDVYMVLVK-------CWMIDAESRPTFKELANEFSK 267
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
758-966 3.24e-17

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: 83.15  E-value: 3.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRITIpSGESLAVKKMWSKEE------SGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFY 831
Cdd:cd14147     3 QELRLEEVIGIGGFGKVYRGSW-RGELVAVKAARQDPDedisvtAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLPNGSLSSRLHG--AGKGGCVDWEARydvvlgVAHALAYLHHDCLPTIIHGDVKAMNVLLG--------PHFEPYLAD 901
Cdd:cd14147    82 EYAAGGPLSRALAGrrVPPHVLVNWAVQ------IARGMHYLHCEALVPVIHRDLKSNNILLLqpienddmEHKTLKITD 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  902 FGLARTisgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14147   156 FGLARE-----------WHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVP 209
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
765-967 3.54e-17

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: 82.70  E-value: 3.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYLPNGSLSSR 842
Cdd:cd06612    10 KLGEGSYGSVYKaIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCDSPYIVKYYGsYFKNTDLWIVM-EYCGAGSVSDI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGKggcVDWEARYDVVL-GVAHALAYLHhdcLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgiDLAKp 921
Cdd:cd06612    89 MKITNK---TLTEEEIAAILyQTLKGLEYLH---SNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTD------TMAK- 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 240256081  922 tnRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06612   156 --RNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPY 199
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
766-966 7.29e-17

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 82.07  E-value: 7.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR----ITIPsgesLAVKKM----WSKEEsgaFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd05068    16 LGSGQFGEVWEglwnNTTP----VAVKTLkpgtMDPED---FLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGagKGGCVDWEARYDVVLGVAHALAYLHhdcLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypNTGID 917
Cdd:cd05068    89 SLLEYLQG--KGRSLQLPQLIDMAAQVASGMAYLE---SQNYIHRDLAARNVLVGENNICKVADFGLARVIK---VEDEY 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  918 LAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05068   161 EAREGAKFPIK----WTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIP 206
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
760-971 7.99e-17

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: 81.93  E-value: 7.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYR-ITIPSGESL----AVKKM--WSKEES-GAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLfY 831
Cdd:cd05111     9 LRKLKVLGSGVFGTVHKgIWIPEGDSIkipvAIKVIqdRSGRQSfQAVTDHMLAIGSLDHAYIVRLLGICPGASLQLV-T 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLPNGSLSSrlHGAGKGGCVDWEARYDVVLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLARTIsgY 911
Cdd:cd05111    88 QLLPLGSLLD--HVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRM---VHRNLAARNVLLKSPSQVQVADFGVADLL--Y 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  912 PNTGIDLAKPTNRPpmagsYGYMAPEHASMQRITEKSDVYSYGVVLLEVLT-------GKHPLD-PDL 971
Cdd:cd05111   161 PDDKKYFYSEAKTP-----IKWMALESIHFGKYTHQSDVWSYGVTVWEMMTfgaepyaGMRLAEvPDL 223
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
765-960 9.17e-17

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: 82.10  E-value: 9.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRiTIPSGESLAVKKMWSKEESGAF-NSEIKTLGSIRHRNIvrlLGWCSNRN------LKL-LFYDYLPN 836
Cdd:cd14143     2 SIGKGRFGEVWR-GRWRGEDVAVKIFSSREERSWFrEAEIYQTVMLRHENI---LGFIAADNkdngtwTQLwLVSDYHEH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAgkggCVDWEARYDVVLGVAHALAYLHHDCL-----PTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGY 911
Cdd:cd14143    78 GSLFDYLNRY----TVTVEGMIKLALSIASGLAHLHMEIVgtqgkPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  912 PNTgIDLAkPTNRppmAGSYGYMAPE----HASMQRIT--EKSDVYSYGVVLLEV 960
Cdd:cd14143   154 TDT-IDIA-PNHR---VGTKRYMAPEvlddTINMKHFEsfKRADIYALGLVFWEI 203
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
760-968 9.65e-17

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: 81.15  E-value: 9.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYRITIPSGESLAVKKM----WSKEEsgaFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLP 835
Cdd:cd05112     6 LTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIregaMSEED---FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGagKGGCVDWEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTG 915
Cdd:cd05112    83 HGCLSDYLRT--QRGLFSAETLLGMCLDVCEGMAYLEEAS---VIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTS 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  916 IDLAKPTNRppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLD 968
Cdd:cd05112   158 STGTKFPVK--------WSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYE 203
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
766-966 1.66e-16

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: 80.67  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVK--------KMWSKEESGAFNS--------EIKTLGSIRHRNIVRL---LGWCSNRN 825
Cdd:cd14008     1 LGRGSFGKVKLALdTETGQLYAIKifnksrlrKRREGKNDRGKIKnalddvrrEIAIMKKLDHPNIVRLyevIDDPESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  826 LKLLFyDYLPNGSLSSRLHGAGKGGCVDWEAR---YDVVLGvahaLAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLAD 901
Cdd:cd14008    81 LYLVL-EYCEGGPVMELDSGDRVPPLPEETARkyfRDLVLG----LEYLHeNG----IVHRDIKPENLLLTADGTVKISD 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  902 FGLARTISGypntGIDLAKPTnrppmAGSYGYMAPEHASMQRIT---EKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14008   152 FGVSEMFED----GNDTLQKT-----AGTPAFLAPELCDGDSKTysgKAADIWALGVTLYCLVFGRLP 210
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
758-972 1.95e-16

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: 80.41  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVV----YRitipsGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKL-LFYD 832
Cdd:cd05082     6 KELKLLQTIGKGEFGDVmlgdYR-----GNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLyIVTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  833 YLPNGSLSSRLHGAGKGgCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYP 912
Cdd:cd05082    81 YMAKGSLVDYLRSRGRS-VLGGDCLLKFSLDVCEAMEYLEGN---NFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQ 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  913 NTGidlakptnRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLdPDLP 972
Cdd:cd05082   157 DTG--------KLPVK----WTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY-PRIP 204
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
744-967 2.20e-16

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: 80.60  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  744 TLYQKLDfsiddivknltsanVIGTGSSGVVYR-ITIPSGESLAVKKM---WSKEESGAFNSEIKTLGSIRH---RNIVR 816
Cdd:cd06917     1 SLYRRLE--------------LVGRGSYGAVYRgYHVKTGRVVALKVLnldTDDDDVSDIQKEVALLSQLKLgqpKNIIK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  817 LLG-WCSNRNLKLLFyDYLPNGSLSSRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHF 895
Cdd:cd06917    67 YYGsYLKGPSLWIIM-DYCEGGSIRTLM----RAGPIAERYIAVIMREVLVALKFIHKD---GIIHRDIKAANILVTNTG 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  896 EPYLADFGLARTISgyPNTGidlakptNRPPMAGSYGYMAPEhasmqRITE------KSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06917   139 NVKLCDFGVAASLN--QNSS-------KRSTFVGTPYWMAPE-----VITEgkyydtKADIWSLGITTYEMATGNPPY 202
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
764-972 3.57e-16

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: 80.07  E-value: 3.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESG--AFNSEIKTLGSI-RHRNIVRLLG----WCSNRNLKLLFYDYLP 835
Cdd:cd13985     6 KQLGEGGFSYVYLaHDVNTGRRYALKRMYFNDEEQlrVAIKEIEIMKRLcGHPNIVQYYDsailSSEGRKEVLLLMEYCP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 nGSLSSRLHGAGKGGCVDWEArYDVVLGVAHALAYLHHdCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNT- 914
Cdd:cd13985    86 -GSLVDILEKSPPSPLSEEEV-LRIFYQICQAVGHLHS-QSPPIIHRDIKIENILFSNTGRFKLCDFGSATTEHYPLERa 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  915 ---GI---DLAKPTNrpPMagsygYMAPEHA---SMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLP 972
Cdd:cd13985   163 eevNIieeEIQKNTT--PM-----YRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSK 222
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
752-966 3.61e-16

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: 79.59  E-value: 3.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  752 SIDDIVKNLTSANVIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGA--FNSEIKTLGSIRHRNIVRLL-GWCSNRNLK 827
Cdd:cd06647     1 SVGDPKKKYTRFEKIGQGASGTVYTaIDVATGQEVAIKQMNLQQQPKKelIINEILVMRENKNPNIVNYLdSYLVGDELW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  828 LLFyDYLPNGSLSSRLHGAgkggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLART 907
Cdd:cd06647    81 VVM-EYLAGGSLTDVVTET----CMDEGQIAAVCRECLQALEFLHSN---QVIHRDIKSDNILLGMDGSVKLTDFGFCAQ 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  908 ISgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06647   153 IT---------PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPP 202
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
765-1038 4.84e-16

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: 79.58  E-value: 4.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIpSGESLAVKkMWSKEESGAFNS------------------------EIKTLGSIRHRNIVRLLGW 820
Cdd:cd14000     1 LLGDGGFGSVYRASY-KGEPVAVK-IFNKHTSSNFANvpadtmlrhlratdamknfrllrqELTVLSHLHHPSIVYLLGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  821 CSNRnlKLLFYDYLPNGSLSSRL-HGAGKGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLL-----GPH 894
Cdd:cd14000    79 GIHP--LMLVLELAPLGSLDHLLqQDSRSFASLGRTLQQRIALQVADGLRYLHS---AMIIYRDLKSHNVLVwtlypNSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  895 FEPYLADFGLARTISgypntgidlakPTNRPPMAGSYGYMAPEHASMQRI-TEKSDVYSYGVVLLEVLTGKHPLDpdlpg 973
Cdd:cd14000   154 IIIKIADYGISRQCC-----------RMGAKGSEGTPGFRAPEIARGNVIyNEKVDVFSFGMLLYEILSGGAPMV----- 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  974 GAHLVKwvrdhlaEKKDPSRLLDPRLDGRTDSIMHEMlqtLAVAFLCVSNKANERPLMKDVVAML 1038
Cdd:cd14000   218 GHLKFP-------NEFDIHGGLRPPLKQYECAPWPEV---EVLMKKCWKENPQQRPTAVTVVSIL 272
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
766-962 5.18e-16

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: 79.73  E-value: 5.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR--ITIPSGE----SLAVKKMwsKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:cd05048    13 LGEGAFGKVYKgeLLGPSSEesaiSVAIKTL--KENASPktqqdFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRL-----HGAGKGGCVDWEARY--------DVVLGVAHALAYL--HHdclptIIHGDVKAMNVLLGPHFEPYL 899
Cdd:cd05048    91 AHGDLHEFLvrhspHSDVGVSSDDDGTASsldqsdflHIAIQIAAGMEYLssHH-----YVHRDLAARNCLVGDGLTVKI 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256081  900 ADFGLARTIsgYPNtgiDLAKPTNRPPMagSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05048   166 SDFGLSRDI--YSS---DYYRVQSKSLL--PVRWMPPEAILYGKFTTESDVWSFGVVLWEIFS 221
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
766-966 5.78e-16

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: 78.95  E-value: 5.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVY--RITIPSGESLAVKKMWSKEESGAFN---SEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd14120     1 IGHGAFAVVFkgRHRKKPDLPVAIKCITKKNLSKSQNllgKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAGKGGcvdwEARYDVVLG-VAHALAYLHHDclpTIIHGDVKAMNVLL----GPHFEPY-----LADFGLARtisg 910
Cdd:cd14120    81 DYLQAKGTLS----EDTIRVFLQqIAAAMKALHSK---GIVHRDLKPQNILLshnsGRKPSPNdirlkIADFGFAR---- 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  911 YPNTGIDLAKptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14120   150 FLQDGMMAAT------LCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAP 199
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
758-968 6.61e-16

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: 78.64  E-value: 6.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRITIPSGESLAVKKMwsKEESGA---FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:cd05059     4 SELTFLKELGSGQFGVVHLGKWRGKIDVAIKMI--KEGSMSeddFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLHG-AGKGGCvdwEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPN 913
Cdd:cd05059    82 ANGCLLNYLRErRGKFQT---EQLLEMCKDVCEAMEYLESNG---FIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEY 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  914 TGIDLAK-PTNRPPmagsygymaPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLD 968
Cdd:cd05059   156 TSSVGTKfPVKWSP---------PEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYE 203
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
757-973 6.76e-16

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: 79.72  E-value: 6.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  757 VKNLTSANVIGTGSSGVVYRI-TIPSGESLAVKKM-WSKEESGAFNS---EIKTLGSIRHRNIVRLLGWCSNRNLKLLF- 830
Cdd:cd07845     6 VTEFEKLNRIGEGTYGIVYRArDTTSGEIVALKKVrMDNERDGIPISslrEITLLLNLRHPNIVELKEVVVGKHLDSIFl 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 -YDYLPNgSLSSRLHGAGkggCVDWEARYD-VVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd07845    86 vMEYCEQ-DLASLLDNMP---TPFSESQVKcLMLQLLRGLQYLHENF---IIHRDLKVSNLLLTDKGCLKIADFGLARTY 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  909 sGYPntgidlakPTNRPPMAGSYGYMAPEHA-SMQRITEKSDVYSYGVVLLEVLTGKhpldPDLPG 973
Cdd:cd07845   159 -GLP--------AKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHK----PLLPG 211
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
764-972 6.94e-16

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 78.90  E-value: 6.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIPSGESLAV------KKMWSKEESgAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd14202     8 DLIGHGAFAVVFKGRHKEKHDLEVavkcinKKNLAKSQT-LLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGkggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL----GPHFEP-----YLADFGLARTI 908
Cdd:cd14202    87 DLADYLHTMR---TLSEDTIRLFLQQIAGAMKMLHSK---GIIHRDLKPQNILLsysgGRKSNPnniriKIADFGFARYL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  909 SGypntgiDLAKPTnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLP 972
Cdd:cd14202   161 QN------NMMAAT----LCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSP 214
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
766-972 8.34e-16

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 78.83  E-value: 8.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKM--WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd14222     1 LGKGFFGQAIKVThKATGKVMVMKELirCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGKggcVDWEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTI-SGYPNTGIDlaKP 921
Cdd:cd14222    81 LRADDP---FPWQQKVSFAKGIASGMAYLHSMS---IIHRDLNSHNCLIKLDKTVVVADFGLSRLIvEEKKKPPPD--KP 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  922 TN------------RPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLtGKHPLDPD-LP 972
Cdd:cd14222   153 TTkkrtlrkndrkkRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII-GQVYADPDcLP 215
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
766-1029 8.64e-16

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: 78.93  E-value: 8.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMWSKEES-GAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLH 844
Cdd:cd05072    15 LGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSvQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLLDFLK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 gAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDLAK-PTN 923
Cdd:cd05072    95 -SDEGGKVLLPKLIDFSAQIAEGMAYIERK---NYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKfPIK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  924 rppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPldpdLPGGAHlvkwvRDHLAEKKDPSRLldPRLDGR 1002
Cdd:cd05072   171 ---------WTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIP----YPGMSN-----SDVMSALQRGYRM--PRMENC 230
                         250       260
                  ....*....|....*....|....*..
gi 240256081 1003 TDSiMHEMLQTlavaflCVSNKANERP 1029
Cdd:cd05072   231 PDE-LYDIMKT------CWKEKAEERP 250
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
765-970 1.22e-15

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: 78.24  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVKKM----WSKEES----GAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLP 835
Cdd:cd06630     7 LLGTGAFSSCYQARdVKTGTLMAVKQVsfcrNSSSEQeevvEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLH--GAGKGGCVdweARYdvVLGVAHALAYLHHDClptIIHGDVKAMNVLL---GPHFEpyLADFGLARTISG 910
Cdd:cd06630    87 GGSVASLLSkyGAFSENVI---INY--TLQILRGLAYLHDNQ---IIHRDLKGANLLVdstGQRLR--IADFGAAARLAS 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  911 yPNTGIDLAKPTnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd06630   157 -KGTGAGEFQGQ----LLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAE 211
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
737-962 1.40e-15

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: 77.85  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  737 EIDSWEVTLYQKLdfsiddivknltsanviGTGSSGVVYR-ITIPSGESLAVKKMwsKEESGA---FNSEIKTLGSIRHR 812
Cdd:cd05052     2 EIERTDITMKHKL-----------------GGGQYGEVYEgVWKKYNLTVAVKTL--KEDTMEveeFLKEAAVMKEIKHP 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  813 NIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGGcVDWEARYDVVLGVAHALAYLHHDCLptiIHGDVKAMNVLLG 892
Cdd:cd05052    63 NLVQLLGVCTREPPFYIITEFMPYGNLLDYLRECNREE-LNAVVLLYMATQIASAMEYLEKKNF---IHRDLAARNCLVG 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  893 PHFEPYLADFGLARTISGYPNTGIDLAK-PTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05052   139 ENHLVKVADFGLSRLMTGDTYTAHAGAKfPIK---------WTAPESLAYNKFSIKSDVWAFGVLLWEIAT 200
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
785-970 1.44e-15

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: 78.08  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  785 LAVKKMWSK--EESGA---FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKggcVDWEARYD 859
Cdd:cd14116    33 LALKVLFKAqlEKAGVehqLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSK---FDEQRTAT 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  860 VVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgypntgidlAKPTNRPPMAGSYGYMAPEHA 939
Cdd:cd14116   110 YITELANALSYCHSK---RVIHRDIKPENLLLGSAGELKIADFGWSVH-----------APSSRRTTLCGTLDYLPPEMI 175
                         170       180       190
                  ....*....|....*....|....*....|.
gi 240256081  940 SMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14116   176 EGRMHDEKVDLWSLGVLCYEFLVGKPPFEAN 206
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
758-960 1.59e-15

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: 77.78  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRITIpSGESLAVKKMwsKEESGA---FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:cd05039     6 KDLKLGELIGKGEFGDVMLGDY-RGQKVAVKCL--KDDSTAaqaFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLHGAGKGgCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARtisgYPNT 914
Cdd:cd05039    83 AKGSLVDYLRSRGRA-VITRKDQLGFALDVCEGMEYLESK---KFVHRDLAARNVLVSEDNVAKVSDFGLAK----EASS 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 240256081  915 GIDLAK-PTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEV 960
Cdd:cd05039   155 NQDGGKlPIK---------WTAPEALREKKFSTKSDVWSFGILLWEI 192
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
766-972 1.79e-15

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: 77.69  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKM--WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd14221     1 LGKGCFGQAIKVThRETGEVMVMKELirFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGKGgcVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTI---SGYPNTGIDLA 919
Cdd:cd14221    81 IKSMDSH--YPWSQRVSFAKDIASGMAYLHS---MNIIHRDLNSHNCLVRENKSVVVADFGLARLMvdeKTQPEGLRSLK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  920 KPTNRP--PMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLtGKHPLDPD-LP 972
Cdd:cd14221   156 KPDRKKryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII-GRVNADPDyLP 210
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
765-966 2.17e-15

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: 77.25  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM--WSKEESGAFNsEIKTLGSIRHRNIVRLLGwcSNRNLKLLF--YDYLPNGSL 839
Cdd:cd06614     7 KIGEGASGEVYKaTDRATGKEVAIKKMrlRKQNKELIIN-EILIMKECKHPNIVDYYD--SYLVGDELWvvMEYMDGGSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSrlhgagkggCVDW------EARYDVVLG-VAHALAYLH--HdclptIIHGDVKAMNVLLGPHFEPYLADFGLARTISg 910
Cdd:cd06614    84 TD---------IITQnpvrmnESQIAYVCReVLQGLEYLHsqN-----VIHRDIKSDNILLSKDGSVKLADFGFAAQLT- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  911 ypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06614   149 --------KEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPP 196
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
766-966 2.22e-15

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: 77.76  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMW--SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLfYDYLPNGSLSSRL 843
Cdd:cd14149    20 IGSGSFGTVYKGKWHGDVAVKILKVVdpTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIV-TQWCEGSSLYKHL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  844 HGAgkggcvdwEARY------DVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLArTISGYPNTGID 917
Cdd:cd14149    99 HVQ--------ETKFqmfqliDIARQTAQGMDYLHAK---NIIHRDMKSNNIFLHEGLTVKIGDFGLA-TVKSRWSGSQQ 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  918 LAKPTnrppmaGSYGYMAPEHASMQR---ITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14149   167 VEQPT------GSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMTGELP 212
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
766-968 2.40e-15

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: 77.21  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVK----------KMWSKeesgaFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:cd14099     9 LGKGGFAKCYEVTdMSTGKVYAGKvvpkssltkpKQREK-----LKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSsRLHGAgKGGCVDWEARYdVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLA--------- 905
Cdd:cd14099    84 SNGSLM-ELLKR-RKALTEPEVRY-FMRQILSGVKYLHSNR---IIHRDLKLGNLFLDENMNVKIGDFGLAarleydger 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  906 -RTISGYPNtgidlakptnrppmagsygYMAPEhasmqrITEKS-------DVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14099   158 kKTLCGTPN-------------------YIAPE------VLEKKkghsfevDIWSLGVILYTLLVGKPPFE 203
PLN03150 PLN03150
hypothetical protein; Provisional
122-211 4.05e-15

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 79.86  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  122 LDLSDNSLSGDIPVEIFRLKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGEIPRSIGELKNLQVLRAGGNKn 201
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNS- 501
                          90
                  ....*....|
gi 240256081  202 LRGELPWEIG 211
Cdd:PLN03150  502 LSGRVPAALG 511
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
765-966 4.85e-15

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: 76.11  E-value: 4.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAvkkmW--------SKEESGAFNSEIKTLGSIRHRNIVRLLG-WCSNRNLKLLFY-DY 833
Cdd:cd13983     8 VLGRGSFKTVYRaFDTEEGIEVA----WneiklrklPKAERQRFKQEIEILKSLKHPNIIKFYDsWESKSKKEVIFItEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSLSSRLhgaGKGGCVDWEARYDVVLGVAHALAYLHhDCLPTIIHGDVKAMNVLL-GPHFEPYLADFGLA------- 905
Cdd:cd13983    84 MTSGTLKQYL---KRFKRLKLKVIKSWCRQILEGLNYLH-TRDPPIIHRDLKCDNIFInGNTGEVKIGDLGLAtllrqsf 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  906 -RTISGYPNtgidlakptnrppmagsygYMAPEhasM--QRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd13983   160 aKSVIGTPE-------------------FMAPE---MyeEHYDEKVDIYAFGMCLLEMATGEYP 201
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
786-996 5.26e-15

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: 76.98  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  786 AVKKMWSKE-ESGAFNSEIKTLGSIRHRNIVRLLGWCSN-RNLKL---LFYDYLPNGSLSSRLhgagKGGCVDWEARYDV 860
Cdd:cd14053    22 AVKIFPLQEkQSWLTEREIYSLPGMKHENILQFIGAEKHgESLEAeywLITEFHERGSLCDYL----KGNVISWNELCKI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  861 VLGVAHALAYLHHDCL-------PTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypnTGIDLAKPTNRppmAGSYGY 933
Cdd:cd14053    98 AESMARGLAYLHEDIPatngghkPSIAHRDFKSKNVLLKSDLTACIADFGLALKFE----PGKSCGDTHGQ---VGTRRY 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  934 MAPE---------HASMQRIteksDVYSYGVVLLEVLT-----GKHPLDPDLP----GGAH-----LVKWVrdhlAEKKD 990
Cdd:cd14053   171 MAPEvlegainftRDAFLRI----DMYAMGLVLWELLSrcsvhDGPVDEYQLPfeeeVGQHptledMQECV----VHKKL 242

                  ....*.
gi 240256081  991 PSRLLD 996
Cdd:cd14053   243 RPQIRD 248
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
758-966 7.91e-15

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: 75.97  E-value: 7.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRIT----IPSGES--LAVKKMWSKEESGA---FNSEIKTLGSIRHRNIVRLLGWCSNRNLKL 828
Cdd:cd05049     5 DTIVLKRELGEGAFGKVFLGEcynlEPEQDKmlVAVKTLKDASSPDArkdFEREAELLTNLQHENIVKFYGVCTEGDPLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSS--RLHGA---------GKGGCVDWEARYDVVLGVAHALAYLhhdCLPTIIHGDVKAMNVLLGPHFEP 897
Cdd:cd05049    85 MVFEYMEHGDLNKflRSHGPdaaflasedSAPGELTLSQLLHIAVQIASGMVYL---ASQHFVHRDLATRNCLVGTNLVV 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  898 YLADFGLARTIsgYPNTGIDLAKPTNRPpmagsYGYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05049   162 KIGDFGMSRDI--YSTDYYRVGGHTMLP-----IRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQP 224
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
765-967 9.51e-15

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: 75.74  E-value: 9.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM---WSKEESGAFNSEIKTLGSIRHRNIVRLLGwCSNRNLKL-LFYDYLPNGSL 839
Cdd:cd06609     8 RIGKGSFGEVYKgIDKRTNQVVAIKVIdleEAEDEIEDIQQEIQFLSQCDSPYITKYYG-SFLKGSKLwIIMEYCGGGSV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgidlA 919
Cdd:cd06609    87 LDLL----KPGPLDETYIAFILREVLLGLEYLHSEGK---IHRDIKAANILLSEEGDVKLADFGVSGQLT---------S 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  920 KPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06609   151 TMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPL 198
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
765-966 1.45e-14

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: 75.08  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVKKMW-------SKEESGAFNSEIKTLGSIRHRNIVRLLGwCSNRNLKL-LFYDYLP 835
Cdd:cd06625     7 LLGQGAFGQVYLCYdADTGRELAVKQVEidpinteASKEVKALECEIQLLKNLQHERIVQYYG-CLQDEKSLsIFMEYMP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHgagKGGCVDwearyDVVLG-----VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLAR---T 907
Cdd:cd06625    86 GGSVKDEIK---AYGALT-----ENVTRkytrqILEGLAYLHSN---MIVHRDIKGANILRDSNGNVKLGDFGASKrlqT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  908 ISGypNTGIDlakptnrpPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06625   155 ICS--STGMK--------SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPP 203
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
766-966 1.62e-14

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 74.84  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVK----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRnlKLLFYDYLPNGSLS 840
Cdd:cd14025     4 VGSGGFGQVYKVRhKHWKTWLAIKcppsLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSEP--VGLVMEYMETGSLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAgkggCVDWEARYDVVLGVAHALAYLHhdCL-PTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDla 919
Cdd:cd14025    82 KLLASE----PLPWELRFRIIHETAVGMNFLH--CMkPPLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHSHDLS-- 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  920 kptnRPPMAGSYGYMAPEhasmqRITEKS-------DVYSYGVVLLEVLTGKHP 966
Cdd:cd14025   154 ----RDGLRGTIAYLPPE-----RFKEKNrcpdtkhDVYSFAIVIWGILTQKKP 198
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
766-968 3.10e-14

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: 74.14  E-value: 3.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR---ITIPSGESLAVK----KMWSKEESGAF-NSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd14080     8 IGEGSYSKVKLaeyTKSGLKEKVACKiidkKKAPKDFLEKFlPRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAEHG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSS--RLHGAGKGGcvdwEARyDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISgyPNTG 915
Cdd:cd14080    88 DLLEyiQKRGALSES----QAR-IWFRQLALAVQYLHSLD---IAHRDLKCENILLDSNNNVKLSDFGFARLCP--DDDG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  916 IDLAKpTnrppMAGSYGYMAPEhaSMQRIT---EKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14080   158 DVLSK-T----FCGSAAYAAPE--ILQGIPydpKKYDIWSLGVILYIMLCGSMPFD 206
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
766-966 3.13e-14

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: 73.71  E-value: 3.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMwSKE------ESGAFNSEIKTLGSIRHRNIVRLlgWCS---NRNLKLLFyDYLP 835
Cdd:cd05123     1 LGKGSFGKVLLVRkKDTGKLYAMKVL-RKKeiikrkEVEHTLNERNILERVNHPFIVKL--HYAfqtEEKLYLVL-DYVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHgagKGGCVD-WEARY---DVVLgvahALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTISg 910
Cdd:cd05123    77 GGELFSHLS---KEGRFPeERARFyaaEIVL----ALEYLHsLG----IIYRDLKPENILLDSDGHIKLTDFGLAKELS- 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  911 ypnTGIDLAKPtnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd05123   145 ---SDGDRTYT-----FCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPP 192
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
779-972 3.32e-14

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: 74.12  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  779 IPSGESLAVKKMWSK--EESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEA 856
Cdd:cd14045    27 IYDGRTVAIKKIAKKsfTLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVL--LNEDIPLNWGF 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  857 RYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLArtisgypntgidLAKPTNRPPMAGSYG---- 932
Cdd:cd14045   105 RFSFATDIARGMAYLHQH---KIYHGRLKSSNCVIDDRWVCKIADYGLT------------TYRKEDGSENASGYQqrlm 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 240256081  933 --YMAPEHAS--MQRITEKSDVYSYGVVLLEVLTGKHPLDPDLP 972
Cdd:cd14045   170 qvYLPPENHSntDTEPTQATDVYSYAIILLEIATRNDPVPEDDY 213
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
764-962 3.58e-14

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: 73.92  E-value: 3.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIPSG---ESLAVKKM---WSKEESGAFNSEIKTLGSI-RHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:cd05047     1 DVIGEGNFGQVLKARIKKDglrMDAAIKRMkeyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGA-------------GKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd05047    81 GNLLDFLRKSrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQK---QFIHRDLAARNILVGENYVAKIADFG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  904 LARTISGYpntgidLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05047   158 LSRGQEVY------VKKTMGRLPVR----WMAIESLNYSVYTTNSDVWSYGVLLWEIVS 206
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
765-966 3.61e-14

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: 73.98  E-value: 3.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKMWSK--EESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd06624    15 VLGKGTFGVVYAaRDLSTQVRIAIKEIPERdsREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGAgkggcvdWEARYDVVLGVAH-------ALAYLHHDclpTIIHGDVKAMNVLLgphfEPY-----LADFGLARTIS 909
Cdd:cd06624    95 LLRSK-------WGPLKDNENTIGYytkqileGLKYLHDN---KIVHRDIKGDNVLV----NTYsgvvkISDFGTSKRLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  910 GY-PNTGidlakptnrpPMAGSYGYMAPEhasmqrITEK--------SDVYSYGVVLLEVLTGKHP 966
Cdd:cd06624   161 GInPCTE----------TFTGTLQYMAPE------VIDKgqrgygppADIWSLGCTIIEMATGKPP 210
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
765-966 3.76e-14

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: 73.75  E-value: 3.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVY--RITIPSGESLAV-----KKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd05065    11 VIGAGEFGEVCrgRLKLPGKREIFVaiktlKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAgkggcvdwEARYDVVL------GVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGy 911
Cdd:cd05065    91 ALDSFLRQN--------DGQFTVIQlvgmlrGIAAGMKYLSE---MNYVHRDLAARNILVNSNLVCKVSDFGLSRFLED- 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  912 pntgiDLAKPTNRPPMAGSYG--YMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05065   159 -----DTSDPTYTSSLGGKIPirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERP 211
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
759-983 4.17e-14

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: 74.44  E-value: 4.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  759 NLTSANVIGTGSSGVVYRIT----IPSGESL--AVKKMWSK---EESGAFNSEIKTLGSI-RHRNIVRLLGWCSNRNLKL 828
Cdd:cd05055    36 NLSFGKTLGAGAFGKVVEATayglSKSDAVMkvAVKMLKPTahsSEREALMSELKIMSHLgNHENIVNLLGACTIGGPIL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSSRLHgAGKGGCVDWEARYDVVLGVAHALAYL-HHDClptiIHGDVKAMNVLLGPHFEPYLADFGLART 907
Cdd:cd05055   116 VITEYCCYGDLLNFLR-RKRESFLTLEDLLSFSYQVAKGMAFLaSKNC----IHRDLAARNVLLTHGKIVKICDFGLARD 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  908 ISGYPNTgidLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLdPDLPGGAHLVKWVRD 983
Cdd:cd05055   191 IMNDSNY---VVKGNARLPVK----WMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPY-PGMPVDSKFYKLIKE 259
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
760-1039 4.32e-14

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: 74.38  E-value: 4.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYR---ITIPSGE----SLAVKKM---WSKEESGAFNSEIKTLGSI-RHRNIVRLLGWCSNRNLKL 828
Cdd:cd05053    14 LTLGKPLGEGAFGQVVKaeaVGLDNKPnevvTVAVKMLkddATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSSRLHG-------AGKGGCVDWEAR---YDVV---LGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHF 895
Cdd:cd05053    94 VVVEYASKGNLREFLRArrppgeeASPDDPRVPEEQltqKDLVsfaYQVARGMEYLASK---KCIHRDLAARNVLVTEDN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  896 EPYLADFGLARTISgypntGIDLAKPTN--RPPmagsYGYMAPEhASMQRI-TEKSDVYSYGVVLLEVLT-GKHPLdPDL 971
Cdd:cd05053   171 VMKIADFGLARDIH-----HIDYYRKTTngRLP----VKWMAPE-ALFDRVyTHQSDVWSFGVLLWEIFTlGGSPY-PGI 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  972 PggahlVKWVRDHLAEKKdpsRLLDPRLdgRTDSIMHEMLQtlavaflCVSNKANERP----LMKDVVAMLT 1039
Cdd:cd05053   240 P-----VEELFKLLKEGH---RMEKPQN--CTQELYMLMRD-------CWHEVPSQRPtfkqLVEDLDRILT 294
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
752-966 4.32e-14

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: 74.38  E-value: 4.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  752 SIDDIVKNLTSANVIGTGSSGVVYRIT-IPSGESLAVKK--MWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKL 828
Cdd:cd06655    13 SIGDPKKKYTRYEKIGQGASGTVFTAIdVATGQEVAIKQinLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSSRLHGAgkggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd06655    93 VVMEYLAGGSLTDVVTET----CMDEAQIAAVCRECLQALEFLHAN---QVIHRDIKSDNVLLGMDGSVKLTDFGFCAQI 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  909 SgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06655   166 T---------PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPP 214
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
739-1041 4.77e-14

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: 73.56  E-value: 4.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  739 DSWEVTLYQkldfsiddivknLTSANVIGTGSSGVVYR-------------ITIPSGESLAvkkmwskeesgAFNSEIKT 805
Cdd:cd14151     1 DDWEIPDGQ------------ITVGQRIGSGSFGTVYKgkwhgdvavkmlnVTAPTPQQLQ-----------AFKNEVGV 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  806 LGSIRHRNIVRLLGWCSNRNLKLLfYDYLPNGSLSSRLHGAGKGgcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVK 885
Cdd:cd14151    58 LRKTRHVNILLFMGYSTKPQLAIV-TQWCEGSSLYHHLHIIETK--FEMIKLIDIARQTAQGMDYLHAK---SIIHRDLK 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  886 AMNVLLGPHFEPYLADFGLARTISGYPNTgidlakpTNRPPMAGSYGYMAPEHASMQR---ITEKSDVYSYGVVLLEVLT 962
Cdd:cd14151   132 SNNIFLHEDLTVKIGDFGLATVKSRWSGS-------HQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  963 GKHPLDpDLPGGAHLVKWV-RDHLAEKKDPSRLLDPRldgRTDSIMHEmlqtlavaflCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd14151   205 GQLPYS-NINNRDQIIFMVgRGYLSPDLSKVRSNCPK---AMKRLMAE----------CLKKKRDERPLFPQILASIELL 270
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
766-968 4.95e-14

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: 74.01  E-value: 4.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMWSKEESGAFNS---EIKTLGSIRHRNIVRLLGWCSNRNLKL-LFYDYLPNGSLS 840
Cdd:cd06620    13 LGAGNGGSVSKVLhIPTGTIMAKKVIHIDAKSSVRKQilrELQILHECHSPYIVSFYGAFLNENNNIiICMEYMDCGSLD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHgagKGGCVDWEARYDVVLGVAHALAYL---HHdclptIIHGDVKAMNVLLGPHFEPYLADFGLART-ISGYPNTgi 916
Cdd:cd06620    93 KILK---KKGPFPEEVLGKIAVAVLEGLTYLynvHR-----IIHRDIKPSNILVNSKGQIKLCDFGVSGElINSIADT-- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  917 dlakptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd06620   163 ----------FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFA 204
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
765-966 5.31e-14

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: 73.05  E-value: 5.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIP-SGESLAVK----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYlPNGSL 839
Cdd:cd14002     8 LIGEGSFGKVYKGRRKyTGQVVALKfipkRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEY-AQGEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHGAGKGGcvdwearYDVVLGVA----HALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS--GYPN 913
Cdd:cd14002    87 FQILEDDGTLP-------EEEVRSIAkqlvSALHYLHSN---RIIHRDMKPQNILIGKGGVVKLCDFGFARAMScnTLVL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  914 TGIdlaKPTnrpPMagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14002   157 TSI---KGT---PL-----YMAPELVQEQPYDHTADLWSLGCILYELFVGQPP 198
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
759-998 5.68e-14

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: 73.14  E-value: 5.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  759 NLTSANVIGTGSSGVVYRI-TIPSGESLAVKKM-------WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL- 829
Cdd:cd06653     3 NWRLGKLLGRGAFGEVYLCyDADTGRELAVKQVpfdpdsqETSKEVNALECEIQLLKNLRHDRIVQYYGCLRDPEEKKLs 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 -FYDYLPNGSLSSRLHGAGkggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd06653    83 iFVEYMPGGSVKDQLKAYG---ALTENVTRRYTRQILQGVSYLHSN---MIVHRDIKGANILRDSAGNVKLGDFGASKRI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  909 SGYPNTGIDLAKPTNRPpmagsYgYMAPEHASMQRITEKSDVYSYGVVLLEVLTGK-----------------HPLDPDL 971
Cdd:cd06653   157 QTICMSGTGIKSVTGTP-----Y-WMSPEVISGEGYGRKADVWSVACTVVEMLTEKppwaeyeamaaifkiatQPTKPQL 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 240256081  972 PGGAHlvKWVRDHLA-----EKKDPSRLLDPR 998
Cdd:cd06653   231 PDGVS--DACRDFLRqifveEKRRPTAEFLLR 260
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
766-967 6.49e-14

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 73.11  E-value: 6.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRI-TIPSGESLAVK--KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd06613     8 IGSGTYGDVYKArNIATGELAAVKviKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGGGSLQDI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LH--GAGKGGCVDWEARYdVVLGvahaLAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLARTISgypNTgidLAK 920
Cdd:cd06613    88 YQvtGPLSELQIAYVCRE-TLKG----LAYLHSTGK---IHRDIKGANILLTEDGDVKLADFGVSAQLT---AT---IAK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  921 ptnRPPMAGSYGYMAPEHASMQRI---TEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06613   154 ---RKSFIGTPYWMAPEVAAVERKggyDGKCDIWALGITAIELAELQPPM 200
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
766-973 6.71e-14

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: 73.37  E-value: 6.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKK--MWSKEESGAFNS--EIKTLGSIRHRNIVRLL------GWCSNRNLKLLFYDYL 834
Cdd:cd07840     7 IGEGTYGQVYKaRNKKTGELVALKKirMENEKEGFPITAirEIKLLQKLDHPNVVRLKeivtskGSAKYKGSIYMVFEYM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNgSLSSRLHgagkggcvdweaRYDVVLGVAH----------ALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGL 904
Cdd:cd07840    87 DH-DLTGLLD------------NPEVKFTESQikcymkqlleGLQYLHSN---GILHRDIKGSNILINNDGVLKLADFGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  905 ARTISGYPNtgidlAKPTN-------RPPM----AGSYGYmapehasmqriteKSDVYSYGVVLLEVLTGKhpldPDLPG 973
Cdd:cd07840   151 ARPYTKENN-----ADYTNrvitlwyRPPElllgATRYGP-------------EVDMWSVGCILAELFTGK----PIFQG 208
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
757-966 7.00e-14

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: 72.98  E-value: 7.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  757 VKNLTSANVIGTGSSGVVYRITIpSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLkLLFYDYLPN 836
Cdd:cd05083     5 LQKLTLGEIIGEGEFGAVLQGEY-MGQKVAVKNIKCDVTAQAFLEETAVMTKLQHKNLVRLLGVILHNGL-YIVMELMSK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGgCVDWEARYDVVLGVAHALAYLHhdcLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypnTGI 916
Cdd:cd05083    83 GNLVNFLRSRGRA-LVPVIQLLQFSLDVAEGMEYLE---SKKLVHRDLAARNILVSEDGVAKISDFGLAKVGS----MGV 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  917 DlakpTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05083   155 D----NSRLPVK----WTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAP 197
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
765-966 7.02e-14

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: 72.98  E-value: 7.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVY--RITIPSGESLAV-----KKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd05066    11 VIGAGEFGEVCsgRLKLPGKREIPVaiktlKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSS--RLHgagkggcvdwEARYDVVL------GVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS 909
Cdd:cd05066    91 SLDAflRKH----------DGQFTVIQlvgmlrGIASGMKYLSD---MGYVHRDLAARNILVNSNLVCKVSDFGLSRVLE 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  910 GYPntgiDLAKPTN--RPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05066   158 DDP----EAAYTTRggKIPIR----WTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERP 209
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
765-1038 7.96e-14

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 73.29  E-value: 7.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT------IPSGESLAVKKM---WSKEESGAFNSEIKTLGSI-RHRNIVRLLGWCSNRNLKLL-FYDY 833
Cdd:cd05054    14 PLGRGAFGKVIQASafgidkSATCRTVAVKMLkegATASEHKALMTELKILIHIgHHLNVVNLLGACTKPGGPLMvIVEF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSLSSRLHGA--------GKGGCVDWEARYDVVLG---------------VAHALAYL-HHDClptiIHGDVKAMNV 889
Cdd:cd05054    94 CKFGNLSNYLRSKreefvpyrDKGARDVEEEEDDDELYkepltledlicysfqVARGMEFLaSRKC----IHRDLAARNI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  890 LLGPHFEPYLADFGLARTISGYPNTgidLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPld 968
Cdd:cd05054   170 LLSENNVVKICDFGLARDIYKDPDY---VRKGDARLPLK----WMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASP-- 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  969 pdLPGgahlVKWVRDHLAEKKDPSRLLDPrlDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAML 1038
Cdd:cd05054   241 --YPG----VQMDEEFCRRLKEGTRMRAP--EYTTPEIYQIMLD-------CWHGEPKERPTFSELVEKL 295
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
760-971 1.23e-13

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: 73.18  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYR-ITIPSGESL----AVKKMwsKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL 829
Cdd:cd05110     9 LKRVKVLGSGAFGTVYKgIWVPEGETVkipvAIKIL--NETTGPkanveFMDEALIMASMDHPHLVRLLGVCLSPTIQLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 fYDYLPNGSLSSRLH----GAGKGGCVDWearydvVLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLA 905
Cdd:cd05110    87 -TQLMPHGCLLDYVHehkdNIGSQLLLNW------CVQIAKGMMYLEERRL---VHRDLAARNVLVKSPNHVKITDFGLA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  906 RTISGYpntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLD-------PDL 971
Cdd:cd05110   157 RLLEGD-------EKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDgiptreiPDL 223
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
766-1040 1.38e-13

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 71.99  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR--ITIPSGESL--AVK-----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFyDYLPN 836
Cdd:cd05040     3 LGDGSFGVVRRgeWTTPSGKVIqvAVKclksdVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLMMVT-ELAPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGGCVDWEARYDVvlGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLARTISgypnTGI 916
Cdd:cd05040    82 GSLLDRLRKDQGHFLISTLCDYAV--QIANGMAYLESKRF---IHRDLAARNILLASKDKVKIGDFGLMRALP----QNE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  917 D--LAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPldpdlpggahlvkWV----RDHLaEK- 988
Cdd:cd05040   153 DhyVMQEHRKVPFA----WCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEP-------------WLglngSQIL-EKi 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  989 -KDPSRLldPRLDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAMLTE 1040
Cdd:cd05040   215 dKEGERL--ERPDDCPQDIYNVMLQ-------CWAHKPADRPTFVALRDFLPE 258
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
766-966 1.45e-13

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: 72.16  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMWSKeesgAFNSE-IKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRL 843
Cdd:cd13991    14 IGRGSFGEVHRMEdKQTGFQCAVKKVRLE----VFRAEeLMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQLI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  844 HgagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL---GPHfePYLADFGLARTISgypNTGIDLAK 920
Cdd:cd13991    90 K---EQGCLPEDRALHYLGQALEGLEYLHSR---KILHGDVKADNVLLssdGSD--AFLCDFGHAECLD---PDGLGKSL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 240256081  921 PT-NRPPmaGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd13991   159 FTgDYIP--GTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHP 203
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
766-966 1.60e-13

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: 71.55  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSG--ESLAVKKMWSKE--ESGAFN--SEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd14121     3 LGSGTYATVYKAYRKSGarEVVAVKCVSKSSlnKASTENllTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHGagKGGCVDWEARYdVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYL--ADFGLARTISgypntgi 916
Cdd:cd14121    83 SRFIRS--RRTLPESTVRR-FLQQLASALQFLReHN----ISHMDLKPQNLLLSSRYNPVLklADFGFAQHLK------- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  917 DLAKPTNrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14121   149 PNDEAHS---LRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAP 195
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
752-994 1.69e-13

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: 72.45  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  752 SIDDIVKNLTSANVIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGA--FNSEIKTLGSIRHRNIVRLLGWCSNRNLKL 828
Cdd:cd06656    13 SVGDPKKKYTRFEKIGQGASGTVYTaIDIATGQEVAIKQMNLQQQPKKelIINEILVMRENKNPNIVNYLDSYLVGDELW 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSSRLHGAgkggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd06656    93 VVMEYLAGGSLTDVVTET----CMDEGQIAAVCRECLQALDFLHSN---QVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  909 SgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAhLVKWVRDHLAEK 988
Cdd:cd06656   166 T---------PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRA-LYLIATNGTPEL 235

                  ....*.
gi 240256081  989 KDPSRL 994
Cdd:cd06656   236 QNPERL 241
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
759-985 1.72e-13

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: 72.04  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  759 NLTSANVIGTGSSGVVYRI-TIPSGESLAVKKMW-------SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL- 829
Cdd:cd06651     8 NWRRGKLLGQGAFGRVYLCyDVDTGRELAAKQVQfdpespeTSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLt 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 -FYDYLPNGSLSSRLHGAGkggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd06651    88 iFMEYMPGGSVKDQLKAYG---ALTESVTRKYTRQILEGMSYLHSN---MIVHRDIKGANILRDSAGNVKLGDFGASKRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  909 SGYPNTGIDLAKPTNRPPmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGK-----------------HPLDPDL 971
Cdd:cd06651   162 QTICMSGTGIRSVTGTPY------WMSPEVISGEGYGRKADVWSLGCTVVEMLTEKppwaeyeamaaifkiatQPTNPQL 235
                         250
                  ....*....|....
gi 240256081  972 PggAHLVKWVRDHL 985
Cdd:cd06651   236 P--SHISEHARDFL 247
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
765-962 1.75e-13

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: 71.58  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIPSGESLAVKKM---WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd05085     3 LLGKGNFGEVYKGTLKDKTPVAVKTCkedLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHgaGKGGCVDWEARYDVVLGVAHALAYLH-HDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISG--YPNTGIdl 918
Cdd:cd05085    83 FLR--KKKDELKTKQLVKFSLDAAAGMAYLEsKNC----IHRDLAARNCLVGENNALKISDFGMSRQEDDgvYSSSGL-- 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 240256081  919 akptNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05085   155 ----KQIPIK----WTAPEALNYGRYSSESDVWSFGILLWETFS 190
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
766-966 1.97e-13

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 71.49  E-value: 1.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMWSKEES-GAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLfYDYLPNGSLSSRLH 844
Cdd:cd14203     3 LGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSpEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIV-TEFMSKGSLLDFLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 GaGKGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidlAKPTNR 924
Cdd:cd14203    82 D-GEGKYLKLPQLVDMAAQIASGMAYIER---MNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYT----ARQGAK 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 240256081  925 PPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd14203   154 FPIK----WTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVP 192
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
756-960 2.02e-13

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: 72.09  E-value: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  756 IVKNLTSANVIGTGSSGVVYRITIpSGESLAVKKMWSKEESGAF-NSEIKTLGSIRHRNIVRLLGW-CSNRN----LKLL 829
Cdd:cd14142     3 VARQITLVECIGKGRYGEVWRGQW-QGESVAVKIFSSRDEKSWFrETEIYNTVLLRHENILGFIASdMTSRNsctqLWLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 FYdYLPNGSLSSRLHGAgkggCVDWEARYDVVLGVAHALAYLHHDCL-----PTIIHGDVKAMNVLLGPHFEPYLADFGL 904
Cdd:cd14142    82 TH-YHENGSLYDYLQRT----TLDHQEMLRLALSAASGLVHLHTEIFgtqgkPAIAHRDLKSKNILVKSNGQCCIADLGL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  905 ARTISGYPNTgIDLAkptnRPPMAGSYGYMAPEHASMQRITE------KSDVYSYGVVLLEV 960
Cdd:cd14142   157 AVTHSQETNQ-LDVG----NNPRVGTKRYMAPEVLDETINTDcfesykRVDIYAFGLVLWEV 213
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
766-963 2.14e-13

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 71.26  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP-SGESLAVKK----MWSKEESGAFNSEIKTLGSI-RHRNIVRLL-GWCSNRNLkLLFYDYLPNGS 838
Cdd:cd13997     8 IGSGSFSEVFKVRSKvDGCLYAVKKskkpFRGPKERARALREVEAHAALgQHPNIVRYYsSWEEGGHL-YIQMELCENGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypnTGIDL 918
Cdd:cd13997    87 LQDALEELSPISKLSEAEVWDLLLQVALGLAFIHSK---GIVHLDIKPDNIFISNKGTCKIGDFGLATRLE----TSGDV 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 240256081  919 AKptnrppmaGSYGYMAPEH-ASMQRITEKSDVYSYGVVLLEVLTG 963
Cdd:cd13997   160 EE--------GDSRYLAPELlNENYTHLPKADIFSLGVTVYEAATG 197
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
750-1047 2.23e-13

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: 72.01  E-value: 2.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  750 DFSIDDivknLTSANVIGTGSSGVVYR-ITIPSGESLAVKKMWS---KEESGAFNSEIKTLgsIRHRN---IVRLLGwcs 822
Cdd:cd06616     2 EFTAED----LKDLGEIGRGAFGTVNKmLHKPSGTIMAVKRIRStvdEKEQKRLLMDLDVV--MRSSDcpyIVKFYG--- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  823 nrnlkLLFYD-------YLPNGSL---SSRLHGAGKGgCVDWEARYDVVLGVAHALAYLHHDClpTIIHGDVKAMNVLLG 892
Cdd:cd06616    73 -----ALFREgdcwicmELMDISLdkfYKYVYEVLDS-VIPEEILGKIAVATVKALNYLKEEL--KIIHRDVKPSNILLD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  893 PHFEPYLADFGlartISGYPNTGIdlAKPTNrppmAGSYGYMAPEHASMQRITE----KSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd06616   145 RNGNIKLCDFG----ISGQLVDSI--AKTRD----AGCRPYMAPERIDPSASRDgydvRSDVWSLGITLYEVATGKFPYP 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  969 pdlpggahlvKW--VRDHLAE--KKDPsrlldPRLDgrTDSIMHEMLQTLAVAFLCVSNKANERPLMKDVVAM----LTE 1040
Cdd:cd06616   215 ----------KWnsVFDQLTQvvKGDP-----PILS--NSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHpfikMYE 277

                  ....*..
gi 240256081 1041 IRHIDVG 1047
Cdd:cd06616   278 ERNVDVA 284
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
766-966 2.32e-13

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: 71.92  E-value: 2.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT----IPSGESL--AVKKMWSKEESGA--FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd05092    13 LGEGAFGKVFLAEchnlLPEQDKMlvAVKALKEATESARqdFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRHG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSS--RLHG-------AGKG---GCVDWEARYDVVLGVAHALAYL---HhdclptIIHGDVKAMNVLLGPHFEPYLADF 902
Cdd:cd05092    93 DLNRflRSHGpdakildGGEGqapGQLTLGQMLQIASQIASGMVYLaslH------FVHRDLATRNCLVGQGLVVKIGDF 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  903 GLARTI--SGYPNTGIDLAKPTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05092   167 GMSRDIysTDYYRVGGRTMLPIR---------WMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQP 224
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
764-970 2.38e-13

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: 71.35  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR-ITIPSGESLAVKKM------WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:cd14098     6 DRLGSGTFAEVKKaVEVETGKMRAIKQIvkrkvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRL--HGAgkggcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL---GPhFEPYLADFGLARTISGy 911
Cdd:cd14098    86 GDLMDFImaWGA-----IPEQHARELTKQILEAMAYTHSM---GITHRDLKPENILItqdDP-VIVKISDFGLAKVIHT- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  912 pNTGIDlakptnrpPMAGSYGYMAPEhASMQRIT-------EKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14098   156 -GTFLV--------TFCGTMAYLAPE-ILMSKEQnlqggysNLVDMWSVGCLVYVMLTGALPFDGS 211
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
759-985 2.56e-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: 71.23  E-value: 2.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  759 NLTSANVIGTGSSGVVYRI-TIPSGESLAVKKMW-------SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL- 829
Cdd:cd06652     3 NWRLGKLLGQGAFGRVYLCyDADTGRELAVKQVQfdpespeTSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQERTLs 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 -FYDYLPNGSLSSRLHGAGkggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd06652    83 iFMEYMPGGSIKDQLKSYG---ALTENVTRKYTRQILEGVHYLHSN---MIVHRDIKGANILRDSVGNVKLGDFGASKRL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  909 SGYPNTGIDLAKPTNRPpmagsYgYMAPEHASMQRITEKSDVYSYGVVLLEVLTGK-----------------HPLDPDL 971
Cdd:cd06652   157 QTICLSGTGMKSVTGTP-----Y-WMSPEVISGEGYGRKADIWSVGCTVVEMLTEKppwaefeamaaifkiatQPTNPQL 230
                         250
                  ....*....|....
gi 240256081  972 PggAHLVKWVRDHL 985
Cdd:cd06652   231 P--AHVSDHCRDFL 242
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
764-982 2.57e-13

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: 71.11  E-value: 2.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFN-SEIKTL----GSIRHRNIVRLLG---WCSNRNLKLLFYDYL 834
Cdd:cd05118     5 RKIGEGAFGTVWLaRDKVTGEKVAIKKIKNDFRHPKAAlREIKLLkhlnDVEGHPNIVKLLDvfeHRGGNHLCLVFELMG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PN-----GSLSSRLHgagkggcvDWEARYdVVLGVAHALAYLH-HDclptIIHGDVKAMNVLL-GPHFEPYLADFGLART 907
Cdd:cd05118    85 MNlyeliKDYPRGLP--------LDLIKS-YLYQLLQALDFLHsNG----IIHRDLKPENILInLELGQLKLADFGLARS 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  908 ISGYPNTgidlakptnrpPMAGSYGYMAPEHA-SMQRITEKSDVYSYGVVLLEVLTGKhPLDPDLPGGAHLVKWVR 982
Cdd:cd05118   152 FTSPPYT-----------PYVATRWYRAPEVLlGAKPYGSSIDIWSLGCILAELLTGR-PLFPGDSEVDQLAKIVR 215
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
766-960 2.66e-13

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 71.74  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIpSGESLAVKKMWSKEESGAF-NSEIKTLGSIRHRNIVRLL-----GWCSNRNLkLLFYDYLPNGSL 839
Cdd:cd14144     3 VGKGRYGEVWKGKW-RGEKVAVKIFFTTEEASWFrETEIYQTVLMRHENILGFIaadikGTGSWTQL-YLITDYHENGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDCL-----PTIIHGDVKAMNVLLGPHFEPYLADFGLA-RTISgyPN 913
Cdd:cd14144    81 YDFL----RGNTLDTQSMLKLAYSAACGLAHLHTEIFgtqgkPAIAHRDIKSKNILVKKNGTCCIADLGLAvKFIS--ET 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  914 TGIDLAkPTNRppmAGSYGYMAPE--HASMQRIT----EKSDVYSYGVVLLEV 960
Cdd:cd14144   155 NEVDLP-PNTR---VGTKRYMAPEvlDESLNRNHfdayKMADMYSFGLVLWEI 203
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
766-963 3.04e-13

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: 70.94  E-value: 3.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITI-PSGESLAVKKMWS---KEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd05041     3 IGRGNFGDVYRGVLkPDNTEVAVKTCREtlpPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGAGKGGCVdwEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidLAKP 921
Cdd:cd05041    83 FLRKKGARLTV--KQLLQMCLDAAAGMEYLESKN---CIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYT---VSDG 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 240256081  922 TNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTG 963
Cdd:cd05041   155 LKQIPIK----WTAPEALNYGRYTSESDVWSFGILLWEIFSL 192
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
752-966 4.06e-13

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: 71.29  E-value: 4.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  752 SIDDIVKNLTSANVIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGA--FNSEIKTLGSIRHRNIVRLLGWCSNRNLKL 828
Cdd:cd06654    14 SVGDPKKKYTRFEKIGQGASGTVYTaMDVATGQEVAIRQMNLQQQPKKelIINEILVMRENKNPNIVNYLDSYLVGDELW 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSSRLHGAgkggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd06654    94 VVMEYLAGGSLTDVVTET----CMDEGQIAAVCRECLQALEFLHSN---QVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  909 SgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06654   167 T---------PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPP 215
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
784-967 4.60e-13

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 70.47  E-value: 4.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  784 SLAVKKMWSKEESgafnsEIKTLGSIRHRNIVRLLGWCSNRN-------LKLLFyDYLPNGSLSSRLHGAGKggcVDWEA 856
Cdd:cd14012    35 TSNGKKQIQLLEK-----ELESLKKLRHPNLVSYLAFSIERRgrsdgwkVYLLT-EYAPGGSLSELLDSVGS---VPLDT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  857 RYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFE---PYLADFGLARTISGYPNTGI-DLAKPTnrppmagsyG 932
Cdd:cd14012   106 ARRWTLQLLEALEYLHRN---GVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDMCSRGSlDEFKQT---------Y 173
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 240256081  933 YMAPEHASM-QRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14012   174 WLPPELAQGsKSPTRKTDVWDLGLLFLQMLFGLDVL 209
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
766-1013 4.63e-13

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: 70.44  E-value: 4.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP-SGESLAVKKMWSKEESGAF----NSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd14069     9 LGEGAFGEVFLAVNRnTEEAVAVKFVDMKRAPGDCpeniKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGELF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLhgagkggcvdwEARYDVVLGVAH--------ALAYLHhDClpTIIHGDVKAMNVLLGPHFEPYLADFGLArTISGYP 912
Cdd:cd14069    89 DKI-----------EPDVGMPEDVAQfyfqqlmaGLKYLH-SC--GITHRDIKPENLLLDENDNLKISDFGLA-TVFRYK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  913 NTGIDLAKPTNRPPmagsygYMAPE-HASMQRITEKSDVYSYGVVLLEVLTGKHPLdpDLPGGAHLvkwvrDHLAEKKDP 991
Cdd:cd14069   154 GKERLLNKMCGTLP------YVAPElLAKKKYRAEPVDVWSCGIVLFAMLAGELPW--DQPSDSCQ-----EYSDWKENK 220
                         250       260
                  ....*....|....*....|....
gi 240256081  992 SRLLDP--RLDGRTDSIMHEMLQT 1013
Cdd:cd14069   221 KTYLTPwkKIDTAALSLLRKILTE 244
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
766-966 5.03e-13

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 70.87  E-value: 5.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMWSKEES-GAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLfYDYLPNGSLSSRLH 844
Cdd:cd05070    17 LGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSpESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIV-TEYMSKGSLLDFLK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 GaGKGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidlAKPTNR 924
Cdd:cd05070    96 D-GEGRALKLPNLVDMAAQVAAGMAYIER---MNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYT----ARQGAK 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 240256081  925 PPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05070   168 FPIK----WTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVP 206
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
765-969 5.49e-13

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


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 70.81  E-value: 5.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVY----RITipsGESLAVKKMWSKEESGAFNS----EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:cd07833     8 VVGEGAYGVVLkcrnKAT---GEIVAIKKFKESEDDEDVKKtalrEVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLssRLHGAGKGGcVDWEARYDVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTG 915
Cdd:cd07833    85 TLL--ELLEASPGG-LPPDAVRSYIWQLLQAIAYCHsHN----IIHRDIKPENILVSESGVLKLCDFGFARALTARPASP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  916 ID--LAKPTNRPP--MAGSYGYMAPehasmqritekSDVYSYGVVLLEVLTGKhPLDP 969
Cdd:cd07833   158 LTdyVATRWYRAPelLVGDTNYGKP-----------VDVWAIGCIMAELLDGE-PLFP 203
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
802-966 5.78e-13

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: 70.22  E-value: 5.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIH 881
Cdd:cd14027    41 EGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVL----KKVSVPLSVKGRIILEIIEGMAYLHGK---GVIH 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  882 GDVKAMNVLLGPHFEPYLADFGLARTisgypNTGIDLAKPTNR---------PPMAGSYGYMAPEHAS--MQRITEKSDV 950
Cdd:cd14027   114 KDLKPENILVDNDFHIKIADLGLASF-----KMWSKLTKEEHNeqrevdgtaKKNAGTLYYMAPEHLNdvNAKPTEKSDV 188
                         170
                  ....*....|....*.
gi 240256081  951 YSYGVVLLEVLTGKHP 966
Cdd:cd14027   189 YSFAIVLWAIFANKEP 204
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
758-962 5.85e-13

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: 70.80  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRITIPS-GESLA-----VKKMWSKEESGAFNSEIKTLGSI-RHRNIVRLLGWCSNRNLKLLF 830
Cdd:cd05089     2 EDIKFEDVIGEGNFGQVIKAMIKKdGLKMNaaikmLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 YDYLPNGSLSSRLHGA-------------GKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEP 897
Cdd:cd05089    82 IEYAPYGNLLDFLRKSrvletdpafakehGTASTLTSQQLLQFASDVAKGMQYLSEK---QFIHRDLAARNVLVGENLVS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  898 YLADFGLARTISGYpntgidLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05089   159 KIADFGLSRGEEVY------VKKTMGRLPVR----WMAIESLNYSVYTTKSDVWSFGVLLWEIVS 213
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
766-1037 5.96e-13

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: 70.53  E-value: 5.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPS--GESLAVKKMwsKEESGAFNS------EI---KTLGSIRHRNIVRLL-GWCSNRNLKLLFyDY 833
Cdd:cd14052     8 IGSGEFSQVYKVSERVptGKVYAVKKL--KPNYAGAKDrlrrleEVsilRELTLDGHDNIVQLIdSWEYHGHLYIQT-EL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSLSSRLHGAGKGGCVDwEAR-YDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgYP 912
Cdd:cd14052    85 CENGSLDVFLSELGLLGRLD-EFRvWKILVELSLGLRFIHDH---HFVHLDLKPANVLITFEGTLKIGDFGMATV---WP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  913 -NTGIDLAkptnrppmaGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD-------------PDLPGGAHLV 978
Cdd:cd14052   158 lIRGIERE---------GDREYIAPEILSEHMYDKPADIFSLGLILLEAAANVVLPDngdawqklrsgdlSDAPRLSSTD 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  979 KWVRDHLAEKKDPSRLLDPRLDGRTDSIMHEMLqtlavaflcvSNKANERPLMKDVVAM 1037
Cdd:cd14052   229 LHSASSPSSNPPPDPPNMPILSGSLDRVVRWML----------SPEPDRRPTADDVLAT 277
PLN03150 PLN03150
hypothetical protein; Provisional
276-354 6.03e-13

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 72.93  E-value: 6.03e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  276 GSIPTTIGGLKKLQSLLLWQNNLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTIPEEL 354
Cdd:PLN03150  432 GFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAAL 510
PLN03150 PLN03150
hypothetical protein; Provisional
363-484 6.57e-13

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 72.93  E-value: 6.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  363 LEIDNNLITGEIPSLMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIfglrnltkllllsndl 442
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESL---------------- 486
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 240256081  443 sgfippdiGNCTNLYRLRLNGNRLAGSIPSEIGNL----KNLNFVD 484
Cdd:PLN03150  487 --------GQLTSLRILNLNGNSLSGRVPAALGGRllhrASFNFTD 524
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
759-1034 6.68e-13

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: 70.76  E-value: 6.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  759 NLTSANVIGTGSSGVVYRIT------IPSGESLAVK---KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL 829
Cdd:cd05045     1 NLVLGKTLGEGEFGKVVKATafrlkgRAGYTTVAVKmlkENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 FYDYLPNGSLSSRLHGAGKGGC-------------VDWEARYDVVLG--------VAHALAYLHHDCLptiIHGDVKAMN 888
Cdd:cd05045    81 IVEYAKYGSLRSFLRESRKVGPsylgsdgnrnssyLDNPDERALTMGdlisfawqISRGMQYLAEMKL---VHRDLAARN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  889 VLLGPHFEPYLADFGLARTIsgYPNTGIdLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPl 967
Cdd:cd05045   158 VLVAEGRKMKISDFGLSRDV--YEEDSY-VKRSKGRIPVK----WMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNP- 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  968 dpdLPGGAhlvkwvrdhlaekkdPSRLLD-----PRLDgRTDSIMHEMLQtlaVAFLCVSNKANERPLMKDV 1034
Cdd:cd05045   230 ---YPGIA---------------PERLFNllktgYRME-RPENCSEEMYN---LMLTCWKQEPDKRPTFADI 279
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
766-966 6.72e-13

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 70.49  E-value: 6.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMWSKEESG-AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLfYDYLPNGSLSSRLH 844
Cdd:cd05071    17 LGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPeAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIV-TEYMSKGSLLDFLK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 GAgKGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidlAKPTNR 924
Cdd:cd05071    96 GE-MGKYLRLPQLVDMAAQIASGMAYVER---MNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYT----ARQGAK 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 240256081  925 PPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05071   168 FPIK----WTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVP 206
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
859-972 7.05e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 72.52  E-value: 7.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  859 DVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypNTGIdlakpTNRPPMAGSYGYMAPE 937
Cdd:NF033483  111 EIMIQILSALEHAHrNG----IVHRDIKPQNILITKDGRVKVTDFGIARALS---STTM-----TQTNSVLGTVHYLSPE 178
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 240256081  938 HASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLP 972
Cdd:NF033483  179 QARGGTVDARSDIYSLGIVLYEMLTGRPPFDGDSP 213
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
767-962 7.46e-13

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: 70.51  E-value: 7.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  767 GTGSSgvVYRI----TIPSGES-LAVKKMWSKEESGA-------FNSEIKTLGSIRHRNIVRLLGWCSNRNLKL-LFYDY 833
Cdd:cd14001    10 GTGVN--VYLMkrspRGGSSRSpWAVKKINSKCDKGQrslyqerLKEEAKILKSLNHPNIVGFRAFTKSEDGSLcLAMEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LpNGSLSSRLhgagkggcvdwEARYD-------------VVLGVAHALAYLHHDCLptIIHGDVKAMNVLLGPHFEPY-L 899
Cdd:cd14001    88 G-GKSLNDLI-----------EERYEaglgpfpaatilkVALSIARALEYLHNEKK--ILHGDIKSGNVLIKGDFESVkL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  900 ADFGLARTISGypnTGIDLAKPTNRppMAGSYGYMAPE-HASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd14001   154 CDFGVSLPLTE---NLEVDSDPKAQ--YVGTEPWKAKEaLEEGGVITDKADIFAYGLVLWEMMT 212
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
762-971 8.23e-13

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: 69.99  E-value: 8.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  762 SANVIGTGSSG-VVYRITIpSGESLAVKKMWSKEESGAFNsEIKTL-GSIRHRNIVRLlgWCSNRNLKLLF--------- 830
Cdd:cd13982     5 SPKVLGYGSEGtIVFRGTF-DGRPVAVKRLLPEFFDFADR-EVQLLrESDEHPNVIRY--FCTEKDRQFLYialelcaas 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 -YDYLPNGSLSSRLHgagKGGCVDWEARYDVVLGVAHalayLHHdclPTIIHGDVKAMNVLLGP-----HFEPYLADFGL 904
Cdd:cd13982    81 lQDLVESPRESKLFL---RPGLEPVRLLRQIASGLAH----LHS---LNIVHRDLKPQNILISTpnahgNVRAMISDFGL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  905 ARTISGYPNTGIDLAKPtnrppmAGSYGYMAPEHAS---MQRITEKSDVYSYGVVLLEVLT-GKHPLDPDL 971
Cdd:cd13982   151 CKKLDVGRSSFSRRSGV------AGTSGWIAPEMLSgstKRRQTRAVDIFSLGCVFYYVLSgGSHPFGDKL 215
PLN03150 PLN03150
hypothetical protein; Provisional
442-536 8.66e-13

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 72.54  E-value: 8.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  442 LSGFIPPDIGNCTNLYRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLSGSL--- 518
Cdd:PLN03150  430 LRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVpaa 509
                          90
                  ....*....|....*...
gi 240256081  519 LGTTLPKSLKFiDFSDNA 536
Cdd:PLN03150  510 LGGRLLHRASF-NFTDNA 526
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
766-1040 1.06e-12

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: 69.72  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMWSKEESG-AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLfYDYLPNGSLSSRLH 844
Cdd:cd05069    20 LGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPeAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIV-TEFMGKGSLLDFLK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 gAGKGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidlAKPTNR 924
Cdd:cd05069    99 -EGDGKYLKLPQLVDMAAQIADGMAYIER---MNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYT----ARQGAK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  925 PPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPldpdLPGGAHlvkwvRDHLAEKKDPSRLLDPRldGRT 1003
Cdd:cd05069   171 FPIK----WTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVP----YPGMVN-----REVLEQVERGYRMPCPQ--GCP 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 240256081 1004 DSiMHEMLQtlavafLCVSNKANERPLMKDVVAMLTE 1040
Cdd:cd05069   236 ES-LHELMK------LCWKKDPDERPTFEYIQSFLED 265
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
765-966 1.49e-12

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: 69.53  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRI-TIPSGESLAVKKMwSKEESGAF------NSEIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYLPN 836
Cdd:cd05580     8 TLGTGSFGRVRLVkHKDSGKYYALKIL-KKAKIIKLkqvehvLNEKRILSEVRHPFIVNLLGsFQDDRNLYMVM-EYVPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGGcvDWEARY---DVVLgvahALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPN 913
Cdd:cd05580    86 GELFSLLRRSGRFP--NDVAKFyaaEVVL----ALEYLHSL---DIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRTY 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  914 TgidlakptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd05580   157 T------------LCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPP 197
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
766-1038 1.60e-12

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: 69.29  E-value: 1.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR---ITIPSGES---LAVKKMWSKEESG---AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:cd05032    14 LGQGSFGMVYEglaKGVVKGEPetrVAIKTVNENASMReriEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMELMAK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHG-------AGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS 909
Cdd:cd05032    94 GDLKSYLRSrrpeaenNPGLGPPTLQKFIQMAAEIADGMAYLAAK---KFVHRDLAARNCMVAEDLTVKIGDFGMTRDIY 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  910 gypNTgiDLAKPTNRPPMAgsYGYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPldpdLPGGAH--LVKWV--RDH 984
Cdd:cd05032   171 ---ET--DYYRKGGKGLLP--VRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQP----YQGLSNeeVLKFVidGGH 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  985 LAEKKDPsrlldprldgrtDSIMHEMLQTlavaflCVSNKANERPLMKDVVAML 1038
Cdd:cd05032   240 LDLPENC------------PDKLLELMRM------CWQYNPKMRPTFLEIVSSL 275
PLN03150 PLN03150
hypothetical protein; Provisional
459-566 1.77e-12

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 71.39  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  459 LRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLSGSllgttlpkslkfidfsdnals 538
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGS--------------------- 481
                          90       100
                  ....*....|....*....|....*...
gi 240256081  539 stLPPGIGLLTELTKLNLAKNRLSGEIP 566
Cdd:PLN03150  482 --IPESLGQLTSLRILNLNGNSLSGRVP 507
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
766-1035 2.07e-12

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: 68.84  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSG-VVYRITIpSGESLAVKKMWSKEESGA-----------------------FNSEIKTLGSIRHRNIVRLLGWc 821
Cdd:cd14067     1 LGQGGSGtVIYRARY-QGQPVAVKRFHIKKCKKRtdgsadtmlkhlraadamknfseFRQEASMLHSLQHPCIVYLIGI- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  822 snrNLKLLFY--DYLPNGSLSSRLHGAGKGGC---VDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL----- 891
Cdd:cd14067    79 ---SIHPLCFalELAPLGSLNTVLEENHKGSSfmpLGHMLTFKIAYQIAAGLAYLHKK---NIIFCDLKSDNILVwsldv 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  892 GPHFEPYLADFGLARTISGYPNTGIDlakptnrppmaGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDpdl 971
Cdd:cd14067   153 QEHINIKLSDYGISRQSFHEGALGVE-----------GTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSL--- 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  972 pgGAHlvkwvrdHLAEKKDPSRLLDPRLdGRTDSIMHEMLQTLAVAflCVSNKANERPLMKDVV 1035
Cdd:cd14067   219 --GHH-------QLQIAKKLSKGIRPVL-GQPEEVQFFRLQALMME--CWDTKPEKRPLACSVV 270
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
764-971 2.09e-12

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 68.65  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITI----PSGESLAVK---KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWC-SNRNLKLLFYDYLP 835
Cdd:cd05058     1 EVIGKGHFGCVYHGTLidsdGQKIHCAVKslnRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGIClPSEGSPLVVLPYMK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGAGKGGCVDwearyDVV---LGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI---- 908
Cdd:cd05058    81 HGDLRNFIRSETHNPTVK-----DLIgfgLQVAKGMEYLASK---KFVHRDLAARNCMLDESFTVKVADFGLARDIydke 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  909 --SGYPNTGIDLakptnrpPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDL 971
Cdd:cd05058   153 yySVHNHTGAKL-------PVK----WMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDV 206
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
751-968 2.29e-12

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: 68.74  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  751 FSIDD--IVKNLtsanviGTGSSGVVYRITIPSGESLAVKKMWSK---EESGA---FNSEIKTLGSIRHRNIVRLLGWCS 822
Cdd:cd14117     3 FTIDDfdIGRPL------GKGKFGNVYLAREKQSKFIVALKVLFKsqiEKEGVehqLRREIEIQSHLRHPNILRLYNYFH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  823 NRNLKLLFYDYLPNGSLSSRLHgagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADF 902
Cdd:cd14117    77 DRKRIYLILEYAPRGELYKELQ---KHGRFDEQRTATFMEELADALHYCHEK---KVIHRDIKPENLLMGYKGELKIADF 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  903 GLARTisgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14117   151 GWSVH-----------APSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFE 205
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
860-968 2.32e-12

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: 68.99  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  860 VVLGVAHALAYLHHDClpTIIHGDVKAMNVLLGPHFEPYLADFGlartISGYPntgID-LAKPTNrppmAGSYGYMAPEH 938
Cdd:cd06617   108 IAVSIVKALEYLHSKL--SVIHRDVKPSNVLINRNGQVKLCDFG----ISGYL---VDsVAKTID----AGCKPYMAPER 174
                          90       100       110
                  ....*....|....*....|....*....|....
gi 240256081  939 ----ASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd06617   175 inpeLNQKGYDVKSDVWSLGITMIELATGRFPYD 208
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
766-983 2.32e-12

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: 69.09  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP---SGES---LAVKKMwsKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:cd05050    13 IGQGAFGRVFQARAPgllPYEPftmVAVKML--KEEASAdmqadFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLH----------GAGKGGCVDWEARY---------DVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHF 895
Cdd:cd05050    91 AYGDLNEFLRhrspraqcslSHSTSSARKCGLNPlplscteqlCIAKQVAAGMAYLSER---KFVHRDLATRNCLVGENM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  896 EPYLADFGLARTI--SGYPNTGIDLAKPTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPldpdLP 972
Cdd:cd05050   168 VVKIADFGLSRNIysADYYKASENDAIPIR---------WMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQP----YY 234
                         250
                  ....*....|...
gi 240256081  973 GGAH--LVKWVRD 983
Cdd:cd05050   235 GMAHeeVIYYVRD 247
PLN03150 PLN03150
hypothetical protein; Provisional
207-310 2.79e-12

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 71.00  E-value: 2.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  207 PWEIGNCE------NLVM--LGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLYQNSISGSI 278
Cdd:PLN03150  403 PWSGADCQfdstkgKWFIdgLGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSI 482
                          90       100       110
                  ....*....|....*....|....*....|..
gi 240256081  279 PTTIGGLKKLQSLLLWQNNLVGKIPTELGNCP 310
Cdd:PLN03150  483 PESLGQLTSLRILNLNGNSLSGRVPAALGGRL 514
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
766-968 3.05e-12

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: 68.24  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSG-VVYRITIPSGESLAVK-----------KMWSKEESGAFNSEIKT-----LGSI-RHRNIVRLLGWCSNRNLK 827
Cdd:cd14077     9 IGAGSMGkVKLAKHIRTGEKCAIKiiprasnaglkKEREKRLEKEISRDIRTireaaLSSLlNHPHICRLRDFLRTPNHY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  828 LLFYDYLPNGSLSSRL--HGAGKggcvDWEARyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLA 905
Cdd:cd14077    89 YMLFEYVDGGQLLDYIisHGKLK----EKQAR-KFARQIASALDYLHRN---SIVHRDLKIENILISKSGNIKIIDFGLS 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  906 RTISgypntgidlaKPTNRPPMAGSYGYMAPEHASMQRIT-EKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14077   161 NLYD----------PRRLLRTFCGSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVCGKVPFD 214
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
766-969 3.20e-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: 68.55  E-value: 3.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRI-TIPSGESLAVKKMWSKEESGAFNS----EIKTLGSIRHRNIVRLLG-WCSNRNLKLLFY--DYLPNG 837
Cdd:cd07847     9 IGEGSYGVVFKCrNRETGQIVAIKKFVESEDDPVIKKialrEIRMLKQLKHPNLVNLIEvFRRKRKLHLVFEycDHTVLN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGagkggcVDWEARYDVVLGVAHALAYLH-HDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGI 916
Cdd:cd07847    89 ELEKNPRG------VPEHLIKKIIWQTLQAVNFCHkHNC----IHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYT 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  917 D-LAKPTNRPP--MAGSYGYMAPehasmqritekSDVYSYGVVLLEVLTGKhPLDP 969
Cdd:cd07847   159 DyVATRWYRAPelLVGDTQYGPP-----------VDVWAIGCVFAELLTGQ-PLWP 202
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
766-967 3.86e-12

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: 68.28  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKM-WSKEESGAFNS---EIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYLPNgSL 839
Cdd:cd07829     7 LGEGTYGVVYKAKdKKTGEIVALKKIrLDNEEEGIPSTalrEISLLKELKHPNIVKLLDvIHTENKLYLVF-EYCDQ-DL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHgagkggcvdwEARYDVVLGVA--------HALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgy 911
Cdd:cd07829    85 KKYLD----------KRPGPLPPNLIksimyqllRGLAYCHSHR---ILHRDLKPQNLLINRDGVLKLADFGLARAF--- 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  912 pntGIDLAKPTN-------RPP--MAGSYGYmapehasmqriTEKSDVYSYGVVLLEVLTGKhPL 967
Cdd:cd07829   149 ---GIPLRTYTHevvtlwyRAPeiLLGSKHY-----------STAVDIWSVGCIFAELITGK-PL 198
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
786-959 4.04e-12

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: 68.16  E-value: 4.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  786 AVKKMWSKEESGAFN---SEIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYLPNGSLSSRLHgAGKGGCVDWEARYdvV 861
Cdd:cd14046    35 AIKKIKLRSESKNNSrilREVMLLSRLNHQHVVRYYQaWIERANLYIQM-EYCEKSTLRDLID-SGLFQDTDRLWRL--F 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  862 LGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLA---RTISGYPNTGIDLAKPTNRPP------MAGSYG 932
Cdd:cd14046   111 RQILEGLAYIHSQ---GIIHRDLKPVNIFLDSNGNVKIGDFGLAtsnKLNVELATQDINKSTSAALGSsgdltgNVGTAL 187
                         170       180
                  ....*....|....*....|....*....
gi 240256081  933 YMAPEHAS--MQRITEKSDVYSYGVVLLE 959
Cdd:cd14046   188 YVAPEVQSgtKSTYNEKVDMYSLGIIFFE 216
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
765-966 4.32e-12

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 67.42  E-value: 4.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVKK-----MWSKEESGAFNsEIKTLGSIRHRNIVRLL-GWCSNRNLKLLFyDYLPNG 837
Cdd:cd08530     7 KLGKGSYGSVYKVKrLSDNQVYALKEvnlgsLSQKEREDSVN-EIRLLASVNHPNIIRYKeAFLDGNRLCIVM-EYAPFG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRL-HGAGKGGCVDWEARYDVVLGVAHALAYLHhDClpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgi 916
Cdd:cd08530    85 DLSKLIsKRKKKRRLFPEDDIWRIFIQMLRGLKALH-DQ--KILHRDLKSANILLSAGDLVKIGDLGISKVLKK------ 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  917 DLAKPTNRPPMagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd08530   156 NLAKTQIGTPL-----YAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPP 200
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
781-962 4.62e-12

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: 68.00  E-value: 4.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  781 SGESLAVKKMW--SKEESGAFNSEIKTLGSIRHRNIVRLLGWC---SNRNLKLLFyDYLPNGSLSsrlhgagkggcvDWE 855
Cdd:cd05081    32 TGALVAVKQLQhsGPDQQRDFQREIQILKALHSDFIVKYRGVSygpGRRSLRLVM-EYLPSGCLR------------DFL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  856 ARYDVVLGVAHALAYLHHDCLPTI-------IHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgIDLAKPTNRPPMA 928
Cdd:cd05081    99 QRHRARLDASRLLLYSSQICKGMEylgsrrcVHRDLAARNILVESEAHVKIADFGLAKLLP------LDKDYYVVREPGQ 172
                         170       180       190
                  ....*....|....*....|....*....|....
gi 240256081  929 GSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05081   173 SPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
765-966 4.95e-12

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: 67.38  E-value: 4.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGA---------FNSEIKTLGSI-RHRNIVRLLGWCSNRNLKLLFYDY 833
Cdd:cd13993     7 PIGEGAYGVVYLaVDLRTGRKYAIKCLYKSGPNSKdgndfqklpQLREIDLHRRVsRHPNIITLHDVFETEVAIYIVLEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSL----SSRLHGAGKGgcvdwEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEP-YLADFGLARTi 908
Cdd:cd13993    87 CPNGDLfeaiTENRIYVGKT-----ELIKNVFLQLIDAVKHCHSL---GIYHRDIKPENILLSQDEGTvKLCDFGLATT- 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  909 sgypntgidlaKPTNRPPMAGSYGYMAPEhasmqRITEK-----------SDVYSYGVVLLEVLTGKHP 966
Cdd:cd13993   158 -----------EKISMDFGVGSEFYMAPE-----CFDEVgrslkgypcaaGDIWSLGIILLNLTFGRNP 210
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
765-962 6.81e-12

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: 67.40  E-value: 6.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITI---PSG--ESLAVKkMWSKEESGAFNSE--IKTLGSIRHRNIVRLLGWCSNRNLK----LLFYDY 833
Cdd:cd14055     2 LVGKGRFAEVWKAKLkqnASGqyETVAVK-IFPYEEYASWKNEkdIFTDASLKHENILQFLTAEERGVGLdrqyWLITAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSLSSRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDCLPT------IIHGDVKAMNVLLGPHFEPYLADFGLA-- 905
Cdd:cd14055    81 HENGSLQDYL----TRHILSWEDLCKMAGSLARGLAHLHSDRTPCgrpkipIAHRDLKSSNILVKNDGTCVLADFGLAlr 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  906 ----RTISGYPNTGidlakptnrppMAGSYGYMAPEhASMQRIT-------EKSDVYSYGVVLLEVLT 962
Cdd:cd14055   157 ldpsLSVDELANSG-----------QVGTARYMAPE-ALESRVNledlesfKQIDVYSMALVLWEMAS 212
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
766-999 7.09e-12

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 67.46  E-value: 7.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMW---SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd06611    13 LGDGAFGKVYKAQHKETGLFAAAKIIqieSEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGALDSI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGKGgCVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLArtisgypntgidlAKPT 922
Cdd:cd06611    93 MLELERG-LTEPQIRY-VCRQMLEALNFLHSH---KVIHRDLKAGNILLTLDGDVKLADFGVS-------------AKNK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  923 N----RPPMAGSYGYMAPEHASMQRITE-----KSDVYSYGVVLLEvLTGKHPLDPDLPGGAHLVKwvrdhlAEKKDPSR 993
Cdd:cd06611   155 StlqkRDTFIGTPYWMAPEVVACETFKDnpydyKADIWSLGITLIE-LAQMEPPHHELNPMRVLLK------ILKSEPPT 227

                  ....*.
gi 240256081  994 LLDPRL 999
Cdd:cd06611   228 LDQPSK 233
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
765-968 7.63e-12

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: 66.91  E-value: 7.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIPSGESLAV------KKMWSKEESgAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd08225     7 KIGEGSFGKIYLAKAKSDSEHCVikeidlTKMPVKEKE-ASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRL---HGA--GKGGCVDWEARydVVLGVAHAlaylhHDclPTIIHGDVKAMNVLLGPH-FEPYLADFGLARTIsgyp 912
Cdd:cd08225    86 LMKRInrqRGVlfSEDQILSWFVQ--ISLGLKHI-----HD--RKILHRDIKSQNIFLSKNgMVAKLGDFGIARQL---- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  913 NTGIDLAKPTnrppmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd08225   153 NDSMELAYTC-----VGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFE 203
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
737-966 8.21e-12

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: 66.97  E-value: 8.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  737 EIDSWEVTLyqkldfsiddivKNLTSANVIGTGSSGVVYRITIPSGESLAVKKMWSKEES-GAFNSEIKTLGSIRHRNIV 815
Cdd:cd05073     2 EKDAWEIPR------------ESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSvEAFLAEANVMKTLQHDKLV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  816 RLLGWCSNRNLKLLfYDYLPNGSLSSRLHgAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHF 895
Cdd:cd05073    70 KLHAVVTKEPIYII-TEFMAKGSLLDFLK-SDEGSKQPLPKLIDFSAQIAEGMAFIEQR---NYIHRDLRAANILVSASL 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256081  896 EPYLADFGLARTISGYPNTGIDLAK-PTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05073   145 VCKIADFGLARVIEDNEYTAREGAKfPIK---------WTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIP 208
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
760-967 8.69e-12

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 67.93  E-value: 8.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFNS---EIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYL 834
Cdd:PLN00034   76 LERVNRIGSGAGGTVYKvIHRPTGRLYALKVIYGNHEDTVRRQicrEIEILRDVNHPNVVKCHDmFDHNGEIQVLL-EFM 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSsrlhgagkgGCVDWEARY--DVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgyp 912
Cdd:PLN00034  155 DGGSLE---------GTHIADEQFlaDVARQILSGIAYLHRR---HIVHRDIKPSNLLINSAKNVKIADFGVSRIL---- 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  913 NTGIDlakPTNRPpmAGSYGYMAPEhasmqRITEK----------SDVYSYGVVLLEVLTGKHPL 967
Cdd:PLN00034  219 AQTMD---PCNSS--VGTIAYMSPE-----RINTDlnhgaydgyaGDIWSLGVSILEFYLGRFPF 273
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
758-967 8.98e-12

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: 67.14  E-value: 8.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYR-ITIPSGESLAVKKMW-SKEESgafNSEIKTLGSIRHRNIVRLL------GWCSNRNLKLL 829
Cdd:cd14137     4 ISYTIEKVIGSGSFGVVYQaKLLETGEVVAIKKVLqDKRYK---NRELQIMRRLKHPNIVKLKyffyssGEKKDEVYLNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 FYDYLPNgSLSSRLHgagkggcvdWEARYDVVLGVAH----------ALAYLHHDClptIIHGDVKAMNVLLGPhfEPY- 898
Cdd:cd14137    81 VMEYMPE-TLYRVIR---------HYSKNKQTIPIIYvklysyqlfrGLAYLHSLG---ICHRDIKPQNLLVDP--ETGv 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  899 --LADFGLA-RTISGYPNTgidlakptnrppmagSY----GYMAPE---HAsmQRITEKSDVYSYGVVLLEVLTGKhPL 967
Cdd:cd14137   146 lkLCDFGSAkRLVPGEPNV---------------SYicsrYYRAPElifGA--TDYTTAIDIWSAGCVLAELLLGQ-PL 206
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
764-962 9.04e-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: 9.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIPSG---ESLAVKKM---WSKEESGAFNSEIKTLGSI-RHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:cd05088    13 DVIGEGNFGQVLKARIKKDglrMDAAIKRMkeyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGA-------------GKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd05088    93 GNLLDFLRKSrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQK---QFIHRDLAARNILVGENYVAKIADFG 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  904 LARTISGYpntgidLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05088   170 LSRGQEVY------VKKTMGRLPVR----WMAIESLNYSVYTTNSDVWSYGVLLWEIVS 218
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
786-962 1.01e-11

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: 66.98  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  786 AVKKM---WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLH-----GAGKGGCVDWEAR 857
Cdd:cd05051    50 AVKMLrpdASKNAREDFLKEVKIMSQLKDPNIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQkheaeTQGASATNSKTLS 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  858 YDVVLGVAHALA----YLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARtiSGYPNtgiDLAKPTNRPPMAgsYGY 933
Cdd:cd05051   130 YGTLLYMATQIAsgmkYLES---LNFVHRDLATRNCLVGPNYTIKIADFGMSR--NLYSG---DYYRIEGRAVLP--IRW 199
                         170       180
                  ....*....|....*....|....*....
gi 240256081  934 MAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05051   200 MAWESILLGKFTTKSDVWAFGVTLWEILT 228
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
765-963 1.14e-11

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: 66.13  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIpSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGwcSNRNLKLLFYDYLPNGSLSSRLH 844
Cdd:cd14068     1 LLGDGGFGSVYRAVY-RGEDVAVKIFNKHTSFRLLRQELVVLSHLHHPSLVALLA--AGTAPRMLVMELAPKGSLDALLQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 GagKGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLgphFEPY--------LADFGLARTISgypNTGI 916
Cdd:cd14068    78 Q--DNASLTRTLQHRIALHVADGLRYLHS---AMIIYRDLKPHNVLL---FTLYpncaiiakIADYGIAQYCC---RMGI 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  917 DLAKptnrppmaGSYGYMAPEHASMQRI-TEKSDVYSYGVVLLEVLTG 963
Cdd:cd14068   147 KTSE--------GTPGFRAPEVARGNVIyNQQADVYSFGLLLYDILTC 186
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
758-962 1.29e-11

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: 66.64  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRITI--PSGES----LAVK---KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKL 828
Cdd:cd05036     6 KNLTLIRALGQGAFGEVYEGTVsgMPGDPsplqVAVKtlpELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSSRLH----GAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL---GPHFEPYLAD 901
Cdd:cd05036    86 ILLELMAGGDLKSFLRenrpRPEQPSSLTMLDLLQLAQDVAKGCRYLEEN---HFIHRDIAARNCLLtckGPGRVAKIGD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  902 FGLARTI--SGYPNTGIDLAKPTNrppmagsygYMAPEhASMQRI-TEKSDVYSYGVVLLEVLT 962
Cdd:cd05036   163 FGMARDIyrADYYRKGGKAMLPVK---------WMPPE-AFLDGIfTSKTDVWSFGVLLWEIFS 216
PLN03150 PLN03150
hypothetical protein; Provisional
107-186 1.42e-11

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 68.69  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  107 GVIPKEIGDFTELELLDLSDNSLSGDIPVEIFRLKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGEIPRSIG 186
Cdd:PLN03150  432 GFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAALG 511
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
766-968 1.44e-11

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: 65.99  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRI-TIPSGESLAVK-----KMWSKEESGAfNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd08218     8 IGEGSFGKALLVkSKEDGKQYVIKeinisKMSPKEREES-RKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHgAGKG------GCVDWEARydVVLGVAHAlaylhHDclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypN 913
Cdd:cd08218    87 YKRIN-AQRGvlfpedQILDWFVQ--LCLALKHV-----HD--RKILHRDIKSQNIFLTKDGIIKLGDFGIARVL----N 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  914 TGIDLAKPTnrppmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd08218   153 STVELARTC-----IGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFE 202
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
766-966 1.89e-11

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: 65.79  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVV---YRITIPSGESLAVKK--MWSKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKL-LFYDYL 834
Cdd:cd13994     1 IGKGATSVVrivTKKNPRSGVLYAVKEyrRRDDESKRKdyvkrLTSEYIISSKLHHPNIVKVLDLCQDLHGKWcLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLHgagKGGCVDWEARYDVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPN 913
Cdd:cd13994    81 PGGDLFTLIE---KADSLSLEEKDCFFKQILRGVAYLHsHG----IAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  914 tgidlakptNRPPMA----GSYGYMAPEhaSMQRIT---EKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd13994   154 ---------KESPMSaglcGSEPYMAPE--VFTSGSydgRAVDVWSCGIVLFALFTGRFP 202
LRRNT_2 pfam08263
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
25-65 1.98e-11

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: 59.62  E-value: 1.98e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 240256081    25 LDQQGQALLSWKSQLNISGDAFSSWHVADTSPCNWVGVKCN 65
Cdd:pfam08263    1 LNDDGQALLAFKSSLNDPPGALSSWNSSSSDPCSWTGVTCD 41
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
766-966 2.10e-11

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: 65.78  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVY----RITIpsgESLAVKKMWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd14010     8 IGRGKHSVVYkgrrKGTI---EFVAIKCVDKSKRPEVLN-EVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLET 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHgagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLAR-------TISGYPNT 914
Cdd:cd14010    84 LLR---QDGNLPESSVRKFGRDLVRGLHYIHSK---GIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkELFGQFSD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  915 GIDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14010   158 EGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPP 209
PLN03150 PLN03150
hypothetical protein; Provisional
507-615 2.19e-11

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 67.92  E-value: 2.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  507 LDLHTNSLSGsLLGTTLPK--SLKFIDFSDNALSSTLPPGIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLLNLGEND 584
Cdd:PLN03150  423 LGLDNQGLRG-FIPNDISKlrHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNS 501
                          90       100       110
                  ....*....|....*....|....*....|.
gi 240256081  585 FSGEIPDELGQIPSLAISLNLSCNRFVGEIP 615
Cdd:PLN03150  502 LSGRVPAALGGRLLHRASFNFTDNAGLCGIP 532
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
788-962 2.62e-11

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: 65.82  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  788 KKMWSKEEsgafnsEIKTLGSIRHRNIVRLLGW---CSNRNLKL-LFYDYLPNGSLSSRLhgagKGGCVDWEARYDVVLG 863
Cdd:cd14140    31 KQSWQSER------EIFSTPGMKHENLLQFIAAekrGSNLEMELwLITAFHDKGSLTDYL----KGNIVSWNELCHIAET 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHDC--------LPTIIHGDVKAMNVLLGPHFEPYLADFGLA-RTISGYPntgidlakPTNRPPMAGSYGYM 934
Cdd:cd14140   101 MARGLSYLHEDVprckgeghKPAIAHRDFKSKNVLLKNDLTAVLADFGLAvRFEPGKP--------PGDTHGQVGTRRYM 172
                         170       180       190
                  ....*....|....*....|....*....|...
gi 240256081  935 APE----HASMQRIT-EKSDVYSYGVVLLEVLT 962
Cdd:cd14140   173 APEvlegAINFQRDSfLRIDMYAMGLVLWELVS 205
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
766-970 2.92e-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: 65.64  E-value: 2.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMWSKEESGAFNSEIKTLgSIRHR----NIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd06622     9 LGKGNYGSVYKVLhRPTGVTMAMKEIRLELDESKFNQIIMEL-DILHKavspYIVDFYGAFFIEGAVYMCMEYMDAGSLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDclPTIIHGDVKAMNVLLGPHFEPYLADFGlartISGypNTGIDLAK 920
Cdd:cd06622    88 KLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEE--HNIIHRDVKPTNVLVNGNGQVKLCDFG----VSG--NLVASLAK 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  921 pTNrppmAGSYGYMAPEHASMQRITE------KSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd06622   160 -TN----IGCQSYMAPERIKSGGPNQnptytvQSDVWSLGLSILEMALGRYPYPPE 210
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
766-977 3.02e-11

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: 65.80  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFN----SEIKTLGSIRHRNIVRLLGWCSNR-----NLKLLFYDYLP 835
Cdd:cd07866    16 LGEGTFGEVYKaRQIKTGRVVALKKILMHNEKDGFPitalREIKILKKLKHPNVVPLIDMAVERpdkskRKRGSVYMVTP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 --NGSLSSRLHGAgkggcvdwearyDVVLGVAHA----------LAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd07866    96 ymDHDLSGLLENP------------SVKLTESQIkcymlqllegINYLHEN---HILHRDIKAANILIDNQGILKIADFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  904 LARTISGYPntgidlAKPTNRPPMAG-SYG-------YMAPEH-ASMQRITEKSDVYSYGVVLLEVLTGKhpldPDLPGG 974
Cdd:cd07866   161 LARPYDGPP------PNPKGGGGGGTrKYTnlvvtrwYRPPELlLGERRYTTAVDIWGIGCVFAEMFTRR----PILQGK 230

                  ...
gi 240256081  975 AHL 977
Cdd:cd07866   231 SDI 233
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
758-970 3.96e-11

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: 65.14  E-value: 3.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRITIPSGESLAVKKMWSKEESGAFNS----EIKTLGSIRHRNIVRLLGWCSNR---NLKLLF 830
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKqilrELEINKSCASPYIVKYYGAFLDEqdsSIGIAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 yDYLPNGSLSSRLHGA-GKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGlartIS 909
Cdd:cd06621    81 -EYCEGGSLDSIYKKVkKKGGRIGEKVLGKIAESVLKGLSYLHSR---KIIHRDIKPSNILLTRKGQVKLCDFG----VS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  910 GypNTGIDLAKPtnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd06621   153 G--ELVNSLAGT-----FTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPE 206
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
758-1036 4.04e-11

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 64.52  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRITIPSGESLAVKKMwsKEESGA---FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:cd05113     4 KDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMI--KEGSMSedeFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLHGAGKGgcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNT 914
Cdd:cd05113    82 ANGCLLNYLREMRKR--FQTQQLLEMCKDVCEAMEYLESK---QFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  915 GIDLAKPTNRppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLdpDLPGGAHLVkwvrDHLAEKKdpsR 993
Cdd:cd05113   157 SSVGSKFPVR--------WSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPY--ERFTNSETV----EHVSQGL---R 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 240256081  994 LLDPRLDGRTdsimhemlqTLAVAFLCVSNKANERPLMKDVVA 1036
Cdd:cd05113   220 LYRPHLASEK---------VYTIMYSCWHEKADERPTFKILLS 253
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
766-966 4.27e-11

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: 64.91  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMWSKE-ESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLkLLFYDYLPNGSLSSRLH 844
Cdd:cd05067    15 LGAGQFGEVWMGYYNGHTKVAIKSLKQGSmSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPI-YIITEYMENGSLVDFLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 gAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDLAK-PTN 923
Cdd:cd05067    94 -TPSGIKLTINKLLDMAAQIAEGMAFIEER---NYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKfPIK 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 240256081  924 rppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05067   170 ---------WTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIP 204
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
751-967 4.32e-11

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: 65.44  E-value: 4.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  751 FSIDDIVKNLTSANVIGTGSSGVVYRITIP-SGESLAVKKM-----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNR 824
Cdd:cd06633    14 FYKDDPEEIFVDLHEIGHGSFGAVYFATNShTNEVVAIKKMsysgkQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  825 NLKLLFYDYLPnGSLSSRLHGAGKG-GCVDWEArydVVLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd06633    94 HTAWLVMEYCL-GSASDLLEVHKKPlQEVEIAA---ITHGALQGLAYLHSHNM---IHRDIKAGNILLTEPGQVKLADFG 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  904 LArtisgypntgiDLAKPTNRppMAGSYGYMAPE---HASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06633   167 SA-----------SIASPANS--FVGTPYWMAPEvilAMDEGQYDGKVDIWSLGITCIELAERKPPL 220
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
765-966 4.69e-11

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: 64.93  E-value: 4.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVK----KMWSKEESGAF-NSEIKTLGSIRHRNIVRLlgWCSNRNLKLLFY--DYLPN 836
Cdd:cd05581     8 PLGEGSYSTVVLAKeKETGKEYAIKvldkRHIIKEKKVKYvTIEKEVLSRLAHPGIVKL--YYTFQDESKLYFvlEYAPN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHgagKGGCVDWE-ARYdVVLGVAHALAYLHhdcLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTI-SGYPNT 914
Cdd:cd05581    86 GDLLEYIR---KYGSLDEKcTRF-YTAEIVLALEYLH---SKGIIHRDLKPENILLDEDMHIKITDFGTAKVLgPDSSPE 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  915 GIDLAKPTNRPPM-------AGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd05581   159 STKGDADSQIAYNqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPP 217
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
764-970 4.89e-11

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: 64.50  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd14186     7 NLLGKGSFACVYRaRSLHTGLEVAIKMIDKKAMQKAgmvqrVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGKGGCVDwEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLArtisgypntgID 917
Cdd:cd14186    87 EMSRYLKNRKKPFTED-EARH-FMHQIVTGMLYLHSH---GILHRDLTLSNLLLTRNMNIKIADFGLA----------TQ 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  918 LAKPTNRP-PMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14186   152 LKMPHEKHfTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTD 205
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
764-1040 4.93e-11

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: 64.75  E-value: 4.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR---ITIP---SGES-LAVK---KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDY 833
Cdd:cd05044     1 KFLGSGAFGEVFEgtaKDILgdgSGETkVAVKtlrKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSLSSRLHGAGKggcvdwEARY----------DVVLGVAHALAYLH--HdclptIIHGDVKAMNVLL---GPHFEPY 898
Cdd:cd05044    81 MEGGDLLSYLRAARP------TAFTpplltlkdllSICVDVAKGCVYLEdmH-----FVHRDLAARNCLVsskDYRERVV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  899 -LADFGLARTISG---YPNTGIDLAkPTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPldpdLPG 973
Cdd:cd05044   150 kIGDFGLARDIYKndyYRKEGEGLL-PVR---------WMAPESLVDGVFTTQSDVWAFGVLMWEILTlGQQP----YPA 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  974 GAHLvkwvrDHLAEKKDPSRLLDPrlDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAMLTE 1040
Cdd:cd05044   216 RNNL-----EVLHFVRAGGRLDQP--DNCPDDLYELMLR-------CWSTDPEERPSFARILEQLQN 268
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
758-966 6.24e-11

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: 64.11  E-value: 6.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRIT-IPSGESLAVKKMwSKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFY 831
Cdd:cd14097     1 KIYTFGRKLGQGSFGVVIEAThKETQTKWAIKKI-NREKAGSsavklLEREVDILKHVNHAHIIHLEEVFETPKRMYLVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLPNGSLSSRLHGagKGGCVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPH-FEP------YLADFGL 904
Cdd:cd14097    80 ELCEDGELKELLLR--KGFFSENETRH-IIQSLASAVAYLHKN---DIVHRDLKLENILVKSSiIDNndklniKVTDFGL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  905 ARTISGypnTGIDLAKPTNRPPMagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14097   154 SVQKYG---LGEDMLQETCGTPI-----YMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPP 207
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
801-972 6.85e-11

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: 64.65  E-value: 6.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  801 SEIKTLGSI-RHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGGCvdwEARYDV----------------VLG 863
Cdd:cd05101    78 SEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGM---EYSYDInrvpeeqmtfkdlvscTYQ 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYL-HHDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgIDLAKPTN--RPPMAgsygYMAPEHAS 940
Cdd:cd05101   155 LARGMEYLaSQKC----IHRDLAARNVLVTENNVMKIADFGLARDINN-----IDYYKKTTngRLPVK----WMAPEALF 221
                         170       180       190
                  ....*....|....*....|....*....|...
gi 240256081  941 MQRITEKSDVYSYGVVLLEVLT-GKHPLdPDLP 972
Cdd:cd05101   222 DRVYTHQSDVWSFGVLMWEIFTlGGSPY-PGIP 253
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
781-1043 7.01e-11

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: 64.54  E-value: 7.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  781 SGESLAVKKMwsKEESGAFNS-----EIKTLGSIRHRNIVRLLGWCSNRNLK--LLFYDYLPNGSLssrlhgagkggcVD 853
Cdd:cd05080    32 TGEMVAVKAL--KADCGPQHRsgwkqEIDILKTLYHENIVKYKGCCSEQGGKslQLIMEYVPLGSL------------RD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  854 WEARYDVVLG--------VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISG---YPNTGIDLAKPT 922
Cdd:cd05080    98 YLPKHSIGLAqlllfaqqICEGMAYLHSQ---HYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEgheYYRVREDGDSPV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  923 NrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP-LDP-----DLPGGAH-LVKWVR-DHLAEKKDpsRL 994
Cdd:cd05080   175 F---------WYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSsQSPptkflEMIGIAQgQMTVVRlIELLERGE--RL 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 240256081  995 ldPRLDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAMLTEIRH 1043
Cdd:cd05080   244 --PCPDKCPQEVYHLMKN-------CWETEASFRPTFENLIPILKTVHE 283
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
802-973 7.42e-11

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: 63.73  E-value: 7.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGgCVDwEARyDVVLGVAHALAYLHHDclpTIIH 881
Cdd:cd14164    50 ELSILRRVNHPNIVQMFECIEVANGRLYIVMEAAATDLLQKIQEVHHI-PKD-LAR-DMFAQMVGAVNYLHDM---NIVH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  882 GDVKAMNVLLGPHFEPY-LADFGLARTISGYPntgiDLAKPtnrppMAGSYGYMAPEH-ASMQRITEKSDVYSYGVVLLE 959
Cdd:cd14164   124 RDLKCENILLSADDRKIkIADFGFARFVEDYP----ELSTT-----FCGSRAYTPPEViLGTPYDPKKYDVWSLGVVLYV 194
                         170
                  ....*....|....
gi 240256081  960 VLTGKHPLDPDLPG 973
Cdd:cd14164   195 MVTGTMPFDETNVR 208
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
785-966 7.43e-11

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: 64.29  E-value: 7.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  785 LAVKKMWSKEESGA--FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGGCVDWEARYDVVL 862
Cdd:cd05093    38 VAVKTLKDASDNARkdFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNRPAEL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  863 G----------VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI--SGYPNTGIDLAKPTNrppmags 930
Cdd:cd05093   118 TqsqmlhiaqqIAAGMVYLASQ---HFVHRDLATRNCLVGENLLVKIGDFGMSRDVysTDYYRVGGHTMLPIR------- 187
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 240256081  931 ygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05093   188 --WMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQP 222
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
766-973 1.01e-10

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: 64.13  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFNS-------EIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYLPN 836
Cdd:cd07841     8 LGEGTYAVVYKaRDKETGRIVAIKKIKLGERKEAKDGinftalrEIKLLQELKHPNIIGLLDvFGHKSNINLVF-EFMET 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 gslssrlhgagkggcvDWEA---RYDVVLGVAH----------ALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd07841    87 ----------------DLEKvikDKSIVLTPADiksymlmtlrGLEYLHSN---WILHRDLKPNNLLIASDGVLKLADFG 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256081  904 LARTIsGYPNtgidlakpTNRPPMAGSYGYMAPE---HASMqrITEKSDVYSYGVVLLEVLTGKhpldPDLPG 973
Cdd:cd07841   148 LARSF-GSPN--------RKMTHQVVTRWYRAPEllfGARH--YGVGVDMWSVGCIFAELLLRV----PFLPG 205
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
765-970 1.09e-10

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: 63.59  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVK-----KMWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRN-----LKLLFYDY 833
Cdd:cd14082    10 VLGSGQFGIVYGgKHRKTGRDVAIKvidklRFPTKQESQLRN-EVAILQQLSHPGVVNLECMFETPErvfvvMEKLHGDM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 L------PNGSLSSRLhgagkggcvdweARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHfEPY----LADFG 903
Cdd:cd14082    89 LemilssEKGRLPERI------------TKF-LVTQILVALRYLHSK---NIVHCDLKPENVLLASA-EPFpqvkLCDFG 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  904 LARTIsgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14082   152 FARII----------GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED 208
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
787-966 1.16e-10

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 63.49  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  787 VKKMWSKEESGAF----NSEIKTLGSIRHRNIVRL--------------LGWCSNRNLKLLFYDylpNGSLSSRlhgagk 848
Cdd:cd13990    35 LNKDWSEEKKQNYikhaLREYEIHKSLDHPRIVKLydvfeidtdsfctvLEYCDGNDLDFYLKQ---HKSIPER------ 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  849 ggcvdwEARYdVVLGVAHALAYLHhDCLPTIIHGDVKAMNVLLG---PHFEPYLADFGLARTISG--YPNTGIDLAKPTn 923
Cdd:cd13990   106 ------EARS-IIMQVVSALKYLN-EIKPPIIHYDLKPGNILLHsgnVSGEIKITDFGLSKIMDDesYNSDGMELTSQG- 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 240256081  924 rppmAGSYGYMAPE----HASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd13990   177 ----AGTYWYLPPEcfvvGKTPPKISSKVDVWSVGVIFYQMLYGRKP 219
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
764-972 1.18e-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: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVY--RITIPSGESLAVKKMWSKEESGA---FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd14201    12 DLVGHGAFAVVFkgRHRKKTDWEVAIKSINKKNLSKSqilLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGAGKGGcvdwEARYDVVL-GVAHALAYLHHDclpTIIHGDVKAMNVLLG---------PHFEPYLADFGLARti 908
Cdd:cd14201    92 LADYLQAKGTLS----EDTIRVFLqQIAAAMRILHSK---GIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFAR-- 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  909 sgYPNTGIDLAKptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLP 972
Cdd:cd14201   163 --YLQSNMMAAT------LCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSP 218
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
766-972 1.18e-10

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: 63.27  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVY----RITipsGESLAVK-----KMWSKEESGAFNSEIKTLGSIRHR-NIVRLLGWCSNRNLKLLFYDYLP 835
Cdd:cd05611     4 ISKGAFGSVYlakkRST---GDYFAIKvlkksDMIAKNQVTNVKAERAIMMIQGESpYVAKLYYSFQSKDYLYLVMEYLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGAGkGGCVDWEARY--DVVLGVAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARtisgypn 913
Cdd:cd05611    81 GGDCASLIKTLG-GLPEDWAKQYiaEVVLGVED----LHQR---GIIHRDIKPENLLIDQTGHLKLTDFGLSR------- 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  914 tgIDLAKPTNrPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLP 972
Cdd:cd05611   146 --NGLEKRHN-KKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETP 201
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
766-969 1.32e-10

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: 63.51  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMW---SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd06644    20 LGDGAFGKVYKAKNKETGALAAAKVIetkSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAVDAI 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGKGGCvdwEARYDVVL-GVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgypntgiDLAKP 921
Cdd:cd06644   100 MLELDRGLT---EPQIQVICrQMLEALQYLHSM---KIIHRDLKAGNVLLTLDGDIKLADFGVSAK---------NVKTL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  922 TNRPPMAGSYGYMAPEHASMQRITE-----KSDVYSYGVVLLE---VLTGKHPLDP 969
Cdd:cd06644   165 QRRDSFIGTPYWMAPEVVMCETMKDtpydyKADIWSLGITLIEmaqIEPPHHELNP 220
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
785-962 1.34e-10

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: 63.84  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  785 LAVKKMWSKEESGAFN---SEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS---------SRLHGAGKGGCV 852
Cdd:cd05097    47 VAVKMLRADVTKTARNdflKEIKIMSRLKNPNIIRLLGVCVSDDPLCMITEYMENGDLNqflsqreieSTFTHANNIPSV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  853 DWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTI-SGypntgiDLAKPTNRPPMagSY 931
Cdd:cd05097   127 SIANLLYMAVQIASGMKYLAS---LNFVHRDLATRNCLVGNHYTIKIADFGMSRNLySG------DYYRIQGRAVL--PI 195
                         170       180       190
                  ....*....|....*....|....*....|.
gi 240256081  932 GYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05097   196 RWMAWESILLGKFTTASDVWAFGVTLWEMFT 226
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
765-968 1.37e-10

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: 63.89  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVK---KMWSKEESGAFNSEI----KTLGSIRHRNIVRLLGWCSNRNLKLLfYDYLPN 836
Cdd:cd05108    14 VLGSGAFGTVYKgLWIPEGEKVKIPvaiKELREATSPKANKEIldeaYVMASVDNPHVCRLLGICLTSTVQLI-TQLMPF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGGCVDWEARYDVvlGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLARTISG----YP 912
Cdd:cd05108    93 GCLLDYVREHKDNIGSQYLLNWCV--QIAKGMNYLEDRRL---VHRDLAARNVLVKTPQHVKITDFGLAKLLGAeekeYH 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  913 NTGidlakptNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLD 968
Cdd:cd05108   168 AEG-------GKVPIK----WMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYD 213
PLN03150 PLN03150
hypothetical protein; Provisional
394-500 1.67e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 65.22  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  394 LTGNIPQSLSQCRELQAIDLSYNSLSGSIPkeifglrnltkllllsndlsgfipPDIGNCTNLYRLRLNGNRLAGSIPSE 473
Cdd:PLN03150  430 LRGFIPNDISKLRHLQSINLSGNSIRGNIP------------------------PSLGSITSLEVLDLSYNSFNGSIPES 485
                          90       100
                  ....*....|....*....|....*..
gi 240256081  474 IGNLKNLNFVDISENRLVGSIPPAISG 500
Cdd:PLN03150  486 LGQLTSLRILNLNGNSLSGRVPAALGG 512
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
766-969 1.77e-10

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: 63.54  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRN---IVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd06650    13 LGAGNGGVVFKVShKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNspyIVGFYGAFYSDGEISICMEHMDGGSLDQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGAGKggcVDWEARYDVVLGVAHALAYLHHDclPTIIHGDVKAMNVLLGPHFEPYLADFGLA-RTISGYPNTgidlak 920
Cdd:cd06650    93 VLKKAGR---IPEQILGKVSIAVIKGLTYLREK--HKIMHRDVKPSNILVNSRGEIKLCDFGVSgQLIDSMANS------ 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 240256081  921 ptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDP 969
Cdd:cd06650   162 ------FVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPP 204
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
766-1007 1.90e-10

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: 63.12  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITI-PSGESLAVKKMWSKEESGA---FNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd06657    28 IGEGSTGIVCIATVkSSGKLVAVKKMDLRKQQRRellFN-EVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGAGkggcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgidlAKP 921
Cdd:cd06657   107 IVTHTR----MNEEQIAAVCLAVLKALSVLHAQ---GVIHRDIKSDSILLTHDGRVKLSDFGFCAQVS---------KEV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  922 TNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAhlVKWVRDHLAEKKDPSRLLDPRLDG 1001
Cdd:cd06657   171 PRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKA--MKMIRDNLPPKLKNLHKVSPSLKG 248

                  ....*.
gi 240256081 1002 RTDSIM 1007
Cdd:cd06657   249 FLDRLL 254
PLN03150 PLN03150
hypothetical protein; Provisional
199-285 1.94e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 64.84  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  199 NKNLRGELPWEIGNCENLVMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLYQNSISGSI 278
Cdd:PLN03150  427 NQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRV 506

                  ....*..
gi 240256081  279 PTTIGGL 285
Cdd:PLN03150  507 PAALGGR 513
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
766-967 1.97e-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: 62.74  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRI-TIPSGESLAVK--KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd06646    17 VGSGTYGDVYKArNLHTGELAAVKiiKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQDI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGKggCVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgidlAKPT 922
Cdd:cd06646    97 YHVTGP--LSELQIAY-VCRETLQGLAYLHSK---GKMHRDIKGANILLTDNGDVKLADFGVAAKIT---------ATIA 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  923 NRPPMAGSYGYMAPEHASMQR---ITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06646   162 KRKSFIGTPYWMAPEVAAVEKnggYNQLCDIWAVGITAIELAELQPPM 209
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
781-962 1.99e-10

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: 63.02  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  781 SGESLAVKKMwsKEESGAFNS-----EIKTLGSIRHRNIVRLLGWCSN---RNLKLLFyDYLPNGSLSSRLHGAGKGGCV 852
Cdd:cd05079    32 TGEQVAVKSL--KPESGGNHIadlkkEIEILRNLYHENIVKYKGICTEdggNGIKLIM-EFLPSGSLKEYLPRNKNKINL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  853 DWEARYDVvlGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS---GYPNTGIDLAKPTNrppmag 929
Cdd:cd05079   109 KQQLKYAV--QICKGMDYLGSR---QYVHRDLAARNVLVESEHQVKIGDFGLTKAIEtdkEYYTVKDDLDSPVF------ 177
                         170       180       190
                  ....*....|....*....|....*....|...
gi 240256081  930 sygYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05079   178 ---WYAPECLIQSKFYIASDVWSFGVTLYELLT 207
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
764-966 2.03e-10

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: 62.66  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVV----YRITipsGESLAVKKMwSKE---ESGAFNS---EIKTLGSIRHRNIVRLlgW---CSNRNLKLLF 830
Cdd:cd05578     6 RVIGKGSFGKVcivqKKDT---KKMFAMKYM-NKQkciEKDSVRNvlnELEILQELEHPFLVNL--WysfQDEEDMYMVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 yDYLPNGSLssRLHgAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARtisg 910
Cdd:cd05578    80 -DLLLGGDL--RYH-LQQKVKFSEETVKFYICEIVLALDYLHSK---NIIHRDIKPDNILLDEQGHVHITDFNIAT---- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  911 ypntgiDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd05578   149 ------KLTDGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRP 198
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
766-999 2.09e-10

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: 63.08  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVV-YRITIPSGESLAVKKMWSKEESGA---FNsEIKTLGSIRHRNIVRLL-GWCSNRNLKLLFyDYLPNGSLS 840
Cdd:cd06659    29 IGEGSTGVVcIAREKHSGRQVAVKMMDLRKQQRRellFN-EVVIMRDYQHPNVVEMYkSYLVGEELWVLM-EYLQGGALT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAGKGGcvdwEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgiDLAK 920
Cdd:cd06659   107 DIVSQTRLNE----EQIATVCEAVLQALAYLHSQ---GVIHRDIKSDSILLTLDGRVKLSDFGFCAQISK------DVPK 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  921 ptnRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAhlVKWVRDHLAEKKDPSRLLDPRL 999
Cdd:cd06659   174 ---RKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQA--MKRLRDSPPPKLKNSHKASPVL 247
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
799-966 2.19e-10

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: 63.11  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  799 FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS--RLHGAGKGGCVDWEAR-----------YDVVLGVA 865
Cdd:cd05094    54 FQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMKHGDLNKflRAHGPDAMILVDGQPRqakgelglsqmLHIATQIA 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  866 HALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI--SGYPNTGIDLAKPTNrppmagsygYMAPEHASMQR 943
Cdd:cd05094   134 SGMVYLASQ---HFVHRDLATRNCLVGANLLVKIGDFGMSRDVysTDYYRVGGHTMLPIR---------WMPPESIMYRK 201
                         170       180
                  ....*....|....*....|....
gi 240256081  944 ITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05094   202 FTTESDVWSFGVILWEIFTyGKQP 225
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
880-1041 2.53e-10

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: 63.48  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  880 IHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLE 959
Cdd:cd14207   202 IHRDLAARNILLSENNVVKICDFGLARDIYKNPDY---VRKGDARLPLK----WMAPESIFDKIYSTKSDVWSYGVLLWE 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  960 VLT-GKHPldpdLPGgahlVKWVRDHLAEKKDPSRLLDPrlDGRTDSIMHEMLQtlavaflCVSNKANERPLMKDVVAML 1038
Cdd:cd14207   275 IFSlGASP----YPG----VQIDEDFCSKLKEGIRMRAP--EFATSEIYQIMLD-------CWQGDPNERPRFSELVERL 337

                  ...
gi 240256081 1039 TEI 1041
Cdd:cd14207   338 GDL 340
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
766-961 2.61e-10

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: 62.53  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP-SGESLAVKKMW----SKEESGAFNSEIKTLGSIRHRNIV-----------------------RL 817
Cdd:cd14049    14 LGKGGYGKVYKVRNKlDGQYYAIKKILikkvTKRDCMKVLREVKVLAGLQHPNIVgyhtawmehvqlmlyiqmqlcelSL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  818 LGWCSNRNLKLLFYDYlpngslSSRLHGagkggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL-GPHFE 896
Cdd:cd14049    94 WDWIVERNKRPCEEEF------KSAPYT-----PVDVDVTTKILQQLLEGVTYIHSM---GIVHRDLKPRNIFLhGSDIH 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  897 PYLADFGLARTISGYPNTGIDLAKPTNRPPMAGSYG---YMAPEHASMQRITEKSDVYSYGVVLLEVL 961
Cdd:cd14049   160 VRIGDFGLACPDILQDGNDSTTMSRLNGLTHTSGVGtclYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
779-970 2.66e-10

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: 62.27  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  779 IPSGESlAVKKmwskeesgafnsEIKTLGSIRHRNIVRLLGWCSNRN-LKL-LFYDYLpNGSLSSRLHGAGKGGCVDWEA 856
Cdd:cd14119    34 IPNGEA-NVKR------------EIQILRRLNHRNVIKLVDVLYNEEkQKLyMVMEYC-VGGLQEMLDSAPDKRLPIWQA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  857 -RYDVVLgvAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYpnTGIDLAKPTNrppmaGSYGYMA 935
Cdd:cd14119   100 hGYFVQL--IDGLEYLHSQG---IIHKDIKPGNLLLTTDGTLKISDFGVAEALDLF--AEDDTCTTSQ-----GSPAFQP 167
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 240256081  936 PEHASMQRITE--KSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14119   168 PEIANGQDSFSgfKVDIWSAGVTLYNMTTGKYPFEGD 204
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
766-969 3.00e-10

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: 62.35  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFNS----EIKTLGSIR-HRNIVRLLGWCSNRNLKLLFYDYLPnGSL 839
Cdd:cd07832     8 IGEGAHGIVFKaKDRETGETVALKKVALRKLEGGIPNqalrEIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYML-SSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHGAGKGGCVDWEARYDVVL--GVAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgid 917
Cdd:cd07832    87 SEVLRDEERPLTEAQVKRYMRMLlkGVAY----MHAN---RIMHRDLKPANLLISSTGVLKIADFGLARLFS-------- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  918 laKPTNRP--PMAGSYGYMAPE--HASmQRITEKSDVYSYGVVLLEVLTGKhPLDP 969
Cdd:cd07832   152 --EEDPRLysHQVATRWYRAPEllYGS-RKYDEGVDLWAVGCIFAELLNGS-PLFP 203
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
760-971 3.01e-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: 62.35  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYR-ITIPSGESLAVK---KMWSKEESGAFNSEI----KTLGSIRHRNIVRLLGWCSNRNLKLLfY 831
Cdd:cd05109     9 LKKVKVLGSGAFGTVYKgIWIPDGENVKIPvaiKVLRENTSPKANKEIldeaYVMAGVGSPYVCRLLGICLTSTVQLV-T 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLPNGSLSSRLHG----AGKGGCVDWearydvVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLART 907
Cdd:cd05109    88 QLMPYGCLLDYVREnkdrIGSQDLLNW------CVQIAKGMSYLEE---VRLVHRDLAARNVLVKSPNHVKITDFGLARL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  908 I----SGYPNTGidlakptNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLD-------PDL 971
Cdd:cd05109   159 LdideTEYHADG-------GKVPIK----WMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDgipareiPDL 223
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
788-960 3.21e-10

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: 62.37  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  788 KKMWSKEesgafnSEIKTLGSIRHRNIVRLLGW---CSNRNLKL-LFYDYLPNGSLSSRLhgagKGGCVDWEARYDVVLG 863
Cdd:cd14141    31 KLSWQNE------YEIYSLPGMKHENILQFIGAekrGTNLDVDLwLITAFHEKGSLTDYL----KANVVSWNELCHIAQT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHDC-------LPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGidlakptNRPPMAGSYGYMAP 936
Cdd:cd14141   101 MARGLAYLHEDIpglkdghKPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAG-------DTHGQVGTRRYMAP 173
                         170       180
                  ....*....|....*....|....*....
gi 240256081  937 E----HASMQRIT-EKSDVYSYGVVLLEV 960
Cdd:cd14141   174 EvlegAINFQRDAfLRIDMYAMGLVLWEL 202
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
766-966 3.57e-10

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: 61.86  E-value: 3.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKM-------WSKEESgaFNSEIKTLGSIRHRNIVRLlgWCSNRNLKLLFY--DYLP 835
Cdd:cd05572     1 LGVGGFGRVELVQlKSKGRTFALKCVkkrhivqTRQQEH--IFSEKEILEECNSPFIVKL--YRTFKDKKYLYMlmEYCL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGAGKGGcvDWEARY---DVVLgvahALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYP 912
Cdd:cd05572    77 GGELWTILRDRGLFD--EYTARFytaCVVL----AFEYLHSR---GIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGR 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  913 NTGIdlakptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd05572   148 KTWT----------FCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPP 191
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
792-961 4.06e-10

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: 62.26  E-value: 4.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  792 SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRL-------------HGAGKGGC---VDWE 855
Cdd:cd05096    59 NKNARNDFLKEVKILSRLKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLsshhlddkeengnDAVPPAHClpaISYS 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  856 ARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgYPNtgiDLAKPTNRPPMagSYGYMA 935
Cdd:cd05096   139 SLLHVALQIASGMKYLSS---LNFVHRDLATRNCLVGENLTIKIADFGMSRNL--YAG---DYYRIQGRAVL--PIRWMA 208
                         170       180
                  ....*....|....*....|....*.
gi 240256081  936 PEHASMQRITEKSDVYSYGVVLLEVL 961
Cdd:cd05096   209 WECILMGKFTTASDVWAFGVTLWEIL 234
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
765-967 4.40e-10

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: 61.93  E-value: 4.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVKKM---WSKEESgaFNSEIKTLGSI-RHRNIVRLLGWC-----SNRNLKL-LFYDY 833
Cdd:cd06608    13 VIGEGTYGKVYKARhKKTGQLAAIKIMdiiEDEEEE--IKLEINILRKFsNHPNIATFYGAFikkdpPGGDDQLwLVMEY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGS---LSSRLHGAGKGGCVDWEArYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLAR---T 907
Cdd:cd06608    91 CGGGSvtdLVKGLRKKGKRLKEEWIA-Y-ILRETLRGLAYLHEN---KVIHRDIKGQNILLTEEAEVKLVDFGVSAqldS 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  908 ISGYPNTGIdlakptnrppmaGSYGYMAPEH-ASMQR----ITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06608   166 TLGRRNTFI------------GTPYWMAPEViACDQQpdasYDARCDVWSLGITAIELADGKPPL 218
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
765-1037 4.81e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 63.35  E-value: 4.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSG-VVYRITIPSGESLAVKKM----WSKEESGAFNSEIKTLGSIRHRNIVRL---LGWCSNRN-----LKLLFY 831
Cdd:PTZ00283   39 VLGSGATGtVLCAKRVSDGEPFAVKVVdmegMSEADKNRAQAEVCCLLNCDFFSIVKChedFAKKDPRNpenvlMIALVL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLPNGSLSSRLHGAGKGGCVDWEarYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgY 911
Cdd:PTZ00283  119 DYANAGDLRQEIKSRAKTNRTFRE--HEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKM---Y 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  912 PNTGIDLAKPTnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDpdlpgGAHLVKWVRDHLAEKKDP 991
Cdd:PTZ00283  194 AATVSDDVGRT----FCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFD-----GENMEEVMHKTLAGRYDP 264
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 240256081  992 srlldprldgRTDSIMHEMlQTLAVAFLCVSNKAneRPLMKDVVAM 1037
Cdd:PTZ00283  265 ----------LPPSISPEM-QEIVTALLSSDPKR--RPSSSKLLNM 297
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
801-972 4.83e-10

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: 62.29  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  801 SEIKTLGSI-RHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGGC-------------VDWEARYDVVLGVAH 866
Cdd:cd05099    66 SEMELMKLIgKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPdytfditkvpeeqLSFKDLVSCAYQVAR 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  867 ALAYLH-HDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgIDLAKPTN--RPPMAgsygYMAPEhASMQR 943
Cdd:cd05099   146 GMEYLEsRRC----IHRDLAARNVLVTEDNVMKIADFGLARGVHD-----IDYYKKTSngRLPVK----WMAPE-ALFDR 211
                         170       180       190
                  ....*....|....*....|....*....|.
gi 240256081  944 I-TEKSDVYSYGVVLLEVLT-GKHPLdPDLP 972
Cdd:cd05099   212 VyTHQSDVWSFGILMWEIFTlGGSPY-PGIP 241
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
765-970 5.41e-10

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: 61.40  E-value: 5.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIPSGESLAVKKMWSKEESG--AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd14087     8 LIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGreVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGELFDR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LhgAGKGGCVDWEARyDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLL---GPHFEPYLADFGLARTISGYPNtgiDLA 919
Cdd:cd14087    88 I--IAKGSFTERDAT-RVLQMVLDGVKYLHG---LGITHRDLKPENLLYyhpGPDSKIMITDFGLASTRKKGPN---CLM 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  920 KPTnrppmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14087   159 KTT-----CGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDD 204
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
766-967 5.61e-10

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: 61.31  E-value: 5.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKM-----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPnGSL 839
Cdd:cd06607     9 IGHGSFGAVYYARnKRTSEVVAIKKMsysgkQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYCL-GSA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHGAGKGgcvdweARYDVVLGVAH----ALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntg 915
Cdd:cd06607    88 SDIVEVHKKP------LQEVEIAAICHgalqGLAYLHSHNR---IHRDVKAGNILLTEPGTVKLADFGSASLVC------ 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  916 idlakPTNRppMAGSYGYMAPEHA-SMQ--RITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06607   153 -----PANS--FVGTPYWMAPEVIlAMDegQYDGKVDVWSLGITCIELAERKPPL 200
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
756-967 5.64e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 63.11  E-value: 5.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  756 IVKNLTSANviGTGSSGVVYRITIPSGESLAVKKMWSKEESGAF-NSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:PTZ00267   70 VLTTLVGRN--PTTAAFVATRGSDPKEKVVAKFVMLNDERQAAYaRSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLHGAGKGGC--VDWEAR---YDVVLgvahALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLARTIS 909
Cdd:PTZ00267  148 SGGDLNKQIKQRLKEHLpfQEYEVGllfYQIVL----ALDEVHSRKM---MHRDLKSANIFLMPTGIIKLGDFGFSKQYS 220
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  910 GypNTGIDLAKPtnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:PTZ00267  221 D--SVSLDVASS-----FCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPF 271
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
765-966 6.45e-10

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: 61.23  E-value: 6.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGS-SGVVYRITIPSGESLAVK-----KMWSKEESgaFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd14083    10 VLGTGAfSEVVLAEDKATGKLVAIKcidkkALKGKEDS--LENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLhgAGKGGCVDWEARyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEP---YLADFGLARTISGypntG 915
Cdd:cd14083    88 LFDRI--VEKGSYTEKDAS-HLIRQVLEAVDYLHSL---GIVHRDLKPENLLYYSPDEDskiMISDFGLSKMEDS----G 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  916 IdlakptnrppMA---GSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14083   158 V----------MStacGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPP 201
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
801-972 7.60e-10

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: 61.57  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  801 SEIKTLGSI-RHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGG--------CVDWE--ARYDVV---LGVAH 866
Cdd:cd05098    67 SEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGmeycynpsHNPEEqlSSKDLVscaYQVAR 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  867 ALAYL-HHDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgIDLAKPTN--RPPMAgsygYMAPEhASMQR 943
Cdd:cd05098   147 GMEYLaSKKC----IHRDLAARNVLVTEDNVMKIADFGLARDIHH-----IDYYKKTTngRLPVK----WMAPE-ALFDR 212
                         170       180       190
                  ....*....|....*....|....*....|.
gi 240256081  944 I-TEKSDVYSYGVVLLEVLT-GKHPLdPDLP 972
Cdd:cd05098   213 IyTHQSDVWSFGVLLWEIFTlGGSPY-PGVP 242
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
765-967 8.32e-10

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: 61.92  E-value: 8.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVKKMwSK------EESGAFNSEIKTLGSIRHRNIVRLLgwCS---NRNLKLLFyDYL 834
Cdd:cd05573     8 VIGRGAFGEVWLVRdKDTGQVYAMKIL-RKsdmlkrEQIAHVRAERDILADADSPWIVRLH--YAfqdEDHLYLVM-EYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLHgagKGGCVDWE-ARY---DVVLGVaHALAYLHHdclptiIHGDVKAMNVLLGPHFEPYLADFGLA----- 905
Cdd:cd05573    84 PGGDLMNLLI---KYDVFPEEtARFyiaELVLAL-DSLHKLGF------IHRDIKPDNILLDADGHIKLADFGLCtkmnk 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  906 -RTISGYPNTGIDLAKPTNRPPMA--------------GSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05573   154 sGDRESYLNDSVNTLFQDNVLARRrphkqrrvraysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPF 230
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
751-1035 9.73e-10

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: 60.77  E-value: 9.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  751 FSIDDIVKNLtsanvigtgSSGVVY---RITIPSGESLAvKKMWSKEESGAFNseiktlgsirHRNIVRLLGWC-----S 822
Cdd:cd13986    13 FSFVYLVEDL---------STGRLYalkKILCHSKEDVK-EAMREIENYRLFN----------HPNILRLLDSQivkeaG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  823 NRNLKLLFYDYLPNGSLSSRLHGAGKGGCVDWEAR-YDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPHFEPYLAD 901
Cdd:cd13986    73 GKKEVYLLLPYYKRGSLQDEIERRLVKGTFFPEDRiLHIFLGICRGLKAMHEPELVPYAHRDIKPGNVLLSEDDEPILMD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  902 FGLAR----TISGypntgidlakptNRPPMA--------GSYGYMAPE--HA-SMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd13986   153 LGSMNpariEIEG------------RREALAlqdwaaehCTMPYRAPElfDVkSHCTIDEKTDIWSLGCTLYALMYGESP 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  967 LDPDLPGGAHLVKWVRDHLAEKKDPSRLLDPRLDgrtdsIMHEMLQTlavaflcvsnKANERPLMKDVV 1035
Cdd:cd13986   221 FERIFQKGDSLALAVLSGNYSFPDNSRYSEELHQ-----LVKSMLVV----------NPAERPSIDDLL 274
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
765-961 1.06e-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: 60.66  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRI-TIPSGESLAVKKMWSKEESGAFNS---EIKTLGSIRHRNIVRLL---------GW----------- 820
Cdd:cd14048    13 CLGRGGFGVVFEAkNKVDDCNYAVKRIRLPNNELAREKvlrEVRALAKLDHPGIVRYFnawlerppeGWqekmdevylyi 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  821 ----CSNRNLKllfyDYLP-NGSLSSRLHGAgkggCVDWearydvVLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHF 895
Cdd:cd14048    93 qmqlCRKENLK----DWMNrRCTMESRELFV----CLNI------FKQIASAVEYLHSKGL---IHRDLKPSNVFFSLDD 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  896 EPYLADFGLArtisgyPNTGIDLAKPTNRPPM---------AGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVL 961
Cdd:cd14048   156 VVKVGDFGLV------TAMDQGEPEQTVLTPMpayakhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
765-967 1.15e-09

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 60.79  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM-WSKEESGAFNSEIKTLGSI-RHRNIVRLLGW------CSNRNLKLLFYDYLP 835
Cdd:cd06636    23 VVGNGTYGQVYKgRHVKTGQLAAIKVMdVTEDEEEEIKLEINMLKKYsHHRNIATYYGAfikkspPGHDDQLWLVMEFCG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGAgKGGCV--DWEARY--DVVLGVAHAlaYLHHdclptIIHGDVKAMNVLLGPHFEPYLADFG----LART 907
Cdd:cd06636   103 AGSVTDLVKNT-KGNALkeDWIAYIcrEILRGLAHL--HAHK-----VIHRDIKGQNVLLTENAEVKLVDFGvsaqLDRT 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  908 IsGYPNTGIdlakptnrppmaGSYGYMAPEHASMQRITE-----KSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06636   175 V-GRRNTFI------------GTPYWMAPEVIACDENPDatydyRSDIWSLGITAIEMAEGAPPL 226
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
766-960 1.33e-09

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


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 60.44  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYrITIPSGESLAVKKMWSKEESGAF-NSEIKTLGSIRHRNIVRLL-----GWCSNRNLKLLfYDYLPNGSL 839
Cdd:cd14220     3 IGKGRYGEVW-MGKWRGEKVAVKVFFTTEEASWFrETEIYQTVLMRHENILGFIaadikGTGSWTQLYLI-TDYHENGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDCL-----PTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNT 914
Cdd:cd14220    81 YDFL----KCTTLDTRALLKLAYSAACGLCHLHTEIYgtqgkPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNSDTNE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  915 gIDLAKPTNrppmAGSYGYMAPE------HASMQRITEKSDVYSYGVVLLEV 960
Cdd:cd14220   157 -VDVPLNTR----VGTKRYMAPEvldeslNKNHFQAYIMADIYSFGLIIWEM 203
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
801-972 1.34e-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: 61.19  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  801 SEIKTLGSI-RHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGG-------C------VDWEARYDVVLGVAH 866
Cdd:cd05100    66 SEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGmdysfdtCklpeeqLTFKDLVSCAYQVAR 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  867 ALAYL-HHDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgIDLAKPTN--RPPMAgsygYMAPEHASMQR 943
Cdd:cd05100   146 GMEYLaSQKC----IHRDLAARNVLVTEDNVMKIADFGLARDVHN-----IDYYKKTTngRLPVK----WMAPEALFDRV 212
                         170       180       190
                  ....*....|....*....|....*....|
gi 240256081  944 ITEKSDVYSYGVVLLEVLT-GKHPLdPDLP 972
Cdd:cd05100   213 YTHQSDVWSFGVLLWEIFTlGGSPY-PGIP 241
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
766-967 1.38e-09

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: 60.44  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRI-TIPSGESLAVK--KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd06645    19 IGSGTYGDVYKArNVNTGELAAIKviKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSLQDI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGKggCVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgiDLAKpt 922
Cdd:cd06645    99 YHVTGP--LSESQIAY-VSRETLQGLYYLHSK---GKMHRDIKGANILLTDNGHVKLADFGVSAQITA------TIAK-- 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  923 nRPPMAGSYGYMAPEHASMQR---ITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06645   165 -RKSFIGTPYWMAPEVAAVERkggYNQLCDIWAVGITAIELAELQPPM 211
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
764-965 1.50e-09

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: 60.14  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIPS-GESLAVKKM----WSKEESGAFNSEIKTLGSIRHRNIVRLL-GWCSNRNLKLLFYDYLPNG 837
Cdd:cd08223     6 RVIGKGSYGEVWLVRHKRdRKQYVIKKLnlknASKRERKAAEQEAKLLSKLKHPNIVSYKeSFEGEDGFLYIVMGFCEGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHgAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPntgiD 917
Cdd:cd08223    86 DLYTRLK-EQKGVLLEERQVVEWFVQIAMALQYMHER---NILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSS----D 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  918 LAKPtnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKH 965
Cdd:cd08223   158 MATT-----LIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKH 200
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
766-966 1.72e-09

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: 60.02  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-----ITIPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLL-GWCSN---RNLKLLFYDYLPN 836
Cdd:cd14033     9 IGRGSFKTVYRgldteTTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYdSWKSTvrgHKCIILVTELMTS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGkggcvdwEARYDVV----LGVAHALAYLHHDClPTIIHGDVKAMNVLL-GPHFEPYLADFGLArtisgy 911
Cdd:cd14033    89 GTLKTYLKRFR-------EMKLKLLqrwsRQILKGLHFLHSRC-PPILHRDLKCDNIFItGPTGSVKIGDLGLA------ 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  912 pntgiDLAKPTNRPPMAGSYGYMAPEHASmQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14033   155 -----TLKRASFAKSVIGTPEFMAPEMYE-EKYDEAVDVYAFGMCILEMATSEYP 203
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
766-966 1.75e-09

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 59.67  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVV----YRItiPSGESLAVK-KMWSKEESGAFNSEI----KTLGSIRHRNIVRLLGWCSNRNLkLLFYDYLPN 836
Cdd:cd05060     3 LGHGNFGSVrkgvYLM--KSGKEVEVAvKTLKQEHEKAGKKEFlreaSVMAQLDHPCIVRLIGVCKGEPL-MLVMELAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGGCVD---WearydvVLGVAHALAYLHhdcLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypN 913
Cdd:cd05060    80 GPLLKYLKKRREIPVSDlkeL------AHQVAMGMAYLE---SKHFVHRDLAARNVLLVNRHQAKISDFGMSRAL----G 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  914 TGIDL--AKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05060   147 AGSDYyrATTAGRWPLK----WYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKP 198
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
765-973 1.82e-09

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


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 60.13  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVKKMWSKEESGAFNS----EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd07846     8 LVGEGSYGMVMKCRhKETGQIVAIKKFLESEDDKMVKKiamrEIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSrLHGAGKGgcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDla 919
Cdd:cd07846    88 DD-LEKYPNG--LDESRVRKYLFQILRGIDFCHSH---NIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD-- 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  920 kptnrppMAGSYGYMAPEH-ASMQRITEKSDVYSYGVVLLEVLTGkhplDPDLPG 973
Cdd:cd07846   160 -------YVATRWYRAPELlVGDTKYGKAVDVWAVGCLVTEMLTG----EPLFPG 203
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
758-966 1.94e-09

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: 59.94  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYR--ITIPSGESLAV-----KKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLF 830
Cdd:cd05064     5 KSIKIERILGTGRFGELCRgcLKLPSKRELPVaihtlRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 YDYLPNGSLSS--RLHgagkGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHfepyladfgLARTI 908
Cdd:cd05064    85 TEYMSNGALDSflRKH----EGQLVAGQLMGMLPGLASGMKYLSE---MGYVHKGLAAHKVLVNSD---------LVCKI 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  909 SGYpntgidlaKPTNRPPMAGSYGYM---------APEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05064   149 SGF--------RRLQEDKSEAIYTTMsgkspvlwaAPEAIQYHHFSSASDVWSFGIVMWEVMSyGERP 208
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
867-966 2.44e-09

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 59.16  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  867 ALAYLH-HDclptIIHGDVKAMNVLLGPHFEPY-LADFGLARTISgypntgidlAKPTNRPPMAGSYGYMAPE-HASMQR 943
Cdd:cd14019   113 ALKHVHsFG----IIHRDVKPGNFLYNRETGKGvLVDFGLAQREE---------DRPEQRAPRAGTRGFRAPEvLFKCPH 179
                          90       100
                  ....*....|....*....|...
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14019   180 QTTAIDIWSAGVILLSILSGRFP 202
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
765-968 2.60e-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: 59.45  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVKKMWSKEESG--AFNSEIKTLGSIR-HRNIVRllgWCSNRNL----------KLLF 830
Cdd:cd14036     7 VIAEGGFAFVYEAQdVGTGKEYALKRLLSNEEEKnkAIIQEINFMKKLSgHPNIVQ---FCSAASIgkeesdqgqaEYLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 YDYLPNGSLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDCLPtIIHGDVKAMNVLLGPHFEPYLADFGLARTISG 910
Cdd:cd14036    84 LTELCKGQLVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSPP-IIHRDLKIENLLIGNQGQIKLCDFGSATTEAH 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  911 YPNTGIDLAK--------PTNRPPMagsygYMAPEHASMQR---ITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14036   163 YPDYSWSAQKrslvedeiTRNTTPM-----YRTPEMIDLYSnypIGEKQDIWALGCILYLLCFRKHPFE 226
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
766-1035 2.73e-09

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: 59.32  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKM---WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd06641    12 IGKGSFGEVFKgIDNRTQKVVAIKIIdleEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLhgagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypNTGIdlakp 921
Cdd:cd06641    92 LL----EPGPLDETQIATILREILKGLDYLHSE---KKIHRDIKAANVLLSEHGEVKLADFGVAGQLT---DTQI----- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  922 tNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPdlpggAHLVKWVrdHLAEKKDPsrlldPRLDG 1001
Cdd:cd06641   157 -KRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSE-----LHPMKVL--FLIPKNNP-----PTLEG 223
                         250       260       270
                  ....*....|....*....|....*....|....
gi 240256081 1002 RTDSIMHEMLQTlavaflCVSNKANERPLMKDVV 1035
Cdd:cd06641   224 NYSKPLKEFVEA------CLNKEPSFRPTAKELL 251
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
766-973 2.82e-09

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: 59.64  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESL-AVKKMWSKEESGAFNS---EIKTLGSIRHRNIVRLLGWC-SNRNLKLLFyDYLPNgSLS 840
Cdd:cd07871    13 LGEGTYATVFKGRSKLTENLvALKEIRLEHEEGAPCTairEVSLLKNLKHANIVTLHDIIhTERCLTLVF-EYLDS-DLK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAGKGGCVdwearYDV---VLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS----GYPN 913
Cdd:cd07871    91 QYLDNCGNLMSM-----HNVkifMFQLLRGLSYCHKR---KILHRDLKPQNLLINEKGELKLADFGLARAKSvptkTYSN 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  914 TGIDLAKptnRPP--MAGSYGYMAPehasmqritekSDVYSYGVVLLEVLTGKhpldPDLPG 973
Cdd:cd07871   163 EVVTLWY---RPPdvLLGSTEYSTP-----------IDMWGVGCILYEMATGR----PMFPG 206
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
787-966 2.96e-09

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 59.64  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  787 VKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL---------------SSRLHGAGKGGc 851
Cdd:cd05090    42 LKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLheflimrsphsdvgcSSDEDGTVKSS- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  852 VDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgYPNTGIDLAKPTNRPpmagsY 931
Cdd:cd05090   121 LDHGDFLHIAIQIAAGMEYLSSH---FFVHKDLAARNILVGEQLHVKISDLGLSREI--YSSDYYRVQNKSLLP-----I 190
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 240256081  932 GYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05090   191 RWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQP 226
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
811-970 3.22e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 59.10  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  811 HRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHgagKGGCVDWEARYDVVLGVAHALAYLH-HdclpTIIHGDVKAMNV 889
Cdd:PHA03390   68 NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLK---KEGKLSEAEVKKIIRQLVEALNDLHkH----NIIHNDIKLENV 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  890 LlgpHFEP----YLADFGLARTIsGYPNTgidlakptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKH 965
Cdd:PHA03390  141 L---YDRAkdriYLCDYGLCKII-GTPSC------------YDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKH 204

                  ....*
gi 240256081  966 PLDPD 970
Cdd:PHA03390  205 PFKED 209
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
766-970 3.26e-09

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: 58.80  E-value: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVY-----------RITIPSGESLAVKKMWSKEESgafnsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:cd14081     9 LGKGQTGLVKlakhcvtgqkvAIKIVNKEKLSKESVLMKVER-----EIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLhgAGKGGCVDWEARyDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypnt 914
Cdd:cd14081    84 SGGELFDYL--VKKGRLTEKEAR-KFFRQIISALDYCHSHS---ICHRDLKPENLLLDEKNNIKIADFGMASLQ------ 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  915 gidlakPTNRppMA----GSYGYMAPEHASMQRIT-EKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14081   152 ------PEGS--LLetscGSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFDDD 204
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
747-966 3.41e-09

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: 59.31  E-value: 3.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  747 QKLDFSIDDIvKNLTSanvIGTGSSGVVYRIT-IPSGESLAVKKMW---SKEEsgafNSEI-----KTLGSIRHRNIVR- 816
Cdd:cd06618     8 KKYKADLNDL-ENLGE---IGSGTCGQVYKMRhKKTGHVMAVKQMRrsgNKEE----NKRIlmdldVVLKSHDCPYIVKc 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  817 ---------------LLGWCSNRNLKLLfYDYLPNgslssrlHGAGKggcvdwearydVVLGVAHALAYL--HHdclpTI 879
Cdd:cd06618    80 ygyfitdsdvficmeLMSTCLDKLLKRI-QGPIPE-------DILGK-----------MTVSIVKALHYLkeKH----GV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  880 IHGDVKAMNVLLGPHFEPYLADFGlartISGYpntgidLAKPTNRPPMAGSYGYMAPEHASMQRITE---KSDVYSYGVV 956
Cdd:cd06618   137 IHRDVKPSNILLDESGNVKLCDFG----ISGR------LVDSKAKTRSAGCAAYMAPERIDPPDNPKydiRADVWSLGIS 206
                         250
                  ....*....|
gi 240256081  957 LLEVLTGKHP 966
Cdd:cd06618   207 LVELATGQFP 216
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
766-996 3.50e-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: 59.28  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP-SGESLAVKKMWSKEESGA---FNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd06658    30 IGEGSTGIVCIATEKhTGKQVAVKKMDLRKQQRRellFN-EVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGAGkggcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgidlAKP 921
Cdd:cd06658   109 IVTHTR----MNEEQIATVCLSVLRALSYLHNQ---GVIHRDIKSDSILLTSDGRIKLSDFGFCAQVS---------KEV 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  922 TNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGGAhlVKWVRDHLaekkdPSRLLD 996
Cdd:cd06658   173 PKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQA--MRRIRDNL-----PPRVKD 240
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
766-964 3.73e-09

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: 59.06  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRI-TIPSGESLAVKKMWSKEESGAFNS----EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLpNGSLS 840
Cdd:cd07860     8 IGEGTYGVVYKArNKLTGEVVALKKIRLDTETEGVPStairEISLLKELNHPNIVKLLDVIHTENKLYLVFEFL-HQDLK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAGKGGcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypntGIDLAK 920
Cdd:cd07860    87 KFMDASALTG-IPLPLIKSYLFQLLQGLAFCHSH---RVLHRDLKPQNLLINTEGAIKLADFGLARAF------GVPVRT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 240256081  921 PTNRppmAGSYGYMAPEHASMQRI-TEKSDVYSYGVVLLEVLTGK 964
Cdd:cd07860   157 YTHE---VVTLWYRAPEILLGCKYySTAVDIWSLGCIFAEMVTRR 198
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
766-968 3.86e-09

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: 58.82  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVK-----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd14079    10 LGVGSFGKVKLAEhELTGHKVAVKilnrqKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGGEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSrlHGAGKGGCVDWEARY---DVVLGVahalAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLA---------RT 907
Cdd:cd14079    90 FD--YIVQKGRLSEDEARRffqQIISGV----EYCHRH---MVVHRDLKPENLLLDSNMNVKIADFGLSnimrdgeflKT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  908 ISGYPNtgidlakptnrppmagsygYMAPEhasmqRITEKS------DVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14079   161 SCGSPN-------------------YAAPE-----VISGKLyagpevDVWSCGVILYALLCGSLPFD 203
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
759-967 4.05e-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: 58.78  E-value: 4.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  759 NLTSANVIGTGSSGVVYRIT-IPSGESLA---VKKMWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:cd14190     5 SIHSKEVLGGGKFGKVHTCTeKRTGLKLAakvINKQNSKDKEMVLL-EIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLhgagkggcVDWEARYD------VVLGVAHALAYLHHdclPTIIHGDVKAMNVLL--GPHFEPYLADFGLAR 906
Cdd:cd14190    84 EGGELFERI--------VDEDYHLTevdamvFVRQICEGIQFMHQ---MRVLHLDLKPENILCvnRTGHQVKIIDFGLAR 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  907 TISGYPNTGIDLAKPTnrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14190   153 RYNPREKLKVNFGTPE----------FLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPF 203
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
256-488 4.34e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 57.87  E-value: 4.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  256 DEIGYCTELQNLYLYQNSISgSIPtTIGGLKKLQSLLLwQNNLVGKIptelgncpelwlidfsENLltgtiprsfGKLEN 335
Cdd:cd21340    18 DNLSLCKNLKVLYLYDNKIT-KIE-NLEFLTNLTHLYL-QNNQIEKI----------------ENL---------ENLVN 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  336 LQELQLSVNQISgTIpEELTNCTKLTHLEIDN-NLITGEI----P-SLMSNLRSLTMFFAWQNKLTgnIPQSLSQCRELQ 409
Cdd:cd21340    70 LKKLYLGGNRIS-VV-EGLENLTNLEELHIENqRLPPGEKltfdPrSLAALSNSLRVLNISGNNID--SLEPLAPLRNLE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  410 AIDLSYNSLSGsipkeifglrnltkllllSNDLSGFippdIGNCTNLYRLRLNGNRLAG------SIPSEIGNLKNLNFV 483
Cdd:cd21340   146 QLDASNNQISD------------------LEELLDL----LSSWPSLRELDLTGNPVCKkpkyrdKIILASKSLEVLDGK 203

                  ....*
gi 240256081  484 DISEN 488
Cdd:cd21340   204 EITDT 208
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
766-969 4.46e-09

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: 58.88  E-value: 4.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMW---SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd06643    13 LGDGAFGKVYKAQNKETGILAAAKVIdtkSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGKGGCvdwEARYDVVLG-VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLA----RTISgypntgid 917
Cdd:cd06643    93 MLELERPLT---EPQIRVVCKqTLEALVYLHEN---KIIHRDLKAGNILFTLDGDIKLADFGVSakntRTLQ-------- 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  918 lakptNRPPMAGSYGYMAPE----HASMQRITE-KSDVYSYGVVLLE---VLTGKHPLDP 969
Cdd:cd06643   159 -----RRDSFIGTPYWMAPEvvmcETSKDRPYDyKADVWSLGVTLIEmaqIEPPHHELNP 213
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
758-966 4.86e-09

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: 58.59  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYR--ITIPSGESLAVKKMWSKEESGA-----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLF 830
Cdd:cd05056     6 EDITLGRCIGEGQFGDVYQgvYMSPENEKIAVAVKTCKNCTSPsvrekFLQEAYIMRQFDHPHIVKLIGVITENPVWIVM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 yDYLPNGSLSSRLHgagkggcvdwEARYDVVLG--------VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADF 902
Cdd:cd05056    86 -ELAPLGELRSYLQ----------VNKYSLDLAslilyayqLSTALAYLESK---RFVHRDIAARNVLVSSPDCVKLGDF 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  903 GLARTI---SGYPNTgidlakpTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05056   152 GLSRYMedeSYYKAS-------KGKLPIK----WMAPESINFRRFTSASDVWMFGVCMWEILMlGVKP 208
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
756-960 5.12e-09

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


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 58.91  E-value: 5.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  756 IVKNLTSANVIGTGSSGVVYrITIPSGESLAVKKMWSKEESGAF-NSEIKTLGSIRHRNIVRLL-----GWCSNRNLKLL 829
Cdd:cd14219     3 IAKQIQMVKQIGKGRYGEVW-MGKWRGEKVAVKVFFTTEEASWFrETEIYQTVLMRHENILGFIaadikGTGSWTQLYLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 fYDYLPNGSLSSRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDCL-----PTIIHGDVKAMNVLLGPHFEPYLADFGL 904
Cdd:cd14219    82 -TDYHENGSLYDYL----KSTTLDTKAMLKLAYSSVSGLCHLHTEIFstqgkPAIAHRDLKSKNILVKKNGTCCIADLGL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  905 ARTISGYPNTgIDLAkPTNRppmAGSYGYMAPE--HASMQRITEKS----DVYSYGVVLLEV 960
Cdd:cd14219   157 AVKFISDTNE-VDIP-PNTR---VGTKRYMPPEvlDESLNRNHFQSyimaDMYSFGLILWEV 213
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
766-967 6.03e-09

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 57.98  E-value: 6.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP-SGESLAVK--KMWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd14107    10 IGRGTFGFVKRVTHKgNGECCAAKfiPLRSSTRARAFQ-ERDILARLSHRRLTCLLDQFETRKTLILILELCSSEELLDR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAGkggcVDWEARYDVVLG-VAHALAYLHHDclpTIIHGDVKAMNVLL-GPHFEPY-LADFGLARTIsgypntgidla 919
Cdd:cd14107    89 LFLKG----VVTEAEVKLYIQqVLEGIGYLHGM---NILHLDIKPDNILMvSPTREDIkICDFGFAQEI----------- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  920 kpTNRPPMAGSYG---YMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14107   151 --TPSEHQFSKYGspeFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPF 199
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
765-1041 6.09e-09

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 59.22  E-value: 6.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITI------PSGESLAVKKMwsKE-----ESGAFNSEIKTLGSI-RHRNIVRLLGWCSNRNLKLLF-- 830
Cdd:cd05102    14 VLGHGAFGKVVEASAfgidksSSCETVAVKML--KEgatasEHKALMSELKILIHIgNHLNVVNLLGACTKPNGPLMViv 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 ----YDYLPN-----------------------------GSLSSRLHGAGKGGCVDWEARY------------------- 858
Cdd:cd05102    92 efckYGNLSNflrakregfspyrersprtrsqvrsmveaVRADRRSRQGSDRVASFTESTSstnqprqevddlwqspltm 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  859 -DVV---LGVAHALAYL-HHDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidLAKPTNRPPMAgsygY 933
Cdd:cd05102   172 eDLIcysFQVARGMEFLaSRKC----IHRDLAARNILLSENNVVKICDFGLARDIYKDPDY---VRKGSARLPLK----W 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  934 MAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPldpdLPGgahlVKWVRDHLAEKKDPSRLLDPrlDGRTDSIMHEMLQ 1012
Cdd:cd05102   241 MAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASP----YPG----VQINEEFCQRLKDGTRMRAP--EYATPEIYRIMLS 310
                         330       340
                  ....*....|....*....|....*....
gi 240256081 1013 tlavaflCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd05102   311 -------CWHGDPKERPTFSDLVEILGDL 332
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
760-1041 6.19e-09

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: 58.33  E-value: 6.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYRITIPSGESLAVKKM----WSKEEsgaFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLP 835
Cdd:cd05114     6 LTFMKELGSGLFGVVRLGKWRAQYKVAIKAIregaMSEED---FIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTG 915
Cdd:cd05114    83 NGCLLNYLRQ--RRGKLSRDMLLSMCQDVCEGMEYLERN---NFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  916 IDLAK-PTNRPPmagsygymaPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLDPdlpggahlvKWVRDHLAEKKDPSR 993
Cdd:cd05114   158 SSGAKfPVKWSP---------PEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFES---------KSNYEVVEMVSRGHR 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  994 LLDPRLDGRtdsimhemlQTLAVAFLCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd05114   220 LYRPKLASK---------SVYEVMYSCWHEKPEGRPTFADLLRTITEI 258
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
751-967 6.40e-09

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: 58.91  E-value: 6.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  751 FSIDDIVKNLTSANVIGTGSSGVVYRI-TIPSGESLAVKKM-----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNR 824
Cdd:cd06635    18 FFKEDPEKLFSDLREIGHGSFGAVYFArDVRTSEVVAIKKMsysgkQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLRE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  825 NLKLLFYDYLPnGSLSSRLHgAGKGGCVDWEARyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGL 904
Cdd:cd06635    98 HTAWLVMEYCL-GSASDLLE-VHKKPLQEIEIA-AITHGALQGLAYLHSH---NMIHRDIKAGNILLTEPGQVKLADFGS 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  905 ArtisgypntgiDLAKPTNRppMAGSYGYMAPE---HASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06635   172 A-----------SIASPANS--FVGTPYWMAPEvilAMDEGQYDGKVDVWSLGITCIELAERKPPL 224
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
766-966 7.09e-09

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: 57.90  E-value: 7.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGS-SGVVYRITIPSGESLAVK---KMWSKEES---GAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd14070    10 LGEGSfAKVREGLHAVTGEKVAIKvidKKKAKKDSyvtKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGagKGGCVDWEARyDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTiSGYPNTGIDL 918
Cdd:cd14070    90 LMHRIYD--KKRLEEREAR-RYIRQLVSAVEHLHR---AGVVHRDLKIENLLLDENDNIKLIDFGLSNC-AGILGYSDPF 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  919 AKptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14070   163 ST------QCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLP 204
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
766-982 7.26e-09

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: 58.22  E-value: 7.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVY--RITIpSGESLAVKKMWSKE-----ESGAFNSEIKTLGSIRHRNIVRLL-GWCSNRNLKLLFyDYLPNG 837
Cdd:cd05612     9 IGTGTFGRVHlvRDRI-SEHYYALKVMAIPEvirlkQEQHVHNEKRVLKEVSHPFIIRLFwTEHDQRFLYMLM-EYVPGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGkggcvdweaRYDVVLG------VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGY 911
Cdd:cd05612    87 ELFSYLRNSG---------RFSNSTGlfyaseIVCALEYLHSK---EIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDR 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  912 PNTgidlakptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPGG------AHLVKWVR 982
Cdd:cd05612   155 TWT------------LCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGiyekilAGKLEFPR 219
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
766-969 7.83e-09

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: 58.52  E-value: 7.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRN---IVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd06649    13 LGAGNGGVVTKVQhKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNspyIVGFYGAFYSDGEISICMEHMDGGSLDQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGAGKggcVDWEARYDVVLGVAHALAYLHHDclPTIIHGDVKAMNVLLGPHFEPYLADFGLA-RTISGYPNTgidlak 920
Cdd:cd06649    93 VLKEAKR---IPEEILGKVSIAVLRGLAYLREK--HQIMHRDVKPSNILVNSRGEIKLCDFGVSgQLIDSMANS------ 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 240256081  921 ptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDP 969
Cdd:cd06649   162 ------FVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPP 204
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
765-968 7.87e-09

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: 57.69  E-value: 7.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFNS-----EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd14162     7 TLGHGSYAVVKKaYSTKHKCKVAIKIVSKKKAPEDYLQkflprEIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSS--RLHGAgkggCVDWEAR---YDVVLGVahalAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgypn 913
Cdd:cd14162    87 LLDyiRKNGA----LPEPQARrwfRQLVAGV----EYCHSK---GVVHRDLKCENLLLDKNNNLKITDFGFARG------ 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  914 tgiDLAKPTNRPPMA----GSYGYMAPE-HASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14162   150 ---VMKTKDGKPKLSetycGSYAYASPEiLRGIPYDPFLSDIWSMGVVLYTMVYGRLPFD 206
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
751-967 8.76e-09

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: 58.11  E-value: 8.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  751 FSIDDIVKNLTSANVIGTGSSGVVYRI-TIPSGESLAVKKM-----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNR 824
Cdd:cd06634     8 FFKDDPEKLFSDLREIGHGSFGAVYFArDVRNNEVVAIKKMsysgkQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLRE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  825 NLKLLFYDYLPnGSLSSRLHgAGKGGCVDWEARyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGL 904
Cdd:cd06634    88 HTAWLVMEYCL-GSASDLLE-VHKKPLQEVEIA-AITHGALQGLAYLHSH---NMIHRDVKAGNILLTEPGLVKLGDFGS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  905 ARTISgypntgidlakPTNRppMAGSYGYMAPE---HASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06634   162 ASIMA-----------PANS--FVGTPYWMAPEvilAMDEGQYDGKVDVWSLGITCIELAERKPPL 214
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
756-985 8.86e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 58.73  E-value: 8.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  756 IVKNLTSanvigtGSSGVVYRITIPSGESLAVKKMWSKeesGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL------ 829
Cdd:PHA03209   70 VIKTLTP------GSEGRVFVATKPGQPDPVVLKIGQK---GTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMvlphys 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 --FYDYLPNGSlssrlhgagkgGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLART 907
Cdd:PHA03209  141 sdLYTYLTKRS-----------RPLPIDQALIIEKQILEGLRYLHAQ---RIIHRDVKTENIFINDVDQVCIGDLGAAQF 206
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  908 ISGYPNtgiDLAkptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLP-GGAHLVKWVRDHL 985
Cdd:PHA03209  207 PVVAPA---FLG-------LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLAYPSTIFEDPPsTPEEYVKSCHSHL 275
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
764-957 1.02e-08

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: 57.68  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIP-SGESLAVKKMWSKEESG--AFNSEIKTLGSIR-HRNIVRLLGWCSNRNLK-----LLFYDYL 834
Cdd:cd14037     9 KYLAEGGFAHVYLVKTSnGGNRAALKRVYVNDEHDlnVCKREIEIMKRLSgHKNIVGYIDSSANRSGNgvyevLLLMEYC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGS--------LSSRLHgagkggcvdwEAR-----YDVVLGVAhalaYLHHdCLPTIIHGDVKAMNVLLGPHFEPYLAD 901
Cdd:cd14037    89 KGGGvidlmnqrLQTGLT----------ESEilkifCDVCEAVA----AMHY-LKPPLIHRDLKVENVLISDSGNYKLCD 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  902 FGLA-------RTISGYPNTGIDLAKPTNRPpmagsygYMAPEHASMQR---ITEKSDVYSYGVVL 957
Cdd:cd14037   154 FGSAttkilppQTKQGVTYVEEDIKKYTTLQ-------YRAPEMIDLYRgkpITEKSDIWALGCLL 212
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
760-966 1.04e-08

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: 57.76  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYR-ITIPSGESLAVKKM---WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLP 835
Cdd:cd06642     6 FTKLERIGKGSFGEVYKgIDNRTKEVVAIKIIdleEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypNTG 915
Cdd:cd06642    86 GGSALDLL----KPGPLEETYIATILREILKGLDYLHSE---RKIHRDIKAANVLLSEQGDVKLADFGVAGQLT---DTQ 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  916 IdlakptNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06642   156 I------KRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPP 200
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
766-970 1.21e-08

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: 57.66  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKM---WSKEESGAFNSEIKTLGSIRHRNIVRL------LGWCSNRNLKLLFYDYLP 835
Cdd:cd14038     2 LGTGGFGNVLRwINQETGEQVAIKQCrqeLSPKNRERWCLEIQIMKRLNHPNVVAArdvpegLQKLAPNDLPLLAMEYCQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPhfepyladfGLARTISGYpntg 915
Cdd:cd14038    82 GGDLRKYLNQFENCCGLREGAILTLLSDISSALRYLHEN---RIIHRDLKPENIVLQQ---------GEQRLIHKI---- 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  916 IDL--AKPTNRPPM----AGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14038   146 IDLgyAKELDQGSLctsfVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPN 206
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
765-967 1.37e-08

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 57.36  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-------------ITIPSGESLAvkkmwskeesgAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFY 831
Cdd:cd14063     7 VIGKGRFGRVHRgrwhgdvaikllnIDYLNEEQLE-----------AFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLPNGSLSSRLHGAGKGGCVDWEARydVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLgPHFEPYLADFGLArTISGY 911
Cdd:cd14063    76 SLCKGRTLYSLIHERKEKFDFNKTVQ--IAQQICQGMGYLHAK---GIIHKDLKSKNIFL-ENGRVVITDFGLF-SLSGL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  912 PNTGID---LAKPTNRPPmagsygYMAPEHASMQRI----------TEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14063   149 LQPGRRedtLVIPNGWLC------YLAPEIIRALSPdldfeeslpfTKASDVYAFGTVWYELLAGRWPF 211
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
764-967 1.61e-08

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: 57.51  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFN----SEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYD-----Y 833
Cdd:cd07864    13 GIIGEGTYGQVYKaKDKDTGELVALKKVRLDNEKEGFPitaiREIKILRQLNHRSVVNLKEIVTDKQDALDFKKdkgafY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSLSSRLHGAGKGGCVDWEARY--DVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISG- 910
Cdd:cd07864    93 LVFEYMDHDLMGLLESGLVHFSEDHikSFMKQLLEGLNYCHKK---NFLHRDIKCSNILLNNKGQIKLADFGLARLYNSe 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256081  911 ----YPNTGIDLAKptnRPP--MAGSygymapehasmQRITEKSDVYSYGVVLLEVLTgKHPL 967
Cdd:cd07864   170 esrpYTNKVITLWY---RPPelLLGE-----------ERYGPAIDVWSCGCILGELFT-KKPI 217
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
766-966 1.77e-08

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: 56.90  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKK------MWSKEESGAFNsEIKTLGSIRHRNIVRLL-GWCSNRNLKLLFyDYLPNG 837
Cdd:cd08224     8 IGKGQFSVVYRaRCLLDGRLVALKKvqifemMDAKARQDCLK-EIDLLQQLNHPNIIKYLaSFIENNELNIVL-ELADAG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGKGGCVDWEA---RYDVvlGVAHALAYLHhdcLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypnt 914
Cdd:cd08224    86 DLSRLIKHFKKQKRLIPERtiwKYFV--QLCSALEHMH---SKRIMHRDIKPANVFITANGVVKLGDLGLGRFFS----- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  915 gidlAKPTNRPPMAGSYGYMAPEhasmqRITE-----KSDVYSYGVVLLEVLTGKHP 966
Cdd:cd08224   156 ----SKTTAAHSLVGTPYYMSPE-----RIREqgydfKSDIWSLGCLLYEMAALQSP 203
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
766-992 1.87e-08

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 57.07  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFNS-----EIKTLGSIRHRNIVRL------LGWCSNRNLKLLFYDY 833
Cdd:cd13989     1 LGSGGFGYVTLwKHQDTGEYVAIKKCRQELSPSDKNRerwclEVQIMKKLNHPNVVSArdvppeLEKLSPNDLPLLAMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSLSSRLHGAGK-GGCVDWEARyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL--GPHFEPY-LADFGLARtis 909
Cdd:cd13989    81 CSGGDLRKVLNQPENcCGLKESEVR-TLLSDISSAISYLHEN---RIIHRDLKPENIVLqqGGGRVIYkLIDLGYAK--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  910 gypntgiDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDLPggahLVKWVRdhLAEKK 989
Cdd:cd13989   154 -------ELDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFLPNWQ----PVQWHG--KVKQK 220

                  ...
gi 240256081  990 DPS 992
Cdd:cd13989   221 KPE 223
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
766-961 1.87e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 56.73  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP-SGESLAVKKMwsKEESGAFNSEIKTLGSIRHRNIVRLL-------GWCSNRN-------LKLLF 830
Cdd:cd14047    14 IGSGGFGQVFKAKHRiDGKTYAIKRV--KLNNEKAEREVKALAKLDHPNIVRYNgcwdgfdYDPETSSsnssrskTKCLF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 --YDYLPNGSLSSRLHGAGKGGCVDWEArYDVVLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd14047    92 iqMEFCEKGTLESWIEKRNGEKLDKVLA-LEIFEQITKGVEYIHSKKL---IHRDLKPSNIFLVDTGKVKIGDFGLVTSL 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  909 SGYpntgidLAKPTNRppmaGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVL 961
Cdd:cd14047   168 KND------GKRTKSK----GTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
766-966 1.97e-08

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: 57.05  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVK----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL- 839
Cdd:cd14086     9 LGKGAFSVVRRcVQKSTGQEFAAKiintKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELf 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 ---SSRLH--GAGKGGCVDWearydvvlgVAHALAYLHHDclpTIIHGDVKAMNVLLG---PHFEPYLADFGLARTISGy 911
Cdd:cd14086    89 ediVAREFysEADASHCIQQ---------ILESVNHCHQN---GIVHRDLKPENLLLAsksKGAAVKLADFGLAIEVQG- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  912 pntgidlAKPTnRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14086   156 -------DQQA-WFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPP 202
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
860-969 2.00e-08

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: 57.06  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  860 VVLGVAHALAYLH--HDclptIIHGDVKAMNVLLGPHFEPYLADFGlartISGYPntgIDlakptnrpPMAGSY----GY 933
Cdd:cd06615   104 ISIAVLRGLTYLRekHK----IMHRDVKPSNILVNSRGEIKLCDFG----VSGQL---ID--------SMANSFvgtrSY 164
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 240256081  934 MAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDP 969
Cdd:cd06615   165 MSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPP 200
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
760-966 2.33e-08

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 56.77  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYRITIPSGES----LAVKKM----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWC---SNRN--- 825
Cdd:cd05035     1 LKLGKILGEGEFGSVMEAQLKQDDGsqlkVAVKTMkvdiHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCftaSDLNkpp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  826 LKLLFYDYLPNGSL-----SSRLHGAGKGGCVDWEARYdvVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLA 900
Cdd:cd05035    81 SPMVILPFMKHGDLhsyllYSRLGGLPEKLPLQTLLKF--MVDIAKGMEYLSNR---NFIHRDLAARNCMLDENMTVCVA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  901 DFGLARTI-SG-YPNTGIDLAKPTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05035   156 DFGLSRKIySGdYYRQGRISKMPVK---------WIALESLADNVYTSKSDVWSFGVTMWEIATrGQTP 215
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
765-967 2.37e-08

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: 56.51  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVK--KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd14192    11 VLGGGRFGQVHKCTeLSTGLTLAAKiiKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELFD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLhgagkggcVDWE---ARYDVVL---GVAHALAYLHHDclpTIIHGDVKAMNVLLGPHF--EPYLADFGLARTISGYPN 913
Cdd:cd14192    91 RI--------TDESyqlTELDAILftrQICEGVHYLHQH---YILHLDLKPENILCVNSTgnQIKIIDFGLARRYKPREK 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  914 TGIDLAKPTnrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14192   160 LKVNFGTPE----------FLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPF 203
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
766-969 2.55e-08

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: 57.18  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWskeesGAF-NS--------EIKTLGSIR-HRNIVRLLGWC---SNRNLKLLFy 831
Cdd:cd07852    15 LGKGAYGIVWKaIDKKTGEVVALKKIF-----DAFrNAtdaqrtfrEIMFLQELNdHPNIIKLLNVIraeNDKDIYLVF- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLpngslSSRLHGAGKGG-CVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISG 910
Cdd:cd07852    89 EYM-----ETDLHAVIRANiLEDIHKQY-IMYQLLKALKYLHSG---GVIHRDLKPSNILLNSDCRVKLADFGLARSLSQ 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  911 YPNTGIDlakptnrpPMAGSY----GYMAPE--HASmQRITEKSDVYSYGVVLLEVLTGKhPLDP 969
Cdd:cd07852   160 LEEDDEN--------PVLTDYvatrWYRAPEilLGS-TRYTKGVDMWSVGCILGEMLLGK-PLFP 214
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
766-962 2.90e-08

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: 56.09  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESL-AVK---KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSS 841
Cdd:cd05084     4 IGRGNFGEVFSGRLRADNTPvAVKscrETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGAGKGGCVDWEARydVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISG--YPNTGIDLA 919
Cdd:cd05084    84 FLRTEGPRLKVKELIR--MVENAAAGMEYLESKH---CIHRDLAARNCLVTEKNVLKISDFGMSREEEDgvYAATGGMKQ 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 240256081  920 KPTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05084   159 IPVK---------WTAPEALNYGRYSSESDVWSFGILLWETFS 192
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
759-966 3.11e-08

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: 56.32  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  759 NLTSANVIGTGSSGVVYRITIP-----SGESL-AVKKMWSKEESG---AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLL 829
Cdd:cd05046     6 NLQEITTLGRGEFGEVFLAKAKgieeeGGETLvLVKALQKTKDENlqsEFRRELDMFRKLSHKNVVRLLGLCREAEPHYM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 FYDYLPNGSLSSRLHgAGKGGCVDWE-------ARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADF 902
Cdd:cd05046    86 ILEYTDLGDLKQFLR-ATKSKDEKLKppplstkQKVALCTQIALGMDHLSNA---RFVHRDLAARNCLVSSQREVKVSLL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  903 GLARTISG-----YPNTGIDLAkptnrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05046   162 SLSKDVYNseyykLRNALIPLR-------------WLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELP 218
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
765-1014 3.21e-08

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: 56.18  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITI-PSGESLAVKKMWSKE------ESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd05630     7 VLGKGGFGEVCACQVrATGKMYACKKLEKKRikkrkgEAMALN-EKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGKGGCVDWEARY---DVVLGVAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLA------RTI 908
Cdd:cd05630    86 DLKFHIYHMGQAGFPEARAVFyaaEICCGLED----LHRE---RIVYRDLKPENILLDDHGHIRISDLGLAvhvpegQTI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  909 SGypntgidlakptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDP-----DLPGGAHLVKWVRD 983
Cdd:cd05630   159 KG----------------RVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQrkkkiKREEVERLVKEVPE 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 240256081  984 HLAEK--------------KDPSRLLDPRLDGRTDSIMHEMLQTL 1014
Cdd:cd05630   223 EYSEKfspqarslcsmllcKDPAERLGCRGGGAREVKEHPLFKKL 267
PLN03150 PLN03150
hypothetical protein; Provisional
554-662 3.31e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 57.52  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  554 LNLAKNRLSGEIPREISTCRSLQLLNLGENDFSGEIPDELGQIPSLAislnlscnrfvgeipsrfsdlknlgVLDVSHNQ 633
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLE-------------------------VLDLSYNS 477
                          90       100       110
                  ....*....|....*....|....*....|
gi 240256081  634 LTGNL-NVLTDLQNLVSLNISYNDFSGDLP 662
Cdd:PLN03150  478 FNGSIpESLGQLTSLRILNLNGNSLSGRVP 507
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
802-963 3.56e-08

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: 56.07  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLL-GWCSNRNLkLLFYDYLPNGSLSSRLHgagKGGCVDWE-ARY---DVVLgvahALAYLHHDcl 876
Cdd:cd05579    43 ERNILSQAQNPFVVKLYySFQGKKNL-YLVMEYLPGGDLYSLLE---NVGALDEDvARIyiaEIVL----ALEYLHSH-- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  877 pTIIHGDVKAMNVLL---GpHFEpyLADFGLARTISGYPNTGIDLAKPTNRPP------MAGSYGYMAPEHASMQRITEK 947
Cdd:cd05579   113 -GIIHRDLKPDNILIdanG-HLK--LTDFGLSKVGLVRRQIKLSIQKKSNGAPekedrrIVGTPDYLAPEILLGQGHGKT 188
                         170
                  ....*....|....*.
gi 240256081  948 SDVYSYGVVLLEVLTG 963
Cdd:cd05579   189 VDWWSLGVILYEFLVG 204
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
766-1012 3.58e-08

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 56.33  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVY----RITipsGESLAVKKMWSKEESGAFNS---EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLpNGS 838
Cdd:cd07836     8 LGEGTYATVYkgrnRTT---GEIVALKEIHLDAEEGTPSTairEISLMKELKHENIVRLHDVIHTENKLMLVFEYM-DKD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypntGIDL 918
Cdd:cd07836    84 LKKYMDTHGVRGALDPNTVKSFTYQLLKGIAFCHEN---RVLHRDLKPQNLLINKRGELKLADFGLARAF------GIPV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  919 AKPTN-------RPP--MAGSYGYmapehasmqriTEKSDVYSYGVVLLEVLTGK--------------------HPLDP 969
Cdd:cd07836   155 NTFSNevvtlwyRAPdvLLGSRTY-----------STSIDIWSVGCIMAEMITGRplfpgtnnedqllkifrimgTPTES 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 240256081  970 DLPGGAHLVKWVRDHLAEKKDPSRLLDPRLDGRTDSIMHEMLQ 1012
Cdd:cd07836   224 TWPGISQLPEYKPTFPRYPPQDLQQLFPHADPLGIDLLHRLLQ 266
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
766-972 3.61e-08

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: 55.76  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKKMWSKEE-SGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRL 843
Cdd:cd14665     8 IGSGNFGVARLMRdKQTKELVAVKYIERGEKiDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGGELFERI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  844 HGAGKGGcvDWEARY---DVVLGVAhalaYLHHdclPTIIHGDVKAMNVLLGPHFEPYL--ADFGlartisgYPNTGIDL 918
Cdd:cd14665    88 CNAGRFS--EDEARFffqQLISGVS----YCHS---MQICHRDLKLENTLLDGSPAPRLkiCDFG-------YSKSSVLH 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  919 AKPTNrppMAGSYGYMAPEHASMQRITEK-SDVYSYGVVLLEVLTGKHPL-DPDLP 972
Cdd:cd14665   152 SQPKS---TVGTPAYIAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFeDPEEP 204
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
747-909 3.80e-08

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: 56.22  E-value: 3.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  747 QKLDFSIDDIVKNLTSANVIGTGSSGVVYRI-TIPSGESLAVKKMWSKEESGAFN----SEIKTLGSIRHRNIVRLLGWC 821
Cdd:cd07865     1 DQVEFPFCDEVSKYEKLAKIGQGTFGEVFKArHRKTGQIVALKKVLMENEKEGFPitalREIKILQLLKHENVVNLIEIC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  822 SNR-----NLKLLFY------DYLPNGSLSSRLhgagkggcVDW--EARYDVVLGVAHALAYLHHDclpTIIHGDVKAMN 888
Cdd:cd07865    81 RTKatpynRYKGSIYlvfefcEHDLAGLLSNKN--------VKFtlSEIKKVMKMLLNGLYYIHRN---KILHRDMKAAN 149
                         170       180
                  ....*....|....*....|.
gi 240256081  889 VLLGPHFEPYLADFGLARTIS 909
Cdd:cd07865   150 ILITKDGVLKLADFGLARAFS 170
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
766-968 4.44e-08

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: 55.51  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT---IPSGESLAVKKMWS-----KEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd08222     8 LGSGNFGTVYLVSdlkATADEELKVLKEISvgelqPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGK-GGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPyLADFGLARTISGypntGI 916
Cdd:cd08222    88 DLDDKISEYKKsGTTIDENQILDWFIQLLLAVQYMHER---RILHRDLKAKNIFLKNNVIK-VGDFGISRILMG----TS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  917 DLAKPtnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd08222   160 DLATT-----FTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFD 206
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
766-967 4.79e-08

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: 55.74  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP-SGESLAVK--KMWSKEESGAFNSE-----IKTLGSIRHRNIVRLLGWC----SNRNLKL-LFYD 832
Cdd:cd07863     8 IGVGAYGTVYKARDPhSGHFVALKsvRVQTNEDGLPLSTVrevalLKRLEAFDHPNIVRLMDVCatsrTDRETKVtLVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  833 YLpNGSLSSRLHGAGKGGcVDWEARYDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISGyp 912
Cdd:cd07863    88 HV-DQDLRTYLDKVPPPG-LPAETIKDLMRQFLRGLDFLHANC---IVHRDLKPENILVTSGGQVKLADFGLARIYSC-- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  913 NTGIDlakptnrpPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKhPL 967
Cdd:cd07863   161 QMALT--------PVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRK-PL 206
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
756-962 4.90e-08

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: 55.71  E-value: 4.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  756 IVKNLTS-ANVIGTGSSGVVY--RITIPSG--ESLAVKKM----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWC---SN 823
Cdd:cd14204     4 IDRNLLSlGKVLGEGEFGSVMegELQQPDGtnHKVAVKTMkldnFSQREIEEFLSEAACMKDFNHPNVIRLLGVClevGS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  824 RN-------LKLLFYDYLPNGSLSSRLHGAGKGgcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFE 896
Cdd:cd14204    84 QRipkpmviLPFMKYGDLHSFLLRSRLGSGPQH--VPLQTLLKFMIDIALGMEYLSSR---NFLHRDLAARNCMLRDDMT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  897 PYLADFGLARTI-SG-YPNTGIDLAKPTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd14204   159 VCVADFGLSKKIySGdYYRQGRIAKMPVK---------WIAVESLADRVYTVKSDVWAFGVTMWEIAT 217
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
761-1012 5.11e-08

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: 55.47  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  761 TSANVIGTGSSGVVYRITIPSGESLAVKKMWSKE-----------ESGAFNSEIK---TLGSIRHRNIVRLLGWCSNrnl 826
Cdd:cd14004     3 TILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKErilvdtwvrdrKLGTVPLEIHildTLNKRSHPNIVKLLDFFED--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  827 KLLFYdylpngsLSSRLHGAG---------KGGCVDWEARYdVVLGVAHALAYLHhdcLPTIIHGDVKAMNVLLGPHFEP 897
Cdd:cd14004    80 DEFYY-------LVMEKHGSGmdlfdfierKPNMDEKEAKY-IFRQVADAVKHLH---DQGIVHRDIKDENVILDGNGTI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  898 YLADFGLARTIsgypntgidlaKPTNRPPMAGSYGYMAPE--HASMQRITEKsDVYSYGVVLLEVLTGKHP---LDPDLP 972
Cdd:cd14004   149 KLIDFGSAAYI-----------KSGPFDTFVGTIDYAAPEvlRGNPYGGKEQ-DIWALGVLLYTLVFKENPfynIEEILE 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 240256081  973 GGAHLVKWVRDHLAEKKdpSRLLDPRLDGRTDsiMHEMLQ 1012
Cdd:cd14004   217 ADLRIPYAVSEDLIDLI--SRMLNRDVGDRPT--IEELLT 252
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
730-967 6.42e-08

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: 55.38  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  730 GKQLLGEEIDSWEVTlyqkldfsiddivknltsaNVIGTGSSGVVYRITIPSGESLAVKKMWS--KEESGAFNSEIKTLG 807
Cdd:cd06639    13 GLESLADPSDTWDII-------------------ETIGKGTYGKVYKVTNKKDGSLAAVKILDpiSDVDEEIEAEYNILR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  808 SI-RHRNIVRLLGW------CSNRNLKLLFyDYLPNGSLSSRLHGAGKGGCVDWEARYDVVL-GVAHALAYLHHDclpTI 879
Cdd:cd06639    74 SLpNHPNVVKFYGMfykadqYVGGQLWLVL-ELCNGGSVTELVKGLLKCGQRLDEAMISYILyGALLGLQHLHNN---RI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  880 IHGDVKAMNVLLGPHFEPYLADFGLARTIsgypnTGIDLAKPTNrppmAGSYGYMAPEHASMQRITEKS-----DVYSYG 954
Cdd:cd06639   150 IHRDVKGNNILLTTEGGVKLVDFGVSAQL-----TSARLRRNTS----VGTPFWMAPEVIACEQQYDYSydarcDVWSLG 220
                         250
                  ....*....|...
gi 240256081  955 VVLLEVLTGKHPL 967
Cdd:cd06639   221 ITAIELADGDPPL 233
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
760-966 8.80e-08

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: 55.06  E-value: 8.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYRITIPSGESLAVKKMWSKEESgafNSEIKTLgsirhRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd06640     6 FTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEA---EDEIEDI-----QQEITVLSQCDSPYVTKYYGSYLKGTKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHGAGKGGCVDW-------EARYDVVLG-VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgy 911
Cdd:cd06640    78 WIIMEYLGGGSALDLlragpfdEFQIATMLKeILKGLDYLHSE---KKIHRDIKAANVLLSEQGDVKLADFGVAGQLT-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  912 pNTGIdlakptNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06640   153 -DTQI------KRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
766-966 9.16e-08

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 54.58  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVV---YRITIPSGESLAVKKMWSKEESGAFNSEI----KTLGSIRHRNIVRLLGWCSNRNLkLLFYDYLPNGS 838
Cdd:cd05116     3 LGSGNFGTVkkgYYQMKKVVKTVAVKILKNEANDPALKDELlreaNVMQQLDNPYIVRMIGICEAESW-MLVMEMAELGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHgagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNtgIDL 918
Cdd:cd05116    82 LNKFLQ---KNRHVTEKNITELVHQVSMGMKYLEES---NFVHRDLAARNVLLVTQHYAKISDFGLSKALRADEN--YYK 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 240256081  919 AKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05116   154 AQTHGKWPVK----WYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKP 198
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
855-967 1.02e-07

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: 55.06  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  855 EARyDVVLGVAHALAYLHhDCLPTIIHGDVKAMNVLL---GPHFEPYLADFGLARTIS--GYPNTGIDLAKPTnrppmAG 929
Cdd:cd14040   112 EAR-SIVMQIVNALRYLN-EIKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDddSYGVDGMDLTSQG-----AG 184
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 240256081  930 SYGYMAPE----HASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14040   185 TYWYLPPEcfvvGKEPPKISNKVDVWSVGVIFFQCLYGRKPF 226
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
785-967 1.27e-07

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: 54.02  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  785 LAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSnRNLKLLFYDYLPNGSLSSRLHGAGKGGCVDWeaRYDVVLGV 864
Cdd:cd05037    35 LKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCV-ADENIMVQEYVRYGPLDKYLRRMGNNVPLSW--KLQVAKQL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  865 AHALAYLHHDclpTIIHGDVKAMNVLL------GPHFEPYLADfglartiSGYPNTGIDLAKPTNRPPmagsygYMAPE- 937
Cdd:cd05037   112 ASALHYLEDK---KLIHGNVRGRNILLaregldGYPPFIKLSD-------PGVPITVLSREERVDRIP------WIAPEc 175
                         170       180       190
                  ....*....|....*....|....*....|..
gi 240256081  938 -HASMQRITEKSDVYSYGVVLLEVLT-GKHPL 967
Cdd:cd05037   176 lRNLQANLTIAADKWSFGTTLWEICSgGEEPL 207
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
779-968 1.37e-07

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: 54.06  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  779 IPSGESLAVKKMWSKEESGA----FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRL--HGAGKggcv 852
Cdd:cd14072    22 VLTGREVAIKIIDKTQLNPSslqkLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLvaHGRMK---- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  853 DWEARYDVVLGVAhALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgyPNTGIDlakptnrpPMAGSYG 932
Cdd:cd14072    98 EKEARAKFRQIVS-AVQYCHQK---RIVHRDLKAENLLLDADMNIKIADFGFSNEFT--PGNKLD--------TFCGSPP 163
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 240256081  933 YMAPEHASMQRIT-EKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14072   164 YAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFD 200
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
480-693 1.39e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  480 LNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLSGSLLGTTLPKSLKFIDFSDNALSSTLPPGIGLLTELTKLNLAKN 559
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  560 RLSGEI--PREISTCRSLQLLNLGENDfsgeipdELGQIPSLAiSLNLSCNRfVGEIPSRFSDLKNLGVLDVSHNQLTGN 637
Cdd:COG4886    81 LLSLLLlgLTDLGDLTNLTELDLSGNE-------ELSNLTNLE-SLDLSGNQ-LTDLPEELANLTNLKELDLSNNQLTDL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  638 LNVLTDLQNLVSLNISYNDFSgDLPNtpffrrlPLSDLASNRGLYIS-NAISTRPDP 693
Cdd:COG4886   152 PEPLGNLTNLKSLDLSNNQLT-DLPE-------ELGNLTNLKELDLSnNQITDLPEP 200
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
800-966 1.53e-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: 53.94  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  800 NSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEARYdVVLGVAHALAYLHHDclpTI 879
Cdd:cd14084    59 ETEIEILKKLSHPCIIKIEDFFDAEDDYYIVLELMEGGELFDRV--VSNKRLKEAICKL-YFYQMLLAVKYLHSN---GI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  880 IHGDVKAMNVLLGPHFEPYL---ADFGLARtisgypNTGIDLAKPTnrppMAGSYGYMAPE---HASMQRITEKSDVYSY 953
Cdd:cd14084   133 IHRDLKPENVLLSSQEEECLikiTDFGLSK------ILGETSLMKT----LCGTPTYLAPEvlrSFGTEGYTRAVDCWSL 202
                         170
                  ....*....|...
gi 240256081  954 GVVLLEVLTGKHP 966
Cdd:cd14084   203 GVILFICLSGYPP 215
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
765-968 1.53e-07

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: 53.97  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSG--VVYRITipSGESLAV------KKMWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:cd08221     7 VLGRGAFGeaVLYRKT--EDNSLVVwkevnlSRLSEKERRDALN-EIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHgAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgi 916
Cdd:cd08221    84 GNLHDKIA-QQKNQLFPEEVVLWYLYQIVSAVSHIHKA---GILHRDIKTLNIFLTKADLVKLGDFGISKVLDS------ 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  917 dlakptnRPPMAGSY----GYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd08221   154 -------ESSMAESIvgtpYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFD 202
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
766-966 1.58e-07

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: 54.05  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGES--LAVKKM---------WSKEESGAFN---SEIKTLGS-IRHRNIVRLLG-WCSNRNLKLL 829
Cdd:cd08528     8 LGSGAFGCVYKVRKKSNGQtlLALKEInmtnpafgrTEQERDKSVGdiiSEVNIIKEqLRHPNIVRYYKtFLENDRLYIV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 --FYDYLPNGSLSSRLHGagKGGCVDWEARYDVVLGVAHALAYLHHDclPTIIHGDVKAMNVLLGPHFEPYLADFGLARt 907
Cdd:cd08528    88 meLIEGAPLGEHFSSLKE--KNEHFTEDRIWNIFVQMVLALRYLHKE--KQIVHRDLKPNNIMLGEDDKVTITDFGLAK- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  908 isgypNTGIDLAKPTNrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd08528   163 -----QKGPESSKMTS---VVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPP 213
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
765-967 1.71e-07

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: 54.23  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITI-PSGESLA---VKKMWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd14166    10 VLGSGAFSEVYLVKQrSTGKLYAlkcIKKSPLSRDSSLEN-EIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAGkggcVDWEARYDVVLG-VAHALAYLHHDclpTIIHGDVKAMNVL-LGP--HFEPYLADFGLARTisgyPNTGI 916
Cdd:cd14166    89 DRILERG----VYTEKDASRVINqVLSAVKYLHEN---GIVHRDLKPENLLyLTPdeNSKIMITDFGLSKM----EQNGI 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  917 dlakptnRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14166   158 -------MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPF 201
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
855-967 1.80e-07

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: 54.30  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  855 EARyDVVLGVAHALAYLHhDCLPTIIHGDVKAMNVLL---GPHFEPYLADFGLARTISGYPNTGIDLAKPTNRPpmAGSY 931
Cdd:cd14041   112 EAR-SIIMQIVNALKYLN-EIKPPIIHYDLKPGNILLvngTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQG--AGTY 187
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 240256081  932 GYMAPE----HASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14041   188 WYLPPEcfvvGKEPPKISNKVDVWSVGVIFYQCLYGRKPF 227
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
765-967 1.80e-07

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: 53.95  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM-WSKEESGAFNSEIKTLGSI-RHRNIVRLLGWCSNRNLK------LLFYDYLP 835
Cdd:cd06637    13 LVGNGTYGQVYKgRHVKTGQLAAIKVMdVTGDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKNPPgmddqlWLVMEFCG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGAgKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFG----LARTIsGY 911
Cdd:cd06637    93 AGSVTDLIKNT-KGNTLKEEWIAYICREILRGLSHLHQH---KVIHRDIKGQNVLLTENAEVKLVDFGvsaqLDRTV-GR 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  912 PNTGIdlakptnrppmaGSYGYMAPEHASMQRITE-----KSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd06637   168 RNTFI------------GTPYWMAPEVIACDENPDatydfKSDLWSLGITAIEMAEGAPPL 216
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
766-977 1.80e-07

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: 54.57  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVV-YRITIPSGESLAVKKMWSKEESGAFNS----EIKTLGSIRHRNIVRLLG-WCSNRNLKLL--FYDYLP-N 836
Cdd:cd07880    23 VGSGAYGTVcSALDRRTGAKVAIKKLYRPFQSELFAKrayrELRLLKHMKHENVIGLLDvFTPDLSLDRFhdFYLVMPfM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGGcvdwEARYD-VVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLAR----TISGY 911
Cdd:cd07880   103 GTDLGKLMKHEKLS----EDRIQfLVYQMLKGLKYIHA---AGIIHRDLKPGNLAVNEDCELKILDFGLARqtdsEMTGY 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  912 PNTgidlakptnrppmagsYGYMAPEHA-SMQRITEKSDVYSYGVVLLEVLTGKhpldPDLPGGAHL 977
Cdd:cd07880   176 VVT----------------RWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGK----PLFKGHDHL 222
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
766-963 1.87e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 53.79  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT---IPSGESLAVKKMWSKEESGA------FNSEIKTLGSIR-HRNIVRLLG-----WCSNRNLKLLF 830
Cdd:cd14020     8 LGQGSSASVYRVSsgrGADQPTSALKEFQLDHQGSQesgdygFAKERAALEQLQgHRNIVTLYGvftnhYSANVPSRCLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 YDYLpNGSLSSRLHGAGKGGCVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPY-LADFGLArtis 909
Cdd:cd14020    88 LELL-DVSVSELLLRSSNQGCSMWMIQH-CARDVLEALAFLHHE---GYVHADLKPRNILWSAEDECFkLIDFGLS---- 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  910 gypntgidlAKPTNRP-PMAGSYGYMAPE--------HASMQRITEKS---DVYSYGVVLLEVLTG 963
Cdd:cd14020   159 ---------FKEGNQDvKYIQTDGYRAPEaelqnclaQAGLQSETECTsavDLWSLGIVLLEMFSG 215
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
791-962 1.94e-07

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: 53.56  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  791 WSKEESGAFNSEIK--------TLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEARYDVVL 862
Cdd:cd14043    27 WLKKFPGGSHTELRpstknvfsKLRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLL--RNDDMKLDWMFKSSLLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  863 GVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYpntgiDLAKPTNRPpmaGSYGYMAPE----H 938
Cdd:cd14043   105 DLIKGMRYLHH---RGIVHGRLKSRNCVVDGRFVLKITDYGYNEILEAQ-----NLPLPEPAP---EELLWTAPEllrdP 173
                         170       180
                  ....*....|....*....|....
gi 240256081  939 ASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd14043   174 RLERRGTFPGDVFSFAIIMQEVIV 197
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
785-962 2.01e-07

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: 53.84  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  785 LAVKKMWSKEESGA---FNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS---SRLHGAGKGGC------V 852
Cdd:cd05095    49 VAVKMLRADANKNArndFLKEIKIMSRLKDPNIIRLLAVCITDDPLCMITEYMENGDLNqflSRQQPEGQLALpsnaltV 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  853 DWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTI-SGypntgiDLAKPTNRPPMagSY 931
Cdd:cd05095   129 SYSDLRFMAAQIASGMKYLSS---LNFVHRDLATRNCLVGKNYTIKIADFGMSRNLySG------DYYRIQGRAVL--PI 197
                         170       180       190
                  ....*....|....*....|....*....|.
gi 240256081  932 GYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05095   198 RWMSWESILLGKFTTASDVWAFGVTLWETLT 228
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
880-1038 2.13e-07

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: 54.22  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  880 IHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLE 959
Cdd:cd05103   201 IHRDLAARNILLSENNVVKICDFGLARDIYKDPDY---VRKGDARLPLK----WMAPETIFDRVYTIQSDVWSFGVLLWE 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  960 VLT-GKHPldpdLPGgahlVKWVRDHLAEKKDPSRLLDPrldgrtDSIMHEMLQTLavaFLCVSNKANERPLMKDVVAML 1038
Cdd:cd05103   274 IFSlGASP----YPG----VKIDEEFCRRLKEGTRMRAP------DYTTPEMYQTM---LDCWHGEPSQRPTFSELVEHL 336
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
766-966 2.19e-07

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: 53.68  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP-SGESLAVKKMWSKE------ESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd05577     1 LGRGGFGEVCACQVKaTGKMYACKKLDKKRikkkkgETMALN-EKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGAGKGGCVDWEARY---DVVLGVAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYpntg 915
Cdd:cd05577    80 LKYHIYNVGTRGFSEARAIFyaaEIICGLEH----LHNR---FIVYRDLKPENILLDDHGHVRISDLGLAVEFKGG---- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  916 idlAKPTNRppmAGSYGYMAPEHASMQRITEKS-DVYSYGVVLLEVLTGKHP 966
Cdd:cd05577   149 ---KKIKGR---VGTHGYMAPEVLQKEVAYDFSvDWFALGCMLYEMIAGRSP 194
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
802-967 2.26e-07

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: 53.80  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRL---LGWCSNRNLKLLFyDYLPNGSLssrLHGAGKGGCVDWEARY---DVVLGvahaLAYLHHDc 875
Cdd:cd14200    73 EIAILKKLDHVNIVKLievLDDPAEDNLYMVF-DLLRKGPV---MEVPSDKPFSEDQARLyfrDIVLG----IEYLHYQ- 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  876 lpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgidlaKPTNRPPMAGSYGYMAPEHAS--MQRITEKS-DVYS 952
Cdd:cd14200   144 --KIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEG---------NDALLSSTAGTPAFMAPETLSdsGQSFSGKAlDVWA 212
                         170
                  ....*....|....*
gi 240256081  953 YGVVLLEVLTGKHPL 967
Cdd:cd14200   213 MGVTLYCFVYGKCPF 227
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
755-967 2.26e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 54.46  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  755 DIVKNLTSanvigtGSSGVVYRITIPSGESLavKKMWSKEESGAFN--SEIKTLGSIRHRNIVRLLGWCSNRNLKLLF-- 830
Cdd:PHA03207   95 NILSSLTP------GSEGEVFVCTKHGDEQR--KKVIVKAVTGGKTpgREIDILKTISHRAIINLIHAYRWKSTVCMVmp 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 -YDYlpngSLSSRLHGAGKggcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS 909
Cdd:PHA03207  167 kYKC----DLFTYVDRSGP---LPLEQAITIQRRLLEALAYLHGR---GIIHRDVKTENIFLDEPENAVLGDFGAACKLD 236
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  910 GYPNTgidlakptnrPPMAGSYGYM---APEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:PHA03207  237 AHPDT----------PQCYGWSGTLetnSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTL 287
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
765-968 2.26e-07

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: 53.18  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKMwSKEESGAFN------SEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd14663     7 TLGEGTFAKVKFaRNTKTGESVAIKII-DKEQVAREGmveqikREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGKggCVDWEAR-YDVVLgvAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGi 916
Cdd:cd14663    86 ELFSKIAKNGR--LKEDKARkYFQQL--IDAVDYCHSR---GVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFRQDG- 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  917 dLAKPTnrppmAGSYGYMAPEHASmQR--ITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14663   158 -LLHTT-----CGTPNYVAPEVLA-RRgyDGAKADIWSCGVILFVLLAGYLPFD 204
pknD PRK13184
serine/threonine-protein kinase PknD;
868-966 2.41e-07

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 55.16  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  868 LAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISG---------YPNTGIDLAKPTNRPPMAGSYGYMAPEH 938
Cdd:PRK13184  126 IEYVHSK---GVLHRDLKPDNILLGLFGEVVILDWGAAIFKKLeeedlldidVDERNICYSSMTIPGKIVGTPDYMAPER 202
                          90       100
                  ....*....|....*....|....*...
gi 240256081  939 ASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:PRK13184  203 LLGVPASESTDIYALGVILYQMLTLSFP 230
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
766-964 2.63e-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: 53.95  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT---IPSGESLAVKKMwskeeSGAFNSEIKTLGSIR----------HRNIVRLLG----WCSNRNlKL 828
Cdd:cd07857     8 LGQGAYGIVCSARnaeTSEEETVAIKKI-----TNVFSKKILAKRALRelkllrhfrgHKNITCLYDmdivFPGNFN-EL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSSRLHGagkggcvdwearyDVVLGVAH----------ALAYLHHdclPTIIHGDVKAMNVLLGPHFEPY 898
Cdd:cd07857    82 YLYEELMEADLHQIIRS-------------GQPLTDAHfqsfiyqilcGLKYIHS---ANVLHRDLKPGNLLVNADCELK 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  899 LADFGLARTISgyPNTGIDLAKPTNrppMAGSYGYMAPE-HASMQRITEKSDVYSYGVVLLEVLTGK 964
Cdd:cd07857   146 ICDFGLARGFS--ENPGENAGFMTE---YVATRWYRAPEiMLSFQSYTKAIDVWSVGCILAELLGRK 207
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
785-966 2.80e-07

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: 53.41  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  785 LAVKKMWSKEESgAFNSEIKTLGSIRHR----NIVRLLGWCSNRNLkLLFYDYLPNGSLSSRLhgAGKGGCVDWEARYDV 860
Cdd:cd05115    34 VAIKVLKQGNEK-AVRDEMMREAQIMHQldnpYIVRMIGVCEAEAL-MLVMEMASGGPLNKFL--SGKKDEITVSNVVEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  861 VLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypntGIDLAKPTNRPPMAGSYGYMAPEHAS 940
Cdd:cd05115   110 MHQVSMGMKYLEEK---NFVHRDLAARNVLLVNQHYAKISDFGLSKAL------GADDSYYKARSAGKWPLKWYAPECIN 180
                         170       180
                  ....*....|....*....|....*..
gi 240256081  941 MQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05115   181 FRKFSSRSDVWSYGVTMWEAFSyGQKP 207
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
867-966 2.90e-07

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: 53.12  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  867 ALAYLHHDclpTIIHGDVKAMNVLLG---PHFEPYLADFGLARTIsgypNTGIDLAKptnrppMAGSYGYMAPEHASMQR 943
Cdd:cd14106   120 GVQYLHER---NIVHLDLKPQNILLTsefPLGDIKLCDFGISRVI----GEGEEIRE------ILGTPDYVAPEILSYEP 186
                          90       100
                  ....*....|....*....|...
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14106   187 ISLATDMWSIGVLTYVLLTGHSP 209
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
765-974 2.94e-07

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: 53.08  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIPS-GESLAVKKmwSKEESGAFNSEIKTLGSIR-------HRNIVRLL-GWCSNRNLKLlfYDYLP 835
Cdd:cd14050     8 KLGEGSFGEVFKVRSREdGKLYAVKR--SRSRFRGEKDRKRKLEEVErheklgeHPNCVRFIkAWEEKGILYI--QTELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLHGAGKGGCVD-WEARYDVVLGVAHAlaylhHDClpTIIHGDVKAMNVLLGPHFEPYLADFGLArtisgypnt 914
Cdd:cd14050    84 DTSLQQYCEETHSLPESEvWNILLDLLKGLKHL-----HDH--GLIHLDIKPANIFLSKDGVCKLGDFGLV--------- 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  915 gIDLAKPTNRPPMAGSYGYMAPEhaSMQ-RITEKSDVYSYGVVLLEVLTgkhplDPDLPGG 974
Cdd:cd14050   148 -VELDKEDIHDAQEGDPRYMAPE--LLQgSFTKAADIFSLGITILELAC-----NLELPSG 200
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
802-972 3.14e-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: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGKGGcvDWEARY---DVVLGVahalAYLHHdclPT 878
Cdd:cd14662    46 EIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGELFERICNAGRFS--EDEARYffqQLISGV----SYCHS---MQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHFEPYL--ADFglartisGYPNTGIDLAKPTNrppMAGSYGYMAPEHASMQRITEK-SDVYSYGV 955
Cdd:cd14662   117 ICHRDLKLENTLLDGSPAPRLkiCDF-------GYSKSSVLHSQPKS---TVGTPAYIAPEVLSRKEYDGKvADVWSCGV 186
                         170
                  ....*....|....*...
gi 240256081  956 VLLEVLTGKHPL-DPDLP 972
Cdd:cd14662   187 TLYVMLVGAYPFeDPDDP 204
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
766-973 3.26e-07

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 53.43  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGA-FNS--EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLpNGSLSS 841
Cdd:cd07870     8 LGEGSYATVYKgISRINGQLVALKVISMKTEEGVpFTAirEASLLKGLKHANIVLLHDIIHTKETLTFVFEYM-HTDLAQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RL--HGAGKGGCVDWEARYDVVLGvahaLAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNT-GIDL 918
Cdd:cd07870    87 YMiqHPGGLHPYNVRLFMFQLLRG----LAYIHGQ---HILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTySSEV 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  919 AKPTNRPP--MAGSYGYmapehasmqriTEKSDVYSYGVVLLEVLTGKhpldPDLPG 973
Cdd:cd07870   160 VTLWYRPPdvLLGATDY-----------SSALDIWGAGCIFIEMLQGQ----PAFPG 201
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
755-977 3.48e-07

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


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 53.34  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  755 DIVKNLTSANVIGTGSSGVVYRITIP-SGESLAVKKMWSKEESGAFNS----EIKTLGSIRHRNIVRLlgwcSNRNLKLL 829
Cdd:cd07856     7 EITTRYSDLQPVGMGAFGLVCSARDQlTGQNVAVKKIMKPFSTPVLAKrtyrELKLLKHLRHENIISL----SDIFISPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 FYDYLPNGSLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLART-- 907
Cdd:cd07856    83 EDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHS---AGVIHRDLKPSNILVNENCDLKICDFGLARIqd 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256081  908 --ISGYPNTgidlakptnrppmagSYgYMAPE-HASMQRITEKSDVYSYGVVLLEVLTGKhpldPDLPGGAHL 977
Cdd:cd07856   160 pqMTGYVST---------------RY-YRAPEiMLTWQKYDVEVDIWSAGCIFAEMLEGK----PLFPGKDHV 212
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
745-967 3.52e-07

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: 53.05  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  745 LYQKLDfsiddivknltSANVIGTGSSGVVYR-ITIPSGESLAVKKM----------WSKEESGAFNSEIKTLGSIR-HR 812
Cdd:cd14181     8 FYQKYD-----------PKEVIGRGVSSVVRRcVHRHTGQEFAVKIIevtaerlspeQLEEVRSSTLKEIHILRQVSgHP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  813 NIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEARyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLG 892
Cdd:cd14181    77 SIITLIDSYESSTFIFLVFDLMRRGELFDYL--TEKVTLSEKETR-SIMRSLLEAVSYLHAN---NIVHRDLKPENILLD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  893 PHFEPYLADFGLARTISgyPNTGIDlakptnrpPMAGSYGYMAPE--HASMQRITE----KSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14181   151 DQLHIKLSDFGFSCHLE--PGEKLR--------ELCGTPGYLAPEilKCSMDETHPgygkEVDLWACGVILFTLLAGSPP 220

                  .
gi 240256081  967 L 967
Cdd:cd14181   221 F 221
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
753-967 3.83e-07

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: 53.13  E-value: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  753 IDDIVKNLTSANVIGTGS-SGVVYRITIPSGESLAVK---KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKL 828
Cdd:cd14168     5 VEDIKKIFEFKEVLGTGAfSEVVLAEERATGKLFAVKcipKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSSRLhgAGKGGCVDWEARyDVVLGVAHALAYLHHdclPTIIHGDVKAMNVLlgpHFEP------YLADF 902
Cdd:cd14168    85 LVMQLVSGGELFDRI--VEKGFYTEKDAS-TLIRQVLDAVYYLHR---MGIVHRDLKPENLL---YFSQdeeskiMISDF 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  903 GLARTisgyPNTGIDLAKPTNRPpmagsyGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14168   156 GLSKM----EGKGDVMSTACGTP------GYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPF 210
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
864-968 4.15e-07

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: 53.17  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgypntGIDLAKPTNRppMAGSYGYMAPEHASMQR 943
Cdd:cd05582   106 LALALDHLHS---LGIIYRDLKPENILLDEDGHIKLTDFGLSKE-------SIDHEKKAYS--FCGTVEYMAPEVVNRRG 173
                          90       100
                  ....*....|....*....|....*
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd05582   174 HTQSADWWSFGVLMFEMLTGSLPFQ 198
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
802-972 4.21e-07

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: 52.39  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEAR---YDVVLgvahALAYLHHDclpT 878
Cdd:cd14071    49 EVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIFDYL--AQHGRMSEKEARkkfWQILS----AVEYCHKR---H 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHFEPYLADFGLartiSGYPNTGIDLAKPTNRPPmagsygYMAPEHASMQRIT-EKSDVYSYGVVL 957
Cdd:cd14071   120 IVHRDLKAENLLLDANMNIKIADFGF----SNFFKPGELLKTWCGSPP------YAAPEVFEGKEYEgPQLDIWSLGVVL 189
                         170
                  ....*....|....*.
gi 240256081  958 LEVLTGKHPLD-PDLP 972
Cdd:cd14071   190 YVLVCGALPFDgSTLQ 205
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
801-969 4.22e-07

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: 52.84  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  801 SEIKTLGSIRHRNIVRLLGWCSNRNLK-LLFYDYLPNGSL-----SSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHD 874
Cdd:cd05043    56 QESSLLYGLSHQNLLPILHVCIEDGEKpMVLYPYMNWGNLklflqQCRLSEANNPQALSTQQLVHMALQIACGMSYLHRR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  875 clpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgYPNTGIDLAKPTNRPpmagsYGYMAPEHASMQRITEKSDVYSYG 954
Cdd:cd05043   136 ---GVIHKDIAARNCVIDDELQVKITDNALSRDL--FPMDYHCLGDNENRP-----IKWMSLESLVNKEYSSASDVWSFG 205
                         170
                  ....*....|....*....
gi 240256081  955 VVLLEVLT-GKHP---LDP 969
Cdd:cd05043   206 VLLWELMTlGQTPyveIDP 224
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
839-1041 4.27e-07

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: 52.49  E-value: 4.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGAGKGGcVDWEARYDVVLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPYLADFGLART---ISGypntg 915
Cdd:cd13975    87 LHRDLYTGIKAG-LSLEERLQIALDVVEGIRFLHSQGL---VHRDIKLKNVLLDKKNRAKITDLGFCKPeamMSG----- 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  916 idlakptnrpPMAGSYGYMAPEHASmQRITEKSDVYSYGVVLLEVLTGKHPLdPDLPGGAHlvkwVRDHL----AEKKDP 991
Cdd:cd13975   158 ----------SIVGTPIHMAPELFS-GKYDNSVDVYAFGILFWYLCAGHVKL-PEAFEQCA----SKDHLwnnvRKGVRP 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  992 SRLldPRLDGRTDSIMHemlqtlavafLCVSNKANERPLMKDVVAMLTEI 1041
Cdd:cd13975   222 ERL--PVFDEECWNLME----------ACWSGDPSQRPLLGIVQPKLQGI 259
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
864-966 4.68e-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: 53.31  E-value: 4.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYL-HHDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidLAKPTNRPPMAgsygYMAPEHASMQ 942
Cdd:cd05106   221 VAQGMDFLaSKNC----IHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNY---VVKGNARLPVK----WMAPESIFDC 289
                          90       100
                  ....*....|....*....|....*
gi 240256081  943 RITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05106   290 VYTVQSDVWSYGILLWEIFSlGKSP 314
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
760-966 4.89e-07

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: 52.70  E-value: 4.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  760 LTSANVIGTGSSGVVYRITIPSGESL---AVKKM----WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLK----- 827
Cdd:cd05075     2 LALGKTLGEGEFGSVMEGQLNQDDSVlkvAVKTMkiaiCTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTESegyps 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  828 -LLFYDYLPNGSLSSRLHGAGKGGC---VDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd05075    82 pVVILPFMKHGDLHSFLLYSRLGDCpvyLPTQMLVKFMTDIASGMEYLSSK---NFIHRDLAARNCMLNENMNVCVADFG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  904 LARTI--SGYPNTGIDLAKPTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05075   159 LSKKIynGDYYRQGRISKMPVK---------WIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTP 215
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
802-964 5.40e-07

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: 52.58  E-value: 5.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGA---GKGGCVDWEARYDVVLGVAHALAYLHHDclPT 878
Cdd:cd14044    53 ELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKisyPDGTFMDWEFKISVMYDIAKGMSYLHSS--KT 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHFEPYLADFGLARTISgyPNTgiDLakptnrppmagsygYMAPEHASMQRITEKSDVYSYGVVLL 958
Cdd:cd14044   131 EVHGRLKSTNCVVDSRMVVKITDFGCNSILP--PSK--DL--------------WTAPEHLRQAGTSQKGDVYSYGIIAQ 192

                  ....*.
gi 240256081  959 EVLTGK 964
Cdd:cd14044   193 EIILRK 198
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
764-909 6.01e-07

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: 52.28  E-value: 6.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIP-SGESLAVKKM-WSKEESGAFNSEIKTLGSIR------HRNIVRLL----GWCSNRNLKL-LF 830
Cdd:cd07838     5 AEIGEGAYGTVYKARDLqDGRFVALKKVrVPLSEEGIPLSTIREIALLKqlesfeHPNVVRLLdvchGPRTDRELKLtLV 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  831 YDYLpNGSLSSRLHGAGKGGCVDWEARyDVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTIS 909
Cdd:cd07838    85 FEHV-DQDLATYLDKCPKPGLPPETIK-DLMRQLLRGLDFLHSHR---IVHRDLKPQNILVTSDGQVKLADFGLARIYS 158
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
142-419 6.19e-07

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 53.55  E-value: 6.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  142 KLKTLSLNTnnLEGHIPMEIgnlsglVELMLFDNKLSgEIPRSI-GELKNLQVlraggNKNLRGELPWEIGNCENLVMLG 220
Cdd:PRK15370  184 RLKILGLTT--IPACIPEQI------TTLILDNNELK-SLPENLqGNIKTLYA-----NSNQLTSIPATLPDTIQEMELS 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  221 LAE-TSLSGKLPASIgnlkrvQTIAIYTSLLSGpIPDEIGycTELQNLYLYQNSISG---SIPTTIgglkklqSLLLWQN 296
Cdd:PRK15370  250 INRiTELPERLPSAL------QSLDLFHNKISC-LPENLP--EELRYLSVYDNSIRTlpaHLPSGI-------THLNVQS 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  297 NLVGKIPTELGncPELWLIDFSENLLTgTIPRSFGKleNLQELQLSVNQISgTIPEELTncTKLTHLEIDNNLITGEIPS 376
Cdd:PRK15370  314 NSLTALPETLP--PGLKTLEAGENALT-SLPASLPP--ELQVLDVSKNQIT-VLPETLP--PTITTLDVSRNALTNLPEN 385
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 240256081  377 LMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLS 419
Cdd:PRK15370  386 LPAALQIMQASRNNLVRLPESLPHFRGEGPQPTRIIVEYNPFS 428
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
764-1020 6.76e-07

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: 51.95  E-value: 6.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGS-SGVVYRITIPSGESLAVKKMWSKEESGAFNS---EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd14167     9 EVLGTGAfSEVVLAEEKRTQKLVAIKCIAKKALEGKETSienEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLhgAGKGGCVDWEARyDVVLGVAHALAYLHHdclPTIIHGDVKAMNVL---LGPHFEPYLADFGLARtISGyPNTGI 916
Cdd:cd14167    89 FDRI--VEKGFYTERDAS-KLIFQILDAVKYLHD---MGIVHRDLKPENLLyysLDEDSKIMISDFGLSK-IEG-SGSVM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  917 DLAkptnrppmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPDlpGGAHLVKWVRDhlAEKKDPSRLLD 996
Cdd:cd14167   161 STA--------CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDE--NDAKLFEQILK--AEYEFDSPYWD 228
                         250       260
                  ....*....|....*....|....
gi 240256081  997 PRLDGRTDSIMHEMLQTLAVAFLC 1020
Cdd:cd14167   229 DISDSAKDFIQHLMEKDPEKRFTC 252
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
759-967 7.39e-07

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: 51.84  E-value: 7.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  759 NLTSANVIGTGSSGVVYR-ITIPSGESLAVK--KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLP 835
Cdd:cd14193     5 NVNKEEILGGGRFGQVHKcEEKSSGLKLAAKiiKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  836 NGSLSSRLhgagkggcVDWE---ARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGPH--FEPYLADFGLARTISG 910
Cdd:cd14193    85 GGELFDRI--------IDENynlTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSReaNQVKIIDFGLARRYKP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  911 YPNTGIDLAKPTnrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14193   157 REKLRVNFGTPE----------FLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPF 203
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
858-971 8.12e-07

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 51.94  E-value: 8.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  858 YDVV-----LGVAHALAYLHHDClpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS--GYPNTGIDLAKPTNRPPMAGS 930
Cdd:cd14011   112 YDVEikyglLQISEALSFLHNDV--KLVHGNICPESVVINSNGEWKLAGFDFCISSEqaTDQFPYFREYDPNLPPLAQPN 189
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 240256081  931 YGYMAPEHASMQRITEKSDVYSYGVVLLEVL-TGKHPLDPDL 971
Cdd:cd14011   190 LNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVN 231
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
766-967 9.03e-07

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: 52.04  E-value: 9.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKM-WSKEESGAFNS---EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLpNGSLS 840
Cdd:cd07861     8 IGEGTYGVVYKgRNKKTGQIVAMKKIrLESEEEGVPSTairEISLLKELQHPNIVCLEDVLMQENRLYLVFEFL-SMDLK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypntGIDLAK 920
Cdd:cd07861    87 KYLDSLPKGKYMDAELVKSYLYQILQGILFCHSR---RVLHRDLKPQNLLIDNKGVIKLADFGLARAF------GIPVRV 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  921 PTNRppmAGSYGYMAPE-HASMQRITEKSDVYSYGVVLLEVLTgKHPL 967
Cdd:cd07861   158 YTHE---VVTLWYRAPEvLLGSPRYSTPVDIWSIGTIFAEMAT-KKPL 201
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
766-967 9.30e-07

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: 51.96  E-value: 9.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVY--RITIPSGESLAVKKMWSK-EESGAFNSEIKTLGSIR------HRNIVRLLGWCS----NRNLKL-LFY 831
Cdd:cd07862     9 IGEGAYGKVFkaRDLKNGGRFVALKRVRVQtGEEGMPLSTIREVAVLRhletfeHPNVVRLFDVCTvsrtDRETKLtLVF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLpNGSLSSRLHGAGKGGcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGY 911
Cdd:cd07862    89 EHV-DQDLTTYLDKVPEPG-VPTETIKDMMFQLLRGLDFLHSH---RVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQ 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  912 PNTGIDLAkptnrppmagSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTgKHPL 967
Cdd:cd07862   164 MALTSVVV----------TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFR-RKPL 208
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
864-1040 9.41e-07

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: 9.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYL-HHDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidLAKPTNRPPMAgsygYMAPEHASMQ 942
Cdd:cd05104   223 VAKGMEFLaSKNC----IHRDLAARNILLTHGRITKICDFGLARDIRNDSNY---VVKGNARLPVK----WMAPESIFEC 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  943 RITEKSDVYSYGVVLLEVLT-GKHPLdPDLPGGAHLVKWVrdhlaekKDPSRLLDPRLdgrTDSIMHEMLQTlavaflCV 1021
Cdd:cd05104   292 VYTFESDVWSYGILLWEIFSlGSSPY-PGMPVDSKFYKMI-------KEGYRMDSPEF---APSEMYDIMRS------CW 354
                         170
                  ....*....|....*....
gi 240256081 1022 SNKANERPLMKDVVAMLTE 1040
Cdd:cd05104   355 DADPLKRPTFKQIVQLIEQ 373
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
765-967 1.00e-06

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: 51.45  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVK--------KMWSKEESGAFNSEIKTLGSIR----HRNIVRLLGWCSNRNLKLLFY 831
Cdd:cd14182    10 ILGRGVSSVVRRcIHKPTRQEYAVKiiditgggSFSPEEVQELREATLKEIDILRkvsgHPNIIQLKDTYETNTFFFLVF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLPNGSLSSRLhgAGKGGCVDWEARyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLArtisgy 911
Cdd:cd14182    90 DLMKKGELFDYL--TEKVTLSEKETR-KIMRALLEVICALHKL---NIVHRDLKPENILLDDDMNIKLTDFGFS------ 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  912 pntgIDLAKPTNRPPMAGSYGYMAPE--HASM----QRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14182   158 ----CQLDPGEKLREVCGTPGYLAPEiiECSMddnhPGYGKEVDMWSTGVIMYTLLAGSPPF 215
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
758-968 1.05e-06

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: 51.47  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVYRIT-IPSGESLAVK-----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFY 831
Cdd:cd14189     1 RSYCKGRLLGKGGFARCYEMTdLATNKTYAVKviphsRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLPNGSLSSRLHGagKGGCVDWEARYdVVLGVAHALAYLHhdcLPTIIHGDVKAMNVLLGPHFEPYLADFGLA------ 905
Cdd:cd14189    81 ELCSRKSLAHIWKA--RHTLLEPEVRY-YLKQIISGLKYLH---LKGILHRDLKLGNFFINENMELKVGDFGLAarlepp 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  906 ----RTISGYPNtgidlakptnrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14189   155 eqrkKTICGTPN-------------------YLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFE 202
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
766-969 1.09e-06

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: 51.54  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESL-AVKKMWSKEESGAFNS---EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLpNGSLSS 841
Cdd:cd07873    10 LGEGTYATVYKGRSKLTDNLvALKEIRLEHEEGAPCTairEVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYL-DKDLKQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGAGKggCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS----GYPNTGID 917
Cdd:cd07873    89 YLDDCGN--SINMHNVKLFLFQLLRGLAYCHRR---KVLHRDLKPQNLLINERGELKLADFGLARAKSiptkTYSNEVVT 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  918 LAKptnRPP--MAGSYGYmapehasmqriTEKSDVYSYGVVLLEVLTGKhPLDP 969
Cdd:cd07873   164 LWY---RPPdiLLGSTDY-----------STQIDMWGVGCIFYEMSTGR-PLFP 202
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
766-1043 1.11e-06

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: 51.51  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR---ITIPSGES---LAVKKM---WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:cd05061    14 LGQGSFGMVYEgnaRDIIKGEAetrVAVKTVnesASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHgagkggCVDWEARYD-------------VVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd05061    94 GDLKSYLR------SLRPEAENNpgrppptlqemiqMAAEIADGMAYLNAK---KFVHRDLAARNCMVAHDFTVKIGDFG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  904 LARTI--SGYPNTGIDLAKPTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLDPdlPGGAHLVKW 980
Cdd:cd05061   165 MTRDIyeTDYYRKGGKGLLPVR---------WMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQG--LSNEQVLKF 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  981 VRD--HLAEKKD-PSRlldprldgrtdsiMHEMLQtlavafLCVSNKANERPLMKDVVAMLTEIRH 1043
Cdd:cd05061   234 VMDggYLDQPDNcPER-------------VTDLMR------MCWQFNPKMRPTFLEIVNLLKDDLH 280
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
766-966 1.18e-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: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIP-SGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLh 844
Cdd:cd14085    11 LGRGATSVVYRCRQKgTQKPYAVKKLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRI- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  845 gAGKGGCVDWEARyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVL---LGPHFEPYLADFGLARTISGypntgiDLAKP 921
Cdd:cd14085    90 -VEKGYYSERDAA-DAVKQILEAVAYLHEN---GIVHRDLKPENLLyatPAPDAPLKIADFGLSKIVDQ------QVTMK 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 240256081  922 TnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14085   159 T----VCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEP 199
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
792-966 1.35e-06

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: 51.26  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  792 SKEESGAFNSEIKTLGSIRHRNIVRLL-GWCS---NRNLKLLFYDYLPNGSLSSRLHgagKGGCVDWEARYDVVLGVAHA 867
Cdd:cd14031    49 TKAEQQRFKEEAEMLKGLQHPNIVRFYdSWESvlkGKKCIVLVTELMTSGTLKTYLK---RFKVMKPKVLRSWCRQILKG 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  868 LAYLHHDClPTIIHGDVKAMNVLL-GPHFEPYLADFGLArtisgypntgiDLAKPTNRPPMAGSYGYMAPEHASmQRITE 946
Cdd:cd14031   126 LQFLHTRT-PPIIHRDLKCDNIFItGPTGSVKIGDLGLA-----------TLMRTSFAKSVIGTPEFMAPEMYE-EHYDE 192
                         170       180
                  ....*....|....*....|
gi 240256081  947 KSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14031   193 SVDVYAFGMCMLEMATSEYP 212
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
341-583 1.37e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 52.39  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  341 LSVNQISGTIPEELTNctklthLEIDNNlitgEIPSLMSNLR-SLTMFFAWQNKLTgNIPQSLSQcrELQAIDLSYNSLS 419
Cdd:PRK15370  188 LGLTTIPACIPEQITT------LILDNN----ELKSLPENLQgNIKTLYANSNQLT-SIPATLPD--TIQEMELSINRIT 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  420 gsipkeifglrnltkllllsnDLSGFIPpdigncTNLYRLRLNGNRLAG---SIPSEignLKNLNFVDISENRLVGSIPP 496
Cdd:PRK15370  255 ---------------------ELPERLP------SALQSLDLFHNKISClpeNLPEE---LRYLSVYDNSIRTLPAHLPS 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  497 AISgcesleFLDLHTNSLSgsLLGTTLPKSLKFIDFSDNALSS---TLPPgiglltELTKLNLAKNR---LSGEIPREIS 570
Cdd:PRK15370  305 GIT------HLNVQSNSLT--ALPETLPPGLKTLEAGENALTSlpaSLPP------ELQVLDVSKNQitvLPETLPPTIT 370
                         250
                  ....*....|....*.
gi 240256081  571 TC---RSLqLLNLGEN 583
Cdd:PRK15370  371 TLdvsRNA-LTNLPEN 385
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
786-966 1.43e-06

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: 51.06  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  786 AVKKMW--SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL-------SSRLhgagkggcvDWEA 856
Cdd:cd14042    34 AIKKVNkkRIDLTREVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLqdileneDIKL---------DWMF 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  857 RY----DVVLGvahaLAYLHhdCLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDLAKPTNRPpmagsyg 932
Cdd:cd14042   105 RYslihDIVKG----MHYLH--DSEIKSHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPPDDSHAYYAKLL------- 171
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 240256081  933 YMAPEHASMQRI----TEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14042   172 WTAPELLRDPNPpppgTQKGDVYSFGIILQEIATRQGP 209
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
766-966 1.44e-06

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: 51.20  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-----ITIPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLL-GWCS---NRNLKLLFYDYLPN 836
Cdd:cd14030    33 IGRGSFKTVYKgldteTTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYdSWEStvkGKKCIVLVTELMTS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHgagKGGCVDWEARYDVVLGVAHALAYLHHDClPTIIHGDVKAMNVLL-GPHFEPYLADFGLArtisgypntg 915
Cdd:cd14030   113 GTLKTYLK---RFKVMKIKVLRSWCRQILKGLQFLHTRT-PPIIHRDLKCDNIFItGPTGSVKIGDLGLA---------- 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  916 iDLAKPTNRPPMAGSYGYMAPEHASmQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14030   179 -TLKRASFAKSVIGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYP 227
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
764-966 1.50e-06

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: 50.79  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYRITIPS-GESLAVK-----KMWSKEEsgAFNSEIKTLGSIRHRNIVRLLG-WCSNRNLKLLFyDYLPN 836
Cdd:cd14095     6 RVIGDGNFAVVKECRDKAtDKEYALKiidkaKCKGKEH--MIENEVAILRRVKHPNIVQLIEeYDTDTELYLVM-ELVKG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGGCVDwEARYdvVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHfEPY-----LADFGLAR----- 906
Cdd:cd14095    83 GDLFDAITSSTKFTERD-ASRM--VTDLAQALKYLHSL---SIVHRDIKPENLLVVEH-EDGskslkLADFGLATevkep 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  907 --TISGYPNtgidlakptnrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14095   156 lfTVCGTPT-------------------YVAPEILAETGYGLKVDIWAAGVITYILLCGFPP 198
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
783-966 1.87e-06

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: 50.79  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  783 ESLAVKKMWSKEEsGAFNSEIKTLGSIR----HRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRL-----HGAGKGGCVD 853
Cdd:cd05091    37 QAVAIKTLKDKAE-GPLREEFRHEAMLRsrlqHPNIVCLLGVVTKEQPMSMIFSYCSHGDLHEFLvmrspHSDVGSTDDD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  854 WEAR--------YDVVLGVAHALAYL--HHdclptIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgypnTGIDLAKPTN 923
Cdd:cd05091   116 KTVKstlepadfLHIVTQIAAGMEYLssHH-----VVHKDLATRNVLVFDKLNVKISDLGLFREV-----YAADYYKLMG 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 240256081  924 RPPMAgsYGYMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05091   186 NSLLP--IRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQP 227
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
858-972 1.88e-06

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 51.55  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  858 YDVVLG----VAHALAYL-HHDClptiIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidLAKPTNRPPMAgsyg 932
Cdd:cd05107   238 YMDLVGfsyqVANGMEFLaSKNC----VHRDLAARNVLICEGKLVKICDFGLARDIMRDSNY---ISKGSTFLPLK---- 306
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 240256081  933 YMAPEHASMQRITEKSDVYSYGVVLLEVLT-GKHPLdPDLP 972
Cdd:cd05107   307 WMAPESIFNNLYTTLSDVWSFGILLWEIFTlGGTPY-PELP 346
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
765-966 2.03e-06

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: 51.00  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM---WSKEESGAFNSEIKTLGSI----RHRNIVRLLGWCSNRNLKLLFYDYLPN 836
Cdd:cd14094    10 VIGKGPFSVVRRcIHRETGQQFAVKIVdvaKFTSSPGLSTEDLKREASIchmlKHPHIVELLETYSSDGMLYMVFEFMDG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHGAGKGGCVDWEA---RYdvVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGP--HFEPY-LADFGLARTIsg 910
Cdd:cd14094    90 ADLCFEIVKRADAGFVYSEAvasHY--MRQILEALRYCHDN---NIIHRDVKPHCVLLASkeNSAPVkLGGFGVAIQL-- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  911 yPNTGIDLAKPTNRPPmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14094   163 -GESGLVAGGRVGTPH------FMAPEVVKREPYGKPVDVWGCGVILFILLSGCLP 211
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
801-966 2.24e-06

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: 50.39  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  801 SEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAG--KGGCVDWEARYdvvlgVAHALAYLHHDclpT 878
Cdd:cd13995    45 SDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEKLESCGpmREFEIIWVTKH-----VLKGLDFLHSK---N 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHfEPYLADFGLARTISGypntgiDLAKPTNrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLL 958
Cdd:cd13995   117 IIHHDIKPSNIVFMST-KAVLVDFGLSVQMTE------DVYVPKD---LRGTEIYMSPEVILCRGHNTKADIYSLGATII 186

                  ....*...
gi 240256081  959 EVLTGKHP 966
Cdd:cd13995   187 HMQTGSPP 194
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
802-982 2.71e-06

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: 50.18  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEARY---DVVLGVAhalaYLHHDclpT 878
Cdd:cd14076    56 EINILKGLTHPNIVRLLDVLKTKKYIGIVLEFVSGGELFDYI--LARRRLKDSVACRlfaQLISGVA----YLHKK---G 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHFEPYLADFGLARTIsgYPNTGiDLAKPTnrppmAGSYGYMAPEHASMQRITE--KSDVYSYGVV 956
Cdd:cd14076   127 VVHRDLKLENLLLDKNRNLVITDFGFANTF--DHFNG-DLMSTS-----CGSPCYAAPELVVSDSMYAgrKADIWSCGVI 198
                         170       180
                  ....*....|....*....|....*...
gi 240256081  957 LLEVLTGKHPL--DPDLPGGAHLVKWVR 982
Cdd:cd14076   199 LYAMLAGYLPFddDPHNPNGDNVPRLYR 226
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
729-1013 2.82e-06

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 50.59  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  729 AGKQLLGEEIDSWEVTlyqklDFSIDDivknltsanVIGTGSSGVVyRIT--IPSGESLAVKKMWSKE-----ESGAFNS 801
Cdd:PTZ00263    3 AAYMFTKPDTSSWKLS-----DFEMGE---------TLGTGSFGRV-RIAkhKGTGEYYAIKCLKKREilkmkQVQHVAQ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLL-GWCSNRNLKLLFyDYLPNGSLSSRLHGAGKGGCvDWEARY--DVVLgvahALAYLHHDclpT 878
Cdd:PTZ00263   68 EKSILMELSHPFIVNMMcSFQDENRVYFLL-EFVVGGELFTHLRKAGRFPN-DVAKFYhaELVL----AFEYLHSK---D 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidlakptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLL 958
Cdd:PTZ00263  139 IIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFT------------LCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLY 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  959 EVLTGKHPLDPDLPGGAHlvkwvrdhlaEKKDPSRLLDPR-LDGRTDSIMHEMLQT 1013
Cdd:PTZ00263  207 EFIAGYPPFFDDTPFRIY----------EKILAGRLKFPNwFDGRARDLVKGLLQT 252
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
766-968 2.86e-06

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: 50.08  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVK-----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd14073     9 LGKGTYGKVKLAIeRATGREVAIKsikkdKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLhgAGKGGCVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLA---------RTISG 910
Cdd:cd14073    89 YDYI--SERRRLPEREARR-IFRQIVSAVHYCHKN---GVVHRDLKLENILLDQNGNAKIADFGLSnlyskdkllQTFCG 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  911 YPNtgidLAKP--TNRPPmagsygYMAPEhasmqritekSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14073   163 SPL----YASPeiVNGTP------YQGPE----------VDCWSLGVLLYTLVYGTMPFD 202
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
746-974 3.47e-06

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 50.07  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  746 YQKLDfsiddivknltsanVIGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGA-FNS--EIKTLGSIRHRNIVRLLGWC 821
Cdd:cd07844     2 YKKLD--------------KLGEGSYATVYKgRSKLTGQLVALKEIRLEHEEGApFTAirEASLLKDLKHANIVTLHDII 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  822 SNRNLKLLFYDYLpNGSLSSRLHGAGKGGCVDwearyDVVL---GVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPY 898
Cdd:cd07844    68 HTKKTLTLVFEYL-DTDLKQYMDDCGGGLSMH-----NVRLflfQLLRGLAYCHQR---RVLHRDLKPQNLLISERGELK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  899 LADFGLARTIS----GYPNTGIDLAKptnRPP--MAGSYGYmapehasmqriTEKSDVYSYGVVLLEVLTGKhpldPDLP 972
Cdd:cd07844   139 LADFGLARAKSvpskTYSNEVVTLWY---RPPdvLLGSTEY-----------STSLDMWGVGCIFYEMATGR----PLFP 200

                  ..
gi 240256081  973 GG 974
Cdd:cd07844   201 GS 202
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
860-966 3.58e-06

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: 49.63  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  860 VVLGVAHALAYLHHDCLptiIHGDVKAMNVLLgphFEPY-----LADFGLARtisgypntgidlAKPTNRPPMAGSYGYM 934
Cdd:cd13987    96 CAAQLASALDFMHSKNL---VHRDIKPENVLL---FDKDcrrvkLCDFGLTR------------RVGSTVKRVSGTIPYT 157
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 240256081  935 APEHASMQR----ITEKS-DVYSYGVVLLEVLTGKHP 966
Cdd:cd13987   158 APEVCEAKKnegfVVDPSiDVWAFGVLLFCCLTGNFP 194
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
792-966 3.64e-06

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: 49.69  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  792 SKEESGAFNSEIKTLGSIRHRNIVRLLG-WCSNRNLK---LLFYDYLPNGSLSSRLHgagKGGCVDWEARYDVVLGVAHA 867
Cdd:cd14032    40 TKVERQRFKEEAEMLKGLQHPNIVRFYDfWESCAKGKrciVLVTELMTSGTLKTYLK---RFKVMKPKVLRSWCRQILKG 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  868 LAYLHHDClPTIIHGDVKAMNVLL-GPHFEPYLADFGLArtisgypntgiDLAKPTNRPPMAGSYGYMAPEHASmQRITE 946
Cdd:cd14032   117 LLFLHTRT-PPIIHRDLKCDNIFItGPTGSVKIGDLGLA-----------TLKRASFAKSVIGTPEFMAPEMYE-EHYDE 183
                         170       180
                  ....*....|....*....|
gi 240256081  947 KSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14032   184 SVDVYAFGMCMLEMATSEYP 203
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
802-1022 3.68e-06

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: 49.78  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKL-LFYDYLPNGSLssrLHGAGKGGCVDWEARYDVVLGVAHALAYLHHdclPTII 880
Cdd:cd14165    51 ELEILARLNHKSIIKTYEIFETSDGKVyIVMELGVQGDL---LEFIKLRGALPEDVARKMFHQLSSAIKYCHE---LDIV 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  881 HGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDLAKptnrpPMAGSYGYMAPEhaSMQRIT---EKSDVYSYGVVL 957
Cdd:cd14165   125 HRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRIVLSK-----TFCGSAAYAAPE--VLQGIPydpRIYDIWSLGVIL 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  958 LEVLTGKHPLDPDLpggahlvkwVRDHLAEKKDpSRLLDPR---LDGRTDSIMHEMLQTLAVAFLCVS 1022
Cdd:cd14165   198 YIMVCGSMPYDDSN---------VKKMLKIQKE-HRVRFPRsknLTSECKDLIYRLLQPDVSQRLCID 255
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
765-968 4.07e-06

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: 49.63  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVK-----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd14188     8 VLGKGGFAKCYEMTdLTTNKVYAAKiiphsRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGagKGGCVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNtgidl 918
Cdd:cd14188    88 MAHILKA--RKVLTEPEVRY-YLRQIVSGLKYLHEQ---EILHRDLKLGNFFINENMELKVGDFGLAARLEPLEH----- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  919 akptNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14188   157 ----RRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFE 202
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
766-966 4.25e-06

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: 49.19  E-value: 4.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVK----KMWSKEESGAfnsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd14006     1 LGRGRFGVVKRcIEKATGREFAAKfipkRDKKKEAVLR---EISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLhgAGKGGCVDWEARyDVVLGVAHALAYLHhDClpTIIHGDVKAMNVLLGPHFEPY--LADFGLARTIsgypNTGIDL 918
Cdd:cd14006    78 DRL--AERGSLSEEEVR-TYMRQLLEGLQYLH-NH--HILHLDLKPENILLADRPSPQikIIDFGLARKL----NPGEEL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  919 AKPTnrppmaGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14006   148 KEIF------GTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSP 189
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
802-968 4.33e-06

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: 49.55  E-value: 4.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSsRLHGAGKGgCVDWEARY---DVVLGVAhalaYLHHDclpT 878
Cdd:cd14187    57 EIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSLL-ELHKRRKA-LTEPEARYylrQIILGCQ----YLHRN---R 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHFEPYLADFGLARTIS--GYPntgidlakptnRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVV 956
Cdd:cd14187   128 VIHRDLKLGNLFLNDDMEVKIGDFGLATKVEydGER-----------KKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCI 196
                         170
                  ....*....|..
gi 240256081  957 LLEVLTGKHPLD 968
Cdd:cd14187   197 MYTLLVGKPPFE 208
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
770-967 4.72e-06

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 49.57  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  770 SSGVVYRIT-IPSGESLAVKKMWSKEEsgaFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGK 848
Cdd:cd14196    28 STGLEYAAKfIKKRQSRASRRGVSREE---IEREVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDFL--AQK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  849 GGCVDWEARyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLL------GPHFEpyLADFGLARTISgypnTGIDLAKpt 922
Cdd:cd14196   103 ESLSEEEAT-SFIKQILDGVNYLHTK---KIAHFDLKPENIMLldknipIPHIK--LIDFGLAHEIE----DGVEFKN-- 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 240256081  923 nrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14196   171 ----IFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPF 211
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
802-967 4.75e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 50.89  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNR-NLKL-LFYDYLPNGSLSSRLHGAGKG-GCVDWEARYDVVLGVAHALAYLHH----D 874
Cdd:PTZ00266   62 EVNVMRELKHKNIVRYIDRFLNKaNQKLyILMEFCDAGDLSRNIQKCYKMfGKIEEHAIVDITRQLLHALAYCHNlkdgP 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  875 CLPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGID---LAKPTNRPPMA----GSYGYMAPE---HASmQRI 944
Cdd:PTZ00266  142 NGERVLHRDLKPQNIFLSTGIRHIGKITAQANNLNGRPIAKIGdfgLSKNIGIESMAhscvGTPYYWSPElllHET-KSY 220
                         170       180
                  ....*....|....*....|...
gi 240256081  945 TEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:PTZ00266  221 DDKSDMWALGCIIYELCSGKTPF 243
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
766-969 4.92e-06

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: 49.80  E-value: 4.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKkmwskeesgAFNS------------EIKTLGSIRHRNIVRLLGW---CSNRNlKLL 829
Cdd:cd13988     1 LGQGATANVFRgRHKKTGDLYAVK---------VFNNlsfmrpldvqmrEFEVLKKLNHKNIVKLFAIeeeLTTRH-KVL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 FYDYLPNGSLSSRL-HGAGKGGCVDWE---ARYDVVLGVAHalayLHHDclpTIIHGDVKA---MNVLLGPHFEPY-LAD 901
Cdd:cd13988    71 VMELCPCGSLYTVLeEPSNAYGLPESEfliVLRDVVAGMNH----LREN---GIVHRDIKPgniMRVIGEDGQSVYkLTD 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  902 FGLARTISgypntgidlakptNRPPMAGSYG---YMAP---EHASMQRITEKS-----DVYSYGVVLLEVLTGKHPLDP 969
Cdd:cd13988   144 FGAARELE-------------DDEQFVSLYGteeYLHPdmyERAVLRKDHQKKygatvDLWSIGVTFYHAATGSLPFRP 209
LRR_8 pfam13855
Leucine rich repeat;
602-657 5.41e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.82  E-value: 5.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081   602 SLNLSCNRFVGEIPSRFSDLKNLGVLDVSHNQLTG-NLNVLTDLQNLVSLNISYNDF 657
Cdd:pfam13855    5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTlSPGAFSGLPSLRYLDLSGNRL 61
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
744-977 5.65e-06

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: 49.65  E-value: 5.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  744 TLY-QKLDFSIDDIVKNLTSANVIGTGSSG-VVYRITIPSGESLAVKKMwskeeSGAFNS---------EIKTLGSIRHR 812
Cdd:cd07877     2 TFYrQELNKTIWEVPERYQNLSPVGSGAYGsVCAAFDTKTGLRVAVKKL-----SRPFQSiihakrtyrELRLLKHMKHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  813 NIVRLLG-WCSNRNLKLlFYDYLpngsLSSRLHGAGKGGCVDWEARYD-----VVLGVAHALAYLHHdclPTIIHGDVKA 886
Cdd:cd07877    77 NVIGLLDvFTPARSLEE-FNDVY----LVTHLMGADLNNIVKCQKLTDdhvqfLIYQILRGLKYIHS---ADIIHRDLKP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  887 MNVLLGPHFEPYLADFGLAR----TISGYpntgidlakptnrppmAGSYGYMAPE-HASMQRITEKSDVYSYGVVLLEVL 961
Cdd:cd07877   149 SNLAVNEDCELKILDFGLARhtddEMTGY----------------VATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELL 212
                         250
                  ....*....|....*.
gi 240256081  962 TGKHPldpdLPGGAHL 977
Cdd:cd07877   213 TGRTL----FPGTDHI 224
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
802-967 5.66e-06

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: 49.25  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEARyDVVLGVAHALAYLHHdclPTIIH 881
Cdd:cd14194    58 EVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFL--AEKESLTEEEAT-EFLKQILNGVYYLHS---LQIAH 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  882 GDVKAMNVLL----GPHFEPYLADFGLARTIsgypNTGIDLAKptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVL 957
Cdd:cd14194   132 FDLKPENIMLldrnVPKPRIKIIDFGLAHKI----DFGNEFKN------IFGTPEFVAPEIVNYEPLGLEADMWSIGVIT 201
                         170
                  ....*....|
gi 240256081  958 LEVLTGKHPL 967
Cdd:cd14194   202 YILLSGASPF 211
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
766-957 6.19e-06

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: 49.48  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITI-PSGESLAVKKMW--SKEESGAFNSEIKTLGSI--RHRNIVRLLGWCSNRNLkllFYDYLPNGSLS 840
Cdd:cd13977     8 VGRGSYGVVYEAVVrRTGARVAVKKIRcnAPENVELALREFWALSSIqrQHPNVIQLEECVLQRDG---LAQRMSHGSSK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLH-----GAGKGG-CVDWEARY-----------------------------DVVLGVAHALAYLHHDclpTIIHGDVK 885
Cdd:cd13977    85 SDLYlllveTSLKGErCFDPRSACylwfvmefcdggdmneyllsrrpdrqtntSFMLQLSSALAFLHRN---QIVHRDLK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  886 AMNVLLGPHF-EPYL--ADFGLARTISGypnTGIDLAKPTN-----RPPMAGSYGYMAPEhASMQRITEKSDVYSYGVVL 957
Cdd:cd13977   162 PDNILISHKRgEPILkvADFGLSKVCSG---SGLNPEEPANvnkhfLSSACGSDFYMAPE-VWEGHYTAKADIFALGIII 237
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
802-976 6.24e-06

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: 49.28  E-value: 6.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRL---LGWCSNRNLKLLFyDYLPNGS---------LSSRLHgagkggcvdWEARYDVVLGvahaLA 869
Cdd:cd14118    64 EIAILKKLDHPNVVKLvevLDDPNEDNLYMVF-ELVDKGAvmevptdnpLSEETA---------RSYFRDIVLG----IE 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  870 YLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgiDLAKPTNrppMAGSYGYMAPEHASMQRIT---E 946
Cdd:cd14118   130 YLHYQ---KIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEG------DDALLSS---TAGTPAFMAPEALSESRKKfsgK 197
                         170       180       190
                  ....*....|....*....|....*....|
gi 240256081  947 KSDVYSYGVVLLEVLTGKHPLDPDLPGGAH 976
Cdd:cd14118   198 ALDIWAMGVTLYCFVFGRCPFEDDHILGLH 227
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
764-966 8.00e-06

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: 48.72  E-value: 8.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  764 NVIGTGSSGVVYR-ITIPSGESLAVKKM---WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd06619     7 EILGHGNGGTVYKaYHLLTRRILAVKVIpldITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 ----SSRLHGAGKggcvdwearydVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntg 915
Cdd:cd06619    87 dvyrKIPEHVLGR-----------IAVAVVKGLTYLWS---LKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVN----- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  916 iDLAKPtnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd06619   148 -SIAKT-----YVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFP 192
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
798-967 8.52e-06

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: 48.87  E-value: 8.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  798 AFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLF---------YDY-LPNGSLSSRlhgagkggcvdweARYDVVLGVAHA 867
Cdd:cd14088    45 AAKNEINILKMVKHPNILQLVDVFETRKEYFIFlelatgrevFDWiLDQGYYSER-------------DTSNVIRQVLEA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  868 LAYLHHDClptIIHGDVKAMNVLLG---PHFEPYLADFGLARTISGYpntgidLAKPTNRPPmagsygYMAPEHASMQRI 944
Cdd:cd14088   112 VAYLHSLK---IVHRNLKLENLVYYnrlKNSKIVISDFHLAKLENGL------IKEPCGTPE------YLAPEVVGRQRY 176
                         170       180
                  ....*....|....*....|...
gi 240256081  945 TEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14088   177 GRPVDCWAIGVIMYILLSGNPPF 199
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
765-969 9.18e-06

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: 48.90  E-value: 9.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKMwskeeSGAFNS---------EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYD-Y 833
Cdd:cd07855    12 TIGSGAYGVVCSaIDTKSGQKVAIKKI-----PNAFDVvttakrtlrELKILRHFKHDNIIAIRDILRPKVPYADFKDvY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSLSSRLHGA--GKGGCVDWEARYdVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTISgy 911
Cdd:cd07855    87 VVLDLMESDLHHIihSDQPLTLEHIRY-FLYQLLRGLKYIHSAN---VIHRDLKPSNLLVNENCELKIGDFGMARGLC-- 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256081  912 pntgidlAKPTNRPPMAGSY----GYMAPE-HASMQRITEKSDVYSYGVVLLEVLtGKHPLDP 969
Cdd:cd07855   161 -------TSPEEHKYFMTEYvatrWYRAPElMLSLPEYTQAIDMWSVGCIFAEML-GRRQLFP 215
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
758-962 9.63e-06

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: 48.49  E-value: 9.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  758 KNLTSANVIGTGSSGVVY--------------RITIPSgeslaVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSN 823
Cdd:cd05062     6 EKITMSRELGQGSFGMVYegiakgvvkdepetRVAIKT-----VNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  824 RNLKLLFYDYLPNGSLSSRL-------HGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFE 896
Cdd:cd05062    81 GQPTLVIMELMTRGDLKSYLrslrpemENNPVQAPPSLKKMIQMAGEIADGMAYLNAN---KFVHRDLAARNCMVAEDFT 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  897 PYLADFGLARTI--SGYPNTGIDLAKPTNrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLT 962
Cdd:cd05062   158 VKIGDFGMTRDIyeTDYYRKGGKGLLPVR---------WMSPESLKDGVFTTYSDVWSFGVVLWEIAT 216
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
335-515 1.00e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 47.86  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  335 NLQELQLSVNQISgTIpEELTNCTKLTHLEIDNNLITgEIPSLmSNLRSLTMFFAWQNKLT---GnipqsLSQCRELQAI 411
Cdd:cd21340    25 NLKVLYLYDNKIT-KI-ENLEFLTNLTHLYLQNNQIE-KIENL-ENLVNLKKLYLGGNRISvveG-----LENLTNLEEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  412 DLSYNSLSGSiPKEIFGLRNLTKllllsndlsgfippdIGNCtnLYRLRLNGNRLagSIPSEIGNLKNLNFVDISENRL- 490
Cdd:cd21340    96 HIENQRLPPG-EKLTFDPRSLAA---------------LSNS--LRVLNISGNNI--DSLEPLAPLRNLEQLDASNNQIs 155
                         170       180
                  ....*....|....*....|....*.
gi 240256081  491 -VGSIPPAISGCESLEFLDLHTNSLS 515
Cdd:cd21340   156 dLEELLDLLSSWPSLRELDLTGNPVC 181
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
766-966 1.11e-05

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: 48.10  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGS-SGVVYRITIPSGESLAVK-----KMWSKEESgAFNSEIKTLGSIRHRNIVRL------LGwcsnrnlKL-LFYD 832
Cdd:cd14075    10 LGSGNfSQVKLGIHQLTKEKVAIKildktKLDQKTQR-LLSREISSMEKLHHPNIIRLyevvetLS-------KLhLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  833 YLPNGSLSSRLHGAGKggCVDWEARY---DVVLGVAHAlaylhHDClpTIIHGDVKAMNVLLGPHFEPYLADFGLartiS 909
Cdd:cd14075    82 YASGGELYTKISTEGK--LSESEAKPlfaQIVSAVKHM-----HEN--NIIHRDLKAENVFYASNNCVKVGDFGF----S 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  910 GYPNTGIDLAKPTNRPPmagsygYMAPEHASMQR-ITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14075   149 THAKRGETLNTFCGSPP------YAAPELFKDEHyIGIYVDIWALGVLLYFMVTGVMP 200
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
759-970 1.13e-05

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: 48.46  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  759 NLTSANVIGTGSSGVVYRITIPSG-------------ESLAVKKMWSKEESgafNSEIKTLGSIRHRNIVRLLGWCSNRN 825
Cdd:cd05613     1 NFELLKVLGTGAYGKVFLVRKVSGhdagklyamkvlkKATIVQKAKTAEHT---RTERQVLEHIRQSPFLVTLHYAFQTD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  826 LKL-LFYDYLPNGSLSSRLHGAGKGGcvdwEARYDVVLG-VAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd05613    78 TKLhLILDYINGGELFTHLSQRERFT----ENEVQIYIGeIVLALEHLHK---LGIIYRDIKLENILLDSSGHVVLTDFG 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  904 LARTIsgypntgidLAKPTNRP-PMAGSYGYMAPE--HASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd05613   151 LSKEF---------LLDENERAySFCGTIEYMAPEivRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVD 211
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
766-970 1.35e-05

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: 48.10  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKK-----MWSKEESGAFNSEIKTLGSIRHRNIVRLL-GWCSNRNLKLLFyDYLPNGS 838
Cdd:cd08228    10 IGRGQFSEVYRATcLLDRKPVALKKvqifeMMDAKARQDCVKEIDLLKQLNHPNVIKYLdSFIEDNELNIVL-ELADAGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRL-HGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgid 917
Cdd:cd08228    89 LSQMIkYFKKQKRLIPERTVWKYFVQLCSAVEHMHSR---RVMHRDIKPANVFITATGVVKLGDLGLGRFFS-------- 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  918 lAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd08228   158 -SKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 209
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
766-967 1.47e-05

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: 47.96  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPS-GESLAVKKMWSKEESGAF--NSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd14114    10 LGTGAFGVVHRCTERAtGNNFAAKFIMTPHESDKEtvRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGELFER 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LhgAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPH--FEPYLADFGLARTISgyPNTGIDLAk 920
Cdd:cd14114    90 I--AAEHYKMSEAEVINYMRQVCEGLCHMHEN---NIVHLDIKPENIMCTTKrsNEVKLIDFGLATHLD--PKESVKVT- 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 240256081  921 ptnrppmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14114   162 -------TGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPF 201
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
765-967 1.82e-05

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: 47.99  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIPSG-------------ESLAVKKMWSKEESgafNSEIKTLGSIRHRNIVRLLGWCSNRNLKL-LF 830
Cdd:cd05614     7 VLGTGAYGKVFLVRKVSGhdanklyamkvlrKAALVQKAKTVEHT---RTERNVLEHVRQSPFLVTLHYAFQTDAKLhLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 YDYLPNGSLSSRLHGagKGGCVDWEARY---DVVLgvahALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLART 907
Cdd:cd05614    84 LDYVSGGELFTHLYQ--RDHFSEDEVRFysgEIIL----ALEHLHK---LGIVYRDIKLENILLDSEGHVVLTDFGLSKE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  908 IsgypntgidLAKPTNRP-PMAGSYGYMAPEHASMQRITEKS-DVYSYGVVLLEVLTGKHPL 967
Cdd:cd05614   155 F---------LTEEKERTySFCGTIEYMAPEIIRGKSGHGKAvDWWSLGILMFELLTGASPF 207
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
778-966 2.17e-05

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 47.53  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  778 TIPSGESLAVKKMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL---SSRlhgagkggcvDW 854
Cdd:cd14112    26 TTETDAHCAVKIFEVSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQEDVFtrfSSN----------DY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  855 EARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMNVLLGP--HFEPYLADFGLARTISgypntgidlakPTNRPPMAGSYG 932
Cdd:cd14112    96 YSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSvrSWQVKLVDFGRAQKVS-----------KLGKVPVDGDTD 164
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 240256081  933 YMAPE-HASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14112   165 WASPEfHNPETPITVQSDIWGLGVLTFCLLSGFHP 199
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
755-969 2.31e-05

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: 47.68  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  755 DIVKNLTSANVIGTGSSGVVYR-ITIPSGESLAVKKMwSKEESGAFN----SEIKTLGSIRHRNIVRLLGWCSNRNLKLL 829
Cdd:cd07849     2 DVGPRYQNLSYIGEGAYGMVCSaVHKPTGQKVAIKKI-SPFEHQTYClrtlREIKILLRFKHENIIGILDIQRPPTFESF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  830 FYDYLPNGSLSSRLHGAGKGGCV-DWEARYdVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLAR-T 907
Cdd:cd07849    81 KDVYIVQELMETDLYKLIKTQHLsNDHIQY-FLYQILRGLKYIHS---ANVLHRDLKPSNLLLNTNCDLKICDFGLARiA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  908 ISGYPNTGidlakptnrppMAGSY----GYMAPE-HASMQRITEKSDVYSYGVVLLEVLTGKhPLDP 969
Cdd:cd07849   157 DPEHDHTG-----------FLTEYvatrWYRAPEiMLNSKGYTKAIDIWSVGCILAEMLSNR-PLFP 211
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
765-969 2.91e-05

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: 47.30  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRIT-IPSGESLAVKKMWSKEESGAFNS----EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDY------ 833
Cdd:cd07848     8 VVGEGAYGVVLKCRhKETKEIVAIKKFKDSEENEEVKEttlrELKMLRTLKQENIVELKEAFRRRGKLYLVFEYveknml 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 -----LPNGSLSSRLHgagkggcvdwearyDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI 908
Cdd:cd07848    88 elleeMPNGVPPEKVR--------------SYIYQLIKAIHWCHKN---DIVHRDIKPENLLISHNDVLKLCDFGFARNL 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081  909 SgypnTGIDlakpTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKhPLDP 969
Cdd:cd07848   151 S----EGSN----ANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQ-PLFP 202
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
860-967 2.93e-05

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: 46.89  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  860 VVLGVAHAlaylhHDclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgidlakptnrpPMA------GSYGY 933
Cdd:cd08219   109 MCLGVQHI-----HE--KRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTS---------------PGAyactyvGTPYY 166
                          90       100       110
                  ....*....|....*....|....*....|....
gi 240256081  934 MAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd08219   167 VPPEIWENMPYNNKSDIWSLGCILYELCTLKHPF 200
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
762-966 3.26e-05

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: 46.74  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  762 SANVIGTGSSGVVYRIT-IPSGESLAVKKMWSKEesgAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd14109     8 GEEDEKRAAQGAPFHVTeRSTGRNFLAQLRYGDP---FLMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHG-AGKGGCVDWEAR---YDVVLGVAHAlaylhHDclPTIIHGDVKAMNVLLG-PHFEpyLADFGLARTISGYPNTG 915
Cdd:cd14109    85 VRDNLlPGKDYYTERQVAvfvRQLLLALKHM-----HD--LGIAHLDLRPEDILLQdDKLK--LADFGQSRRLLRGKLTT 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240256081  916 IDLAKPTnrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14109   156 LIYGSPE----------FVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISP 196
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
765-967 3.31e-05

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: 46.86  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVyRITIP--SGESLAVK-----KMWSKEEsgAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd14185     7 TIGDGNFAVV-KECRHwnENQEYAMKiidksKLKGKED--MIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGKGGCVDWEArydVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPY----LADFGLARTISGYPN 913
Cdd:cd14185    84 DLFDAIIESVKFTEHDAAL---MIIDLCEALVYIHSK---HIVHRDLKPENLLVQHNPDKSttlkLADFGLAKYVTGPIF 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  914 TgidlakptnrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14185   158 T------------VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPF 199
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
765-967 3.70e-05

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: 46.89  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITI-PSGESLAVKKMWSKE------ESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNG 837
Cdd:cd05632     9 VLGKGGFGEVCACQVrATGKMYACKRLEKKRikkrkgESMALN-EKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  838 SLSSRLHGAGKGGCVDWEARY---DVVLGVAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgyPNT 914
Cdd:cd05632    88 DLKFHIYNMGNPGFEEERALFyaaEILCGLED----LHRE---NTVYRDLKPENILLDDYGHIRISDLGLAVKI---PEG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  915 GIDLAKptnrppmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05632   158 ESIRGR-------VGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPF 203
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
745-967 4.01e-05

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: 46.96  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  745 LYQKLDFSIDDivknltsaNVIGTGSSGVVYRIT-IPSGESLAVKKMWSKEESGAfNSEIKTLGSIR-HRNIVRLLGWCS 822
Cdd:cd14179     2 FYQHYELDLKD--------KPLGEGSFSICRKCLhKKTNQEYAVKIVSKRMEANT-QREIAALKLCEgHPNIVKLHEVYH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  823 NRNLKLLFYDYLPNGSLSSRLHGagKGGCVDWEARYdVVLGVAHALAYLHHdclPTIIHGDVKAMNVLL---GPHFEPYL 899
Cdd:cd14179    73 DQLHTFLVMELLKGGELLERIKK--KQHFSETEASH-IMRKLVSAVSHMHD---VGVVHRDLKPENLLFtdeSDNSEIKI 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  900 ADFGLARtisgypntgidLAKPTNRPPMAGSYG--YMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14179   147 IDFGFAR-----------LKPPDNQPLKTPCFTlhYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPF 205
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
766-968 5.69e-05

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: 46.10  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVK-----KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd14161    11 LGKGTYGRVKKARDSSGRLVAIKsirkdRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLhgAGKGGCVDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTGIDLAK 920
Cdd:cd14161    91 DYI--SERQRLSELEARH-FFRQIVSAVHYCHAN---GIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQTYCGS 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 240256081  921 PT-NRPPMAGSYGYMAPEhasmqritekSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd14161   165 PLyASPEIVNGRPYIGPE----------VDSWSLGVLLYILVHGTMPFD 203
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
739-967 6.49e-05

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: 46.16  E-value: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  739 DSWEVTlyqkldfsiddivknltsaNVIGTGSSGVVYRI-TIPSGESLAVKKMWS----KEESGAFNSEIKTLGSirHRN 813
Cdd:cd06638    18 DTWEII-------------------ETIGKGTYGKVFKVlNKKNGSKAAVKILDPihdiDEEIEAEYNILKALSD--HPN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  814 IVRLLGWCSNRNLK-----LLFYDYLPNGSLSSRLHGAGKGGcvDWEARYDVVLGVAHALAYLHHDCLPTIIHGDVKAMN 888
Cdd:cd06638    77 VVKFYGMYYKKDVKngdqlWLVLELCNGGSVTDLVKGFLKRG--ERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  889 VLLGPHFEPYLADFGLARTIsgypnTGIDLAKPTNrppmAGSYGYMAPEH-ASMQRI----TEKSDVYSYGVVLLEVLTG 963
Cdd:cd06638   155 ILLTTEGGVKLVDFGVSAQL-----TSTRLRRNTS----VGTPFWMAPEViACEQQLdstyDARCDVWSLGITAIELGDG 225

                  ....
gi 240256081  964 KHPL 967
Cdd:cd06638   226 DPPL 229
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
857-970 6.62e-05

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: 45.97  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  857 RY---DVV---LGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgyPNTGIDLAKPTnrppmaGS 930
Cdd:cd14111    95 RYsedDVVgylVQILQGLEYLHGR---RVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFN--PLSLRQLGRRT------GT 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 240256081  931 YGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL-DPD 970
Cdd:cd14111   164 LEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFeDQD 204
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
868-967 7.42e-05

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: 45.68  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  868 LAYLHHDclpTIIHGDVKAMNVLLG---PHFEPYLADFGLARTIsgypntgidlAKPTNRPPMAGSYGYMAPEHASMQRI 944
Cdd:cd14198   123 VYYLHQN---NIVHLDLKPQNILLSsiyPLGDIKIVDFGMSRKI----------GHACELREIMGTPEYLAPEILNYDPI 189
                          90       100
                  ....*....|....*....|...
gi 240256081  945 TEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14198   190 TTATDMWNIGVIAYMLLTHESPF 212
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
866-972 8.02e-05

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: 45.73  E-value: 8.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  866 HALAYLHHDclpTIIHGDVKAMNVLLGPHFEP---YLADFGLArtiSGY-PNTGIDLAKPTNRPPMAGSygymaPEHASM 941
Cdd:cd14015   138 DVLEYIHEN---GYVHADIKASNLLLGFGKNKdqvYLVDYGLA---SRYcPNGKHKEYKEDPRKAHNGT-----IEFTSR 206
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 240256081  942 Q-----RITEKSDVYSYGVVLLEVLTGKHPLDPDLP 972
Cdd:cd14015   207 DahkgvAPSRRGDLEILGYNMLQWLCGKLPWEDNLK 242
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
765-972 8.15e-05

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: 45.49  E-value: 8.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVY---RI---------TIPsgeslaVKKMwSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYD 832
Cdd:cd08220     7 VVGRGAYGTVYlcrRKddnklviikQIP------VEQM-TKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  833 YLPNGSLSSRLHGAgKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPY-LADFGLARTISgy 911
Cdd:cd08220    80 YAPGGTLFEYIQQR-KGSLLSEEEILHFFVQILLALHHVHSK---QILHRDLKTQNILLNKKRTVVkIGDFGISKILS-- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081  912 pntgidlaKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLD-PDLP 972
Cdd:cd08220   154 --------SKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEaANLP 207
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
765-966 8.45e-05

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: 45.81  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYR-ITIPSGESLAVKKM-----WSKEESG-----AFNSEIKTLGSI-RHRNIVRLLGWCSNRNLKLLFYD 832
Cdd:cd14093    10 ILGRGVSSTVRRcIEKETGQEFAVKIIditgeKSSENEAeelreATRREIEILRQVsGHPNIIELHDVFESPTFIFLVFE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  833 YLPNGSLSSRLhgAGKGGCVDWEARYdVVLGVAHALAYLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgyp 912
Cdd:cd14093    90 LCRKGELFDYL--TEVVTLSEKKTRR-IMRQLFEAVEFLHSLN---IVHRDLKPENILLDDNLNVKISDFGFATRL---- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  913 NTGIDLAKptnrppMAGSYGYMAPE--HASMQR----ITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14093   160 DEGEKLRE------LCGTPGYLAPEvlKCSMYDnapgYGKEVDMWACGVIMYTLLAGCPP 213
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
867-966 8.86e-05

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: 45.84  E-value: 8.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  867 ALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLART-ISGYpntgidlAKPTNrppMAGSYGYMAPEHASMQRIT 945
Cdd:cd05592   108 GLQFLHSR---GIIYRDLKLDNVLLDREGHIKIADFGMCKEnIYGE-------NKAST---FCGTPDYIAPEILKGQKYN 174
                          90       100
                  ....*....|....*....|.
gi 240256081  946 EKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd05592   175 QSVDWWSFGVLLYEMLIGQSP 195
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
792-967 9.23e-05

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: 45.38  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  792 SKEEsgaFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEARyDVVLGVAHALAYL 871
Cdd:cd14195    51 SREE---IEREVNILREIQHPNIITLHDIFENKTDVVLILELVSGGELFDFL--AEKESLTEEEAT-QFLKQILDGVHYL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  872 HHDclpTIIHGDVKAMNVLL----GPHFEPYLADFGLARTISGypntGIDLAKptnrppMAGSYGYMAPEHASMQRITEK 947
Cdd:cd14195   125 HSK---RIAHFDLKPENIMLldknVPNPRIKLIDFGIAHKIEA----GNEFKN------IFGTPEFVAPEIVNYEPLGLE 191
                         170       180
                  ....*....|....*....|
gi 240256081  948 SDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14195   192 ADMWSIGVITYILLSGASPF 211
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
765-967 9.31e-05

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: 45.73  E-value: 9.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIPS-GESLAVKKMWSK------EESGAFNSEIKTLGSIRHRNIVRLlGWCSNRNLKLLF-YDYLPN 836
Cdd:cd05603     2 VIGKGSFGKVLLAKRKCdGKFYAVKVLQKKtilkkkEQNHIMAERNVLLKNLKHPFLVGL-HYSFQTSEKLYFvLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHgagKGGC-VDWEARYdVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARtisgypnTG 915
Cdd:cd05603    81 GELFFHLQ---RERCfLEPRARF-YAAEVASAIGYLHSL---NIIYRDLKPENILLDCQGHVVLTDFGLCK-------EG 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  916 IDLAKPTNrpPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05603   147 MEPEETTS--TFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
802-972 9.49e-05

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: 45.37  E-value: 9.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS--LSSRLHGagkGGCVDWEARyDVVLGVAHALAYLHhDClpTI 879
Cdd:cd14163    50 ELQIVERLDHKNIIHVYEMLESADGKIYLVMELAEDGdvFDCVLHG---GPLPEHRAK-ALFRQLVEAIRYCH-GC--GV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  880 IHGDVKAMNVLLgPHFEPYLADFGLARTIsgyPNTGIDLAKPtnrppMAGSYGYMAPEhaSMQRI---TEKSDVYSYGVV 956
Cdd:cd14163   123 AHRDLKCENALL-QGFTLKLTDFGFAKQL---PKGGRELSQT-----FCGSTAYAAPE--VLQGVphdSRKGDIWSMGVV 191
                         170
                  ....*....|....*..
gi 240256081  957 LLEVLTGKHPL-DPDLP 972
Cdd:cd14163   192 LYVMLCAQLPFdDTDIP 208
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
766-969 1.03e-04

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: 45.34  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRI-TIPSGESLAVKKM----WSKEESGAFNsEIKTLGSIR-HRNIVRLLGWCSNR---NLKLLF------ 830
Cdd:cd07831     7 IGEGTFSEVLKAqSRKTGKYYAIKCMkkhfKSLEQVNNLR-EIQALRRLSpHPNILRLIEVLFDRktgRLALVFelmdmn 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  831 -YDYLPNgslssRLHgagkggCVDwEAR-----YDVVLGVAHalayLHHDclpTIIHGDVKAMNVLLgpHFEPY-LADFG 903
Cdd:cd07831    86 lYELIKG-----RKR------PLP-EKRvknymYQLLKSLDH----MHRN---GIFHRDIKPENILI--KDDILkLADFG 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  904 LARTISGYPNTGIDLAKPTNRPP----MAGSYGYmapehasmqriteKSDVYSYGVVLLEVLTgKHPLDP 969
Cdd:cd07831   145 SCRGIYSKPPYTEYISTRWYRAPecllTDGYYGP-------------KMDIWAVGCVFFEILS-LFPLFP 200
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
332-596 1.09e-04

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 45.42  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  332 KLENLQELQLSVNQISGT----IPEELTNCTKLTHLEI-DNNliTGEIP----SLMSNLRS---LTMFFAWQNKLTGNIP 399
Cdd:cd00116    21 KLLCLQVLRLEGNTLGEEaakaLASALRPQPSLKELCLsLNE--TGRIPrglqSLLQGLTKgcgLQELDLSDNALGPDGC 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  400 ---QSLSQCRELQAIDLSYNSLSGSIPKEIFGLRNLTKLLLLSNDLSgfippdignctnlyRLRLNGN---RLAGSIPSe 473
Cdd:cd00116    99 gvlESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLG--------------RNRLEGAsceALAKALRA- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  474 IGNLKNLNFV--DISEnRLVGSIPPAISGCESLEFLDLHTNSLS---GSLLGTTLP--KSLKFIDFSDNALSS----TLP 542
Cdd:cd00116   164 NRDLKELNLAnnGIGD-AGIRALAEGLKANCNLEVLDLNNNGLTdegASALAETLAslKSLEVLNLGDNNLTDagaaALA 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  543 PG-IGLLTELTKLNLAKNRLSGE----IPREISTCRSLQLLNLGENDFSGEIPDELGQI 596
Cdd:cd00116   243 SAlLSPNISLLTLSLSCNDITDDgakdLAEVLAEKESLLELDLRGNKFGEEGAQLLAES 301
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
766-969 1.21e-04

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: 45.37  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESL-AVKKMWSKEESGAFNS---EIKTLGSIRHRNIVRLLGWC-SNRNLKLLFyDYLpNGSLS 840
Cdd:cd07872    14 LGEGTYATVFKGRSKLTENLvALKEIRLEHEEGAPCTairEVSLLKDLKHANIVTLHDIVhTDKSLTLVF-EYL-DKDLK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  841 SRLHGagkggCVDWEARYDVVL---GVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS----GYPN 913
Cdd:cd07872    92 QYMDD-----CGNIMSMHNVKIflyQILRGLAYCHRR---KVLHRDLKPQNLLINERGELKLADFGLARAKSvptkTYSN 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  914 TGIDLAKptnRPP--MAGSYGYmapehasmqriTEKSDVYSYGVVLLEVLTGKhPLDP 969
Cdd:cd07872   164 EVVTLWY---RPPdvLLGSSEY-----------STQIDMWGVGCIFFEMASGR-PLFP 206
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
864-968 1.22e-04

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: 45.46  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgypntGIDLAKPTNRppMAGSYGYMAPEHASMQR 943
Cdd:cd05587   106 IAVGLFFLHSK---GIIYRDLKLDNVMLDAEGHIKIADFGMCKE-------GIFGGKTTRT--FCGTPDYIAPEIIAYQP 173
                          90       100
                  ....*....|....*....|....*
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd05587   174 YGKSVDWWAYGVLLYEMLAGQPPFD 198
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
809-960 1.25e-04

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: 45.12  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  809 IRHRNIVRLLGWCS----NRNLKLLFYDYLPNGSLSSRLHGAGKG-GCVDWEARYDVVLGVAHALAYLHhDCLPTIIHGD 883
Cdd:cd14034    67 LEHLNIVKFHKYWAdvkeNRARVIFITEYMSSGSLKQFLKKTKKNhKTMNEKAWKRWCTQILSALSYLH-SCDPPIIHGN 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  884 VKAMNVllgphfepYLADFGLARTISGYPNTgIDLAKPTNRPPMAGSYgYMAPEHASMQRITEKSDVYSYGVVLLEV 960
Cdd:cd14034   146 LTCDTI--------FIQHNGLIKIGSVAPDT-INNHVKTCREEQKNLH-FFAPEYGEVANVTTAVDIYSFGMCALEM 212
LRR_8 pfam13855
Leucine rich repeat;
310-370 1.37e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 1.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081   310 PELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTIPEELTNCTKLTHLEIDNNLI 370
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
755-970 1.43e-04

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: 45.38  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  755 DIVKnltsanVIGTGSSGVVYRITIPSGESLAVKKMWSKEE------SGAFNSEIKTLGSIRHRNIVRLlgWCSNRNLKL 828
Cdd:cd05621    55 DVVK------VIGRGAFGEVQLVRHKASQKVYAMKLLSKFEmikrsdSAFFWEERDIMAFANSPWVVQL--FCAFQDDKY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFY--DYLPNGSLssrlhgagkggcVDWEARYDV--------VLGVAHALAYLHHDCLptiIHGDVKAMNVLLGPHFEPY 898
Cdd:cd05621   127 LYMvmEYMPGGDL------------VNLMSNYDVpekwakfyTAEVVLALDAIHSMGL---IHRDVKPDNMLLDKYGHLK 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  899 LADFGLARTISGYPNTGIDLAkptnrppmAGSYGYMAPEHASMQ----RITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd05621   192 LADFGTCMKMDETGMVHCDTA--------VGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLFEMLVGDTPFYAD 259
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
855-999 1.56e-04

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 44.96  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  855 EARY---DVVLGVAhalaYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISGYPntgidlAKPTNrppMAGSY 931
Cdd:cd14199   127 QARFyfqDLIKGIE----YLHYQ---KIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSD------ALLTN---TVGTP 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  932 GYMAPEHASMQR--ITEKS-DVYSYGVVLLEVLTGKHP-LD-----------------PDLPGGAHLVKWVRDHLAEKKD 990
Cdd:cd14199   191 AFMAPETLSETRkiFSGKAlDVWAMGVTLYCFVFGQCPfMDerilslhskiktqplefPDQPDISDDLKDLLFRMLDKNP 270

                  ....*....
gi 240256081  991 PSRLLDPRL 999
Cdd:cd14199   271 ESRISVPEI 279
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
747-964 1.70e-04

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: 45.04  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  747 QKLDFSIDDIVKNLTSANVIGTGSSG-VVYRITIPSGESLAVKKMwskeeSGAFNSEIKTLGSIRHrniVRLLGWCSNRN 825
Cdd:cd07878     4 QELNKTVWEVPERYQNLTPVGSGAYGsVCSAYDTRLRQKVAVKKL-----SRPFQSLIHARRTYRE---LRLLKHMKHEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  826 LKLLFYDYLPNGS--------LSSRLHGAGKGGCVDWEARYD-----VVLGVAHALAYLHHdclPTIIHGDVKAMNVLLG 892
Cdd:cd07878    76 VIGLLDVFTPATSienfnevyLVTNLMGADLNNIVKCQKLSDehvqfLIYQLLRGLKYIHS---AGIIHRDLKPSNVAVN 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240256081  893 PHFEPYLADFGLART----ISGYpntgidlakptnrppmAGSYGYMAPE-HASMQRITEKSDVYSYGVVLLEVLTGK 964
Cdd:cd07878   153 EDCELRILDFGLARQaddeMTGY----------------VATRWYRAPEiMLNWMHYNQTVDIWSVGCIMAELLKGK 213
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
806-969 1.83e-04

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 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. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 44.51  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  806 LGSIRHRNIVRLLGWCSNRNLkLLFYDYLPNGSLSSRLHGAGKGGCVDWEARYDVVLGVAHALAYLHHDCLPtiiHGDVK 885
Cdd:cd14208    56 MSQISHKHLVLLHGVCVGKDS-IMVQEFVCHGALDLYLKKQQQKGPVAISWKLQVVKQLAYALNYLEDKQLV---HGNVS 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  886 AMNVLL---GPHFEP---YLADFGLARTIsgypntgIDLAKPTNRPPmagsygYMAPEHAS-MQRITEKSDVYSYGVVLL 958
Cdd:cd14208   132 AKKVLLsreGDKGSPpfiKLSDPGVSIKV-------LDEELLAERIP------WVAPECLSdPQNLALEADKWGFGATLW 198
                         170
                  ....*....|....*
gi 240256081  959 EVLTGKH----PLDP 969
Cdd:cd14208   199 EIFSGGHmplsALDP 213
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
827-970 2.07e-04

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: 44.31  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  827 KL-LFYDYLPNGSLSSRLHGAGKGGcvdwEARYDVVLG-VAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGL 904
Cdd:cd05583    73 KLhLILDYVNGGELFTHLYQREHFT----ESEVRIYIGeIVLALEHLHK---LGIIYRDIKLENILLDSEGHVVLTDFGL 145
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  905 ARTIsgypntgidLAKPTNRP-PMAGSYGYMAPE--HASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd05583   146 SKEF---------LPGENDRAySFCGTIEYMAPEvvRGGSDGHDKAVDWWSLGVLTYELLTGASPFTVD 205
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
765-967 2.28e-04

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: 44.62  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIPSGESL-AVKKMWSK------EESGAFNSEIKTLGSIRHRNIVRLlGWCSNRNLKLLF-YDYLPN 836
Cdd:cd05602    14 VIGKGSFGKVLLARHKSDEKFyAVKVLQKKailkkkEEKHIMSERNVLLKNVKHPFLVGL-HFSFQTTDKLYFvLDYING 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  837 GSLSSRLHgagKGGC-VDWEARYdVVLGVAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgypntg 915
Cdd:cd05602    93 GELFYHLQ---RERCfLEPRARF-YAAEIASALGYLHS---LNIVYRDLKPENILLDSQGHIVLTDFGLCKE-------- 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  916 iDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05602   158 -NIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPF 208
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
864-967 2.30e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 44.99  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLArtisGYPntgIDLAKptNR-PPMAGSYGYMAPEHASMQ 942
Cdd:PHA03212  191 VLRAIQYLHEN---RIIHRDIKAENIFINHPGDVCLGDFGAA----CFP---VDINA--NKyYGWAGTIATNAPELLARD 258
                          90       100
                  ....*....|....*....|....*
gi 240256081  943 RITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:PHA03212  259 PYGPAVDIWSAGIVLFEMATCHDSL 283
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
864-967 2.33e-04

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: 44.57  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARtisgypnTGIDLAKPTNrpPMAGSYGYMAPEHASMQR 943
Cdd:cd05604   106 IASALGYLHS---INIVYRDLKPENILLDSQGHIVLTDFGLCK-------EGISNSDTTT--TFCGTPEYLAPEVIRKQP 173
                          90       100
                  ....*....|....*....|....
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05604   174 YDNTVDWWCLGSVLYEMLYGLPPF 197
LRR_8 pfam13855
Leucine rich repeat;
454-514 2.52e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.20  E-value: 2.52e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081   454 TNLYRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSL 514
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
880-962 2.84e-04

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: 44.63  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  880 IHGDVKAMNVLLGPHFEPYLADFGLARTISGYPNTgidLAKPTNRPPMAgsygYMAPEHASMQRITEKSDVYSYGVVLLE 959
Cdd:cd05105   259 VHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNY---VSKGSTFLPVK----WMAPESIFDNLYTTLSDVWSYGILLWE 331

                  ...
gi 240256081  960 VLT 962
Cdd:cd05105   332 IFS 334
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
864-968 2.86e-04

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: 44.22  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgypntgiDLAKPTNRPPMAGSYGYMAPEHASMQR 943
Cdd:cd05615   120 ISVGLFFLHKK---GIIYRDLKLDNVMLDSEGHIKIADFGMCKE---------HMVEGVTTRTFCGTPDYIAPEIIAYQP 187
                          90       100
                  ....*....|....*....|....*
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd05615   188 YGRSVDWWAYGVLLYEMLAGQPPFD 212
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
766-903 3.10e-04

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: 42.04  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWS--KEESGAFNSEIKTLGSIR--HRNIVRLLGWCSNRNLKLLFYDYLPNGSLS 840
Cdd:cd13968     1 MGEGASAKVFWaEGECTTIGVAVKIGDDvnNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240256081  841 SRLhgagKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd13968    81 AYT----QEEELDEKDVESIMYQLAECMRLLHSF---HLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
864-967 3.60e-04

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: 43.77  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHDclpTIIHGDVKAMNVLL---GPHFEPYLADFGLARTISGYPNTgidlakptnRPPMaGSYGYMAPEHAS 940
Cdd:cd14197   120 ILEGVSFLHNN---NVVHLDLKPQNILLtseSPLGDIKIVDFGLSRILKNSEEL---------REIM-GTPEYVAPEILS 186
                          90       100
                  ....*....|....*....|....*..
gi 240256081  941 MQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14197   187 YEPISTATDMWSIGVLAYVMLTGISPF 213
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
859-966 3.71e-04

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: 43.58  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  859 DVVLGVAHalayLHHDClptIIHGDVKAMNVLLGPHFEPYLADFGLArtisgypntgIDLAKptnRPPMA--GSYGYMAP 936
Cdd:cd05606   106 EVILGLEH----MHNRF---IVYRDLKPANILLDEHGHVRISDLGLA----------CDFSK---KKPHAsvGTHGYMAP 165
                          90       100       110
                  ....*....|....*....|....*....|.
gi 240256081  937 EHASMQRITEKS-DVYSYGVVLLEVLTGKHP 966
Cdd:cd05606   166 EVLQKGVAYDSSaDWFSLGCMLYKLLKGHSP 196
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
827-967 4.22e-04

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: 43.90  E-value: 4.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  827 KLLFYDYLPNGSlSSRLHGAGKGGCVDWEARY---DVVLGVAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFG 903
Cdd:cd05633    82 KLCFILDLMNGG-DLHYHLSQHGVFSEKEMRFyatEIILGLEH----MHNR---FVVYRDLKPANILLDEHGHVRISDLG 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  904 LArtisgypntgIDLAKptnRPPMA--GSYGYMAPEhaSMQRIT---EKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05633   154 LA----------CDFSK---KKPHAsvGTHGYMAPE--VLQKGTaydSSADWFSLGCMLFKLLRGHSPF 207
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
765-995 4.94e-04

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: 43.39  E-value: 4.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIP-SGESLAVKKMwsKEESGAFNSEIK-TLGSIRhrniVRLLGW---------CSNRNLKLLFY-- 831
Cdd:cd05620     2 VLGKGSFGKVLLAELKgKGEYFAVKAL--KKDVVLIDDDVEcTMVEKR----VLALAWenpflthlyCTFQTKEHLFFvm 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  832 DYLPNGSLssRLHGAGKGgcvdweaRYDVVLGVAHA------LAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLA 905
Cdd:cd05620    76 EFLNGGDL--MFHIQDKG-------RFDLYRATFYAaeivcgLQFLHSK---GIIYRDLKLDNVMLDRDGHIKIADFGMC 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  906 RTisgypntgiDLAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP------------LDPDLPg 973
Cdd:cd05620   144 KE---------NVFGDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPfhgddedelfesIRVDTP- 213
                         250       260
                  ....*....|....*....|....*...
gi 240256081  974 gaHLVKWV----RDHLAE--KKDPSRLL 995
Cdd:cd05620   214 --HYPRWItkesKDILEKlfERDPTRRL 239
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
766-970 5.40e-04

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: 43.48  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRIT-IPSGESLAVKK------MWSKEESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd08229    32 IGRGQFSEVYRATcLLDGVPVALKKvqifdlMDAKARADCIK-EIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRL-HGAGKGGCVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTISgypntgid 917
Cdd:cd08229   111 LSRMIkHFKKQKRLIPEKTVWKYFVQLCSALEHMHSR---RVMHRDIKPANVFITATGVVKLGDLGLGRFFS-------- 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240256081  918 lAKPTNRPPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd08229   180 -SKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 231
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
788-971 7.39e-04

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: 42.96  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  788 KKMWSKEESgAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEARYdVVLGVAHA 867
Cdd:cd14169    38 KKALRGKEA-MVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGELFDRI--IERGSYTEKDASQ-LIGQVLQA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  868 LAYLHHdclPTIIHGDVKAMNVLLGPHFEP---YLADFGLAR-TISGYPNTGidlakptnrppmAGSYGYMAPEHASMQR 943
Cdd:cd14169   114 VKYLHQ---LGIVHRDLKPENLLYATPFEDskiMISDFGLSKiEAQGMLSTA------------CGTPGYVAPELLEQKP 178
                         170       180       190
                  ....*....|....*....|....*....|..
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHPL----DPDL 971
Cdd:cd14169   179 YGKAVDVWAIGVISYILLCGYPPFydenDSEL 210
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
802-966 7.86e-04

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: 42.47  E-value: 7.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  802 EIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLhgAGKGGCVDWEArYDVVLGVAHALAYLHhDClpTIIH 881
Cdd:cd14105    58 EVSILRQVLHPNIITLHDVFENKTDVVLILELVAGGELFDFL--AEKESLSEEEA-TEFLKQILDGVNYLH-TK--NIAH 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  882 GDVKAMNVLLG----PHFEPYLADFGLARTISgypntgiDLAKPTNrppMAGSYGYMAPEHASMQRITEKSDVYSYGVVL 957
Cdd:cd14105   132 FDLKPENIMLLdknvPIPRIKLIDFGLAHKIE-------DGNEFKN---IFGTPEFVAPEIVNYEPLGLEADMWSIGVIT 201

                  ....*....
gi 240256081  958 LEVLTGKHP 966
Cdd:cd14105   202 YILLSGASP 210
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
864-968 8.76e-04

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: 42.68  E-value: 8.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTisgypntgiDLAKPTNRPPMAGSYGYMAPEHASMQR 943
Cdd:cd05616   110 IAIGLFFLQSK---GIIYRDLKLDNVMLDSEGHIKIADFGMCKE---------NIWDGVTTKTFCGTPDYIAPEIIAYQP 177
                          90       100
                  ....*....|....*....|....*
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHPLD 968
Cdd:cd05616   178 YGKSVDWWAFGVLLYEMLAGQAPFE 202
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
791-1000 9.21e-04

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK 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: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 42.09  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  791 WSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGaGKGGCVDWEARYDVVLGVAHALAY 870
Cdd:cd14057    31 VTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVLHE-GTGVVVDQSQAVKFALDIARGMAF 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  871 LhHDCLPTIIHGDVKAMNVLLGphfEPYLADFGLARTISGYPNTGiDLAKPtnrppmagsyGYMAPEhaSMQRITEK--- 947
Cdd:cd14057   110 L-HTLEPLIPRHHLNSKHVMID---EDMTARINMADVKFSFQEPG-KMYNP----------AWMAPE--ALQKKPEDinr 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240256081  948 --SDVYSYGVVLLEVLTGKHP-----------------LDPDLPGGA--HLVKWVRDHLAEkkDPSRllDPRLD 1000
Cdd:cd14057   173 rsADMWSFAILLWELVTREVPfadlsnmeigmkialegLRVTIPPGIspHMCKLMKICMNE--DPGK--RPKFD 242
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
801-966 9.29e-04

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: 42.78  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  801 SEIKTLGSIRHRNIVRLLgWCSNRNLKL-LFYDYLPNGSLSSRLHGAGkggcVDWEARYDVVLG-VAHALAYLHHDclpT 878
Cdd:cd05584    49 AERNILEAVKHPFIVDLH-YAFQTGGKLyLILEYLSGGELFMHLEREG----IFMEDTACFYLAeITLALGHLHSL---G 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHFEPYLADFGLARtisgypnTGIDLAKPTNrpPMAGSYGYMAPEHASMQRITEKSDVYSYGVVLL 958
Cdd:cd05584   121 IIYRDLKPENILLDAQGHVKLTDFGLCK-------ESIHDGTVTH--TFCGTIEYMAPEILTRSGHGKAVDWWSLGALMY 191

                  ....*...
gi 240256081  959 EVLTGKHP 966
Cdd:cd05584   192 DMLTGAPP 199
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
860-967 1.08e-03

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: 42.18  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  860 VVLGVAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLArtisgypntgIDLAKPTNRPP-MAGSYGYMAPEH 938
Cdd:cd05608   114 IISGLEH----LHQR---RIIYRDLKPENVLLDDDGNVRISDLGLA----------VELKDGQTKTKgYAGTPGFMAPEL 176
                          90       100
                  ....*....|....*....|....*....
gi 240256081  939 ASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05608   177 LLGEEYDYSVDYFTLGVTLYEMIAARGPF 205
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
765-966 1.11e-03

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 42.34  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVY----RITipsGESLAVKKMWSKE------ESGAFNsEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYL 834
Cdd:cd05605     7 VLGKGGFGEVCacqvRAT---GKMYACKKLEKKRikkrkgEAMALN-EKQILEKVNSRFVVSLAYAYETKDALCLVLTIM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  835 PNGSLSSRLHGAGKGGCVDWEARY---DVVLGVAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIsgy 911
Cdd:cd05605    83 NGGDLKFHIYNMGNPGFEEERAVFyaaEITCGLEH----LHSE---RIVYRDLKPENILLDDHGHVRISDLGLAVEI--- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240256081  912 PNTgiDLAKptNRppmAGSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd05605   153 PEG--ETIR--GR---VGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAP 200
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
765-967 1.12e-03

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: 42.69  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  765 VIGTGSSGVVYRITIPSGESLAVKK------MWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGS 838
Cdd:cd05624    79 VIGRGAFGEVAVVKMKNTERIYAMKilnkweMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGD 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  839 LSSRLHGAGKGGCVDWEARY--DVVLGVaHALAYLHHdclptiIHGDVKAMNVLLGPHFEPYLADFG--LARTISGYPNT 914
Cdd:cd05624   159 LLTLLSKFEDKLPEDMARFYigEMVLAI-HSIHQLHY------VHRDIKPDNVLLDMNGHIRLADFGscLKMNDDGTVQS 231
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  915 GIDLAKPTnrppmagsygYMAPE-----HASMQRITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05624   232 SVAVGTPD----------YISPEilqamEDGMGKYGPECDWWSLGVCMYEMLYGETPF 279
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
879-967 1.22e-03

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: 42.20  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  879 IIHGDVKAMNVLLGPHFEPYLADFGLARTISGypntgidlAKPTNRppMAGSYGYMAPEHASMQRITEKSDVYSYGVVLL 958
Cdd:cd05607   125 IVYRDMKPENVLLDDNGNCRLSDLGLAVEVKE--------GKPITQ--RAGTNGYMAPEILKEESYSYPVDWFAMGCSIY 194

                  ....*....
gi 240256081  959 EVLTGKHPL 967
Cdd:cd05607   195 EMVAGRTPF 203
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
111-318 1.36e-03

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 42.94  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  111 KEIGDF---TELELLDLSDNSLSGDIPVEIFRLKKLKTLSLN-TNNLEgHIPMEIG-------NLSGLVELMLFDNklsg 179
Cdd:PLN03210  648 KEIPDLsmaTNLETLKLSDCSSLVELPSSIQYLNKLEDLDMSrCENLE-ILPTGINlkslyrlNLSGCSRLKSFPD---- 722
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  180 eIPRSIGELknlqVLRAGGNKNLRGELPweignCENLVMLGLAETSlSGKLpasignLKRVQTIAIYTSLLSgpipdeig 259
Cdd:PLN03210  723 -ISTNISWL----DLDETAIEEFPSNLR-----LENLDELILCEMK-SEKL------WERVQPLTPLMTMLS-------- 777
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  260 ycTELQNLYLYQNSISGSIPTTIGGLKKLQSLLLWQ-NNLVgKIPTELgNCPELWLIDFS 318
Cdd:PLN03210  778 --PSLTRLFLSDIPSLVELPSSIQNLHKLEHLEIENcINLE-TLPTGI-NLESLESLDLS 833
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
766-960 1.37e-03

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: 41.80  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLA---VKKMW---SKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSL 839
Cdd:cd05042     3 IGNGWFGKVLLGEIYSGTSVAqvvVKELKasaNPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLGDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  840 SSRLHGAGKGGCVDWEAR--YDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLA--RTISGYPNTG 915
Cdd:cd05042    83 KAYLRSEREHERGDSDTRtlQRMACEVAAGLAHLHKL---NFVHSDLALRNCLLTSDLTVKIGDYGLAhsRYKEDYIETD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240256081  916 IDLAKPTNrppmagsygYMAPE-----HASMQRI--TEKSDVYSYGVVLLEV 960
Cdd:cd05042   160 DKLWFPLR---------WTAPElvtefHDRLLVVdqTKYSNIWSLGVTLWEL 202
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
795-966 1.54e-03

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: 41.86  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  795 ESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRLHGAGK--GGCVDWEAR---------YDVVLG 863
Cdd:cd14206    40 EQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQLGDLKRYLRAQRKadGMTPDLPTRdlrtlqrmaYEITLG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLART--ISGYPNTGIDLAKPTNrppmagsygYMAPE---- 937
Cdd:cd14206   120 LLH----LHKN---NYIHSDLALRNCLLTSDLTVRIGDYGLSHNnyKEDYYLTPDRLWIPLR---------WVAPEllde 183
                         170       180       190
                  ....*....|....*....|....*....|...
gi 240256081  938 -HASMQRI--TEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd14206   184 lHGNLIVVdqSKESNVWSLGVTIWELFEfGAQP 216
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
829-972 1.65e-03

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: 42.17  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  829 LFYDYLPNGSLSSRLHGAGKggcVDWEARYDVVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLART- 907
Cdd:cd05610    81 LVMEYLIGGDVKSLLHIYGY---FDEEMAVKYISEVALALDYLHRH---GIIHRDLKPDNMLISNEGHIKLTDFGLSKVt 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  908 ------ISGYPNTGiDLAKPTN------------------------RPPMA--------------GSYGYMAPEHASMQR 943
Cdd:cd05610   155 lnrelnMMDILTTP-SMAKPKNdysrtpgqvlslisslgfntptpyRTPKSvrrgaarvegerilGTPDYLAPELLLGKP 233
                         170       180
                  ....*....|....*....|....*....
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHPLDPDLP 972
Cdd:cd05610   234 HGPAVDWWALGVCLFEFLTGIPPFNDETP 262
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
766-963 2.01e-03

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: 41.60  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAFNSEIKT---LGSIRHRNIVRLLGWCSNRNLKLLFYDYLpNGSLSS 841
Cdd:cd07869    13 LGEGSYATVYKgKSKVNGKLVALKVIRLQEEEGTPFTAIREaslLKGLKHANIVLLHDIIHTKETLTLVFEYV-HTDLCQ 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  842 RLHGAGKGGCVDWEARYdvVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTIS----GYPNTGID 917
Cdd:cd07869    92 YMDKHPGGLHPENVKLF--LFQLLRGLSYIHQR---YILHRDLKPQNLLISDTGELKLADFGLARAKSvpshTYSNEVVT 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 240256081  918 LAKptnRPP--MAGSYGYmapehasmqriTEKSDVYSYGVVLLEVLTG 963
Cdd:cd07869   167 LWY---RPPdvLLGSTEY-----------STCLDMWGVGCIFVEMIQG 200
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
880-980 2.06e-03

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: 41.53  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  880 IHGDVKAMNVLLGPHFEPYLADFGL--------------ARTISGYPNtgidlakptnrppmagsygYMAPEHASMQRIT 945
Cdd:cd05598   123 IHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdskyylAHSLVGTPN-------------------YIAPEVLLRTGYT 183
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 240256081  946 EKSDVYSYGVVLLEVLTGKHPLDPDLPGGAHL--VKW 980
Cdd:cd05598   184 QLCDWWSVGVILYEMLVGQPPFLAQTPAETQLkvINW 220
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
766-970 2.13e-03

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


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 41.14  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVK--KMWSKEESGAFNSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSR 842
Cdd:cd14191    10 LGSGKFGQVFRlVEKKTKKVWAGKffKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGELFER 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  843 LHGAgkggcvDWE------ARYdvVLGVAHALAYLHHDclpTIIHGDVKAMNVL----LGPHFEpyLADFGLARTISGYP 912
Cdd:cd14191    90 IIDE------DFElterecIKY--MRQISEGVEYIHKQ---GIVHLDLKPENIMcvnkTGTKIK--LIDFGLARRLENAG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240256081  913 NTGIDLAKPTnrppmagsygYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd14191   157 SLKVLFGTPE----------FVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGD 204
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
534-658 2.56e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 40.54  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  534 DNALSSTlpPGIGLLTELTKLNLAKNRLSgEIPrEISTCRSLQLLNLGENDFS---GeipdeLGQIPSLaISLNLSCNR- 609
Cdd:cd21340    33 DNKITKI--ENLEFLTNLTHLYLQNNQIE-KIE-NLENLVNLKKLYLGGNRISvveG-----LENLTNL-EELHIENQRl 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240256081  610 -----FVGEIPSRFSDLKNLGVLDVSHNQLTgNLNVLTDLQNLVSLNISYNDFS 658
Cdd:cd21340   103 ppgekLTFDPRSLAALSNSLRVLNISGNNID-SLEPLAPLRNLEQLDASNNQIS 155
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
859-967 2.94e-03

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: 41.19  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  859 DVVLGVAHalayLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLArtisgypntgIDLAKptnRPPMA--GSYGYMAP 936
Cdd:cd14223   111 EIILGLEH----MHSR---FVVYRDLKPANILLDEFGHVRISDLGLA----------CDFSK---KKPHAsvGTHGYMAP 170
                          90       100       110
                  ....*....|....*....|....*....|....
gi 240256081  937 EhaSMQR---ITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd14223   171 E--VLQKgvaYDSSADWFSLGCMLFKLLRGHSPF 202
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
167-508 3.24e-03

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 41.78  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  167 LVELMLFDNKLSgEIPRSIGELKNLQVLRAGGNKNLRgELPwEIGNCENLVMLGLAETSLSGKLPASIGNLKRVQTIaiy 246
Cdd:PLN03210  613 LVKLQMQGSKLE-KLWDGVHSLTGLRNIDLRGSKNLK-EIP-DLSMATNLETLKLSDCSSLVELPSSIQYLNKLEDL--- 686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  247 tsllsgpipdEIGYCTELQNL-------YLYQNSISG--------SIPTTIgglkklqSLLLWQNNLVGKIPTEL--GNC 309
Cdd:PLN03210  687 ----------DMSRCENLEILptginlkSLYRLNLSGcsrlksfpDISTNI-------SWLDLDETAIEEFPSNLrlENL 749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  310 PELWLIDF-SENLLTGTIPRS--FGKLE-NLQELQLSVNQISGTIPEELTNCTKLTHLEIDN--NLITgeIPSLMsNLRS 383
Cdd:PLN03210  750 DELILCEMkSEKLWERVQPLTplMTMLSpSLTRLFLSDIPSLVELPSSIQNLHKLEHLEIENciNLET--LPTGI-NLES 826
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  384 LtmffawqnkltgnIPQSLSQCRELQAIdlsynslsgsipkeifglrnltkllllsndlsgfipPDIGncTNLYRLRLNG 463
Cdd:PLN03210  827 L-------------ESLDLSGCSRLRTF------------------------------------PDIS--TNISDLNLSR 855
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 240256081  464 NRLAgSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLD 508
Cdd:PLN03210  856 TGIE-EVPWWIEKFSNLSFLDMNGCNNLQRVSLNISKLKHLETVD 899
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
868-967 3.32e-03

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: 41.06  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  868 LAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLAR-TISGYPNTGIdlakptnrppMAGSYGYMAPEHASMQRITE 946
Cdd:cd05619   119 LQFLHSK---GIVYRDLKLDNILLDKDGHIKIADFGMCKeNMLGDAKTST----------FCGTPDYIAPEILLGQKYNT 185
                          90       100
                  ....*....|....*....|.
gi 240256081  947 KSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05619   186 SVDWWSFGVLLYEMLIGQSPF 206
LRR_8 pfam13855
Leucine rich repeat;
358-418 3.42e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 3.42e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256081   358 TKLTHLEIDNNLITGEIPSLMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSL 418
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
489-656 3.66e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 40.80  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  489 RLVGSIPPAISGCESLEFLDLHTNSLS----GSLLGTTLPKSLKFIDFSDNALSST-LPPGIGLLTE----LTKLNLAKN 559
Cdd:cd00116    68 RGLQSLLQGLTKGCGLQELDLSDNALGpdgcGVLESLLRSSSLQELKLNNNGLGDRgLRLLAKGLKDlppaLEKLVLGRN 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  560 RLSGE----IPREISTCRSLQLLNLGENDFSGEIPDELGQI---PSLAISLNLSCNRF----VGEIPSRFSDLKNLGVLD 628
Cdd:cd00116   148 RLEGAsceaLAKALRANRDLKELNLANNGIGDAGIRALAEGlkaNCNLEVLDLNNNGLtdegASALAETLASLKSLEVLN 227
                         170       180       190
                  ....*....|....*....|....*....|....
gi 240256081  629 VSHNQLTGN------LNVLTDLQNLVSLNISYND 656
Cdd:cd00116   228 LGDNNLTDAgaaalaSALLSPNISLLTLSLSCND 261
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
867-972 4.21e-03

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: 40.63  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  867 ALAYLHHdclPTIIHGDVKAMNVLLGPHFEPYLADFGLARtisgypntgIDLAKPTNRPPMAGSYGYMAPEHASMQRITE 946
Cdd:cd05585   106 ALECLHK---FNVIYRDLKPENILLDYTGHIALCDFGLCK---------LNMKDDDKTNTFCGTPEYLAPELLLGHGYTK 173
                          90       100
                  ....*....|....*....|....*..
gi 240256081  947 KSDVYSYGVVLLEVLTGKHPL-DPDLP 972
Cdd:cd05585   174 AVDWWTLGVLLYEMLTGLPPFyDENTN 200
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
766-967 4.98e-03

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: 40.25  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYRITIPSGESLAVKKMWSKEESGAFNSEIKTLGsirHRNIVRLLGWCSNR---NLKLLFY---------DY 833
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIG---ERNILVRTALDESPfivGLKFSFQtptdlylvtDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  834 LPNGSLSSRLHGAGKGGcvDWEARY---DVVLgvahALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARTis 909
Cdd:cd05586    78 MSGGELFWHLQKEGRFS--EDRAKFyiaELVL----ALEHLHkND----IVYRDLKPENILLDANGHIALCDFGLSKA-- 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  910 gypntgiDLAKPTNRPPMAGSYGYMAPEHASMQR-ITEKSDVYSYGVVLLEVLTGKHPL 967
Cdd:cd05586   146 -------DLTDNKTTNTFCGTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPF 197
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
766-966 5.26e-03

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 40.23  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVKKMWSKEESGAF-NSEIKTLGSIRHRNIVRLLGWCSNRNLKLLFYDYLPNGSLSSRL 843
Cdd:cd14104     8 LGRGQFGIVHRcVETSSKKTYMAKFVKVKGADQVLvKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVDIFERI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  844 HGA----GKGGCVDWearydvVLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPY--LADFGLARTisgypntgid 917
Cdd:cd14104    88 TTArfelNEREIVSY------VRQVCEALEFLHSK---NIGHFDIRPENIIYCTRRGSYikIIEFGQSRQ---------- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 240256081  918 lAKPTNRPPMA-GSYGYMAPEHASMQRITEKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14104   149 -LKPGDKFRLQyTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINP 197
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
855-919 5.30e-03

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 38.79  E-value: 5.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240256081  855 EARYDVVLGVAHALAYLH-HDclptIIHGDVKAMNVLLGPHfEPYLADFGLARTISGYPNTGIDLA 919
Cdd:COG3642    51 ELPPELLRELGRLLARLHrAG----IVHGDLTTSNILVDDG-GVYLIDFGLARYSDPLEDKAVDLA 111
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
861-966 5.48e-03

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: 39.90  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  861 VLGVAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARTI-SG-YPNTGIDLAKPTNrppmagsygYMAPEH 938
Cdd:cd05074   129 MIDIASGMEYLSSK---NFIHRDLAARNCMLNENMTVCVADFGLSKKIySGdYYRQGCASKLPVK---------WLALES 196
                          90       100
                  ....*....|....*....|....*....
gi 240256081  939 ASMQRITEKSDVYSYGVVLLEVLT-GKHP 966
Cdd:cd05074   197 LADNVYTTHSDVWAFGVTMWEIMTrGQTP 225
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
868-971 6.63e-03

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; 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. VRK2 exists as two alternative splice forms, A and B, which differ in their C-terminal regions. VRK2A, the predominant isoform, contains a hydrophobic tail and is anchored to the ER and mitochondria. It is expressed in all cell types. VRK2B lacks a membrane-anchor tail and is detected in the cytosol and the nucleus. Like VRK1, it can stabilize p53. VRK2B functionally replaces VRK1 in the nucleus of cell types where VRK1 is absent. VRK2 modulates hypoxia-induced stress responses by interacting with TAK1, an atypical MAPK kinase kinase which triggers cascades that activate JNK following oxidative stress. VRK2 also interacts with JIP1, a scaffold protein that assembles three consecutive members of a MAPK pathway. This interaction prevents the association of JNK with the signaling complex, leading to reduced phosphorylation and AP1-dependent transcription. The VRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271025 [Multi-domain]  Cd Length: 302  Bit Score: 39.83  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  868 LAYLHHDclpTIIHGDVKAMNVLLG---PHfEPYLADFGLARTISgyPNTGIDLAKPTNRPPMAGSYGYMAPEHASMQRI 944
Cdd:cd14123   142 LEYIHEN---EYVHGDIKAANLLLGyrnPN-EVYLADYGLSYRYC--PNGNHKEYKENPRKGHNGTIEFTSLDAHKGVAP 215
                          90       100
                  ....*....|....*....|....*..
gi 240256081  945 TEKSDVYSYGVVLLEVLTGKHPLDPDL 971
Cdd:cd14123   216 SRRGDLEILGYCMLHWLCGKLPWEQNL 242
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
864-970 6.68e-03

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: 39.78  E-value: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLH-HDclptIIHGDVKAMNVLLGPHFEPYLADFGLARtisgypnTGIDLAKPTNrpPMAGSYGYMAPEHASMQ 942
Cdd:cd05591   105 VTLALMFLHrHG----VIYRDLKLDNILLDAEGHCKLADFGMCK-------EGILNGKTTT--TFCGTPDYIAPEILQEL 171
                          90       100
                  ....*....|....*....|....*...
gi 240256081  943 RITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd05591   172 EYGPSVDWWALGVLMYEMMAGQPPFEAD 199
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
454-562 6.80e-03

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: 40.16  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  454 TNLYRLRLNGNRL----AGSIPSEIGNLKNLNFVDISENRL----VGSIPPAISGCESLEFLDLHTNSLSGS---LLGTT 522
Cdd:COG5238   264 TTVETLYLSGNQIgaegAIALAKALQGNTTLTSLDLSVNRIgdegAIALAEGLQGNKTLHTLNLAYNGIGAQgaiALAKA 343
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 240256081  523 LPK--SLKFIDFSDNALS----STLPPGIGLLTELTKLNLAKNRLS 562
Cdd:COG5238   344 LQEntTLHSLDLSDNQIGdegaIALAKYLEGNTTLRELNLGKNNIG 389
LRR_8 pfam13855
Leucine rich repeat;
117-177 6.81e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.96  E-value: 6.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240256081   117 TELELLDLSDNSLSgDIPVEIFR-LKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKL 177
Cdd:pfam13855    1 PNLRSLDLSNNRLT-SLDDGAFKgLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
866-966 6.84e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 39.62  E-value: 6.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  866 HALAYLHHDCLPTIIhgdvkAMNVLLGPHFEPYLADFGLARTisgYPNTGIDLAKPTNRPPMAGSYGYMAPEHASMQRIT 945
Cdd:cd14130   114 HSVGFLHRDIKPSNF-----AMGRLPSTYRKCYMLDFGLARQ---YTNTTGEVRPPRNVAGFRGTVRYASVNAHKNREMG 185
                          90       100
                  ....*....|....*....|.
gi 240256081  946 EKSDVYSYGVVLLEVLTGKHP 966
Cdd:cd14130   186 RHDDLWSLFYMLVEFAVGQLP 206
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
864-970 6.86e-03

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: 39.89  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  864 VAHALAYLHHDclpTIIHGDVKAMNVLLGPHFEPYLADFGLARtisgypnTGIDLAKPTNrpPMAGSYGYMAPEHASMQR 943
Cdd:cd05590   105 ITSALMFLHDK---GIIYRDLKLDNVLLDHEGHCKLADFGMCK-------EGIFNGKTTS--TFCGTPDYIAPEILQEML 172
                          90       100
                  ....*....|....*....|....*..
gi 240256081  944 ITEKSDVYSYGVVLLEVLTGKHPLDPD 970
Cdd:cd05590   173 YGPSVDWWAMGVLLYEMLCGHAPFEAE 199
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
766-905 9.46e-03

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: 39.45  E-value: 9.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256081  766 IGTGSSGVVYR-ITIPSGESLAVK-----KMWskeesgAFNSEIKTLGSIR-HRNIVRLLGWCSNRNLKL--LFYDYLPN 836
Cdd:cd14132    26 IGRGKYSEVFEgINIGNNEKVVIKvlkpvKKK------KIKREIKILQNLRgGPNIVKLLDVVKDPQSKTpsLIFEYVNN 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240256081  837 gslssrlhgagkggcVDWEARY------DVVL---GVAHALAYLHHDclpTIIHGDVKAMNVLLGP-HFEPYLADFGLA 905
Cdd:cd14132   100 ---------------TDFKTLYptltdyDIRYymyELLKALDYCHSK---GIMHRDVKPHNIMIDHeKRKLRLIDWGLA 160
 
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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