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Conserved domains on  [gi|578829925|ref|XP_006721599|]
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misshapen-like kinase 1 isoform X11 [Homo sapiens]

Protein Classification

mitogen-activated protein kinase kinase kinase kinase( domain architecture ID 10159706)

mitogen-activated protein kinase kinase kinase kinase (MAP4K) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Mus musculus misshapen-like kinase 1, also caled MAP4K6

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Ontology:  GO:0004674|GO:0006468|GO:0005524
PubMed:  19614568
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
8-289 0e+00

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: 621.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    8 RSLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYG 87
Cdd:cd06636     1 RSLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   88 AFIKKSPPGNDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 167
Cdd:cd06636    81 AFIKKSPPGHDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  168 KLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR 247
Cdd:cd06636   161 KLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578829925  248 NPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06636   241 NPPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
CNH smart00036
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;
1006-1304 1.55e-94

Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;


:

Pssm-ID: 214481  Cd Length: 302  Bit Score: 306.20  E-value: 1.55e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1006 YKKRFNSEILCAALWgvnLLVGTENGLMLLDRSGQ-GKVYGLIGRRRFQQMDVLEGLNLLITISGKRNKLRVYYLSWLRN 1084
Cdd:smart00036    1 NTAKWNHPITCDGKW---LLVGTEEGLYVLNISDQpGTLEKLIGRRSVTQIWVLEENNVLLMISGKKPQLYSHPLSALVE 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1085 KILH--NDPEVEKKQGWTTVGDMEGCGHYRVVKYERIKFLVIALKSSVEVYAWaPKPYHKFMAFKSFADLP---HRPLLV 1159
Cdd:smart00036   78 KKEAlgSARLVIRKNVLTKIPDVKGCHLCAVVNGKRSLFLCVALQSSVVLLQW-YNPLKKFKLFKSKFLFPlisPVPVFV 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1160 DLTVEEGQRLKVIYGSS-AGFHAVDVDS--GNSYDIYIPVH-IQSQITPHAIIFLPNtdgMEMLLCYEDEGVYVNTYG-R 1234
Cdd:smart00036  157 ELVSSSFERPGICIGSDkGGGDVVQFHEslVSKEDLSLPFLsEETSLKPISVVQVPR---DEVLLCYDEFGVFVNLYGkR 233
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1235 IIKDVVLQWGEMPTSVAYIcSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVR 1304
Cdd:smart00036  234 RSRNPILHWEFMPESFAYH-SPYLLAFHDNGIEIRSIKTGELLQELADRETRKIRLLGSSDRKILLSSSP 302
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
537-793 3.07e-12

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 71.74  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  537 GRGMNPADKPAWAREVEERTRMNKQQNSPLAKSKPGSTGPEPPIPQASPGPPGPLSqTPPMQRPVEPQEGPHKSLVAHRV 616
Cdd:PHA03307   58 GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSS-PDPPPPTPPPASPPPSPAPDLSE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  617 PLKPYAAPVPRSQslqdqptrnlAAFPASHDPDPAIPAPTATPsaRGAVIRQNSDPTSEGPGPSPNPPAWVRPDNEAPPK 696
Cdd:PHA03307  137 MLRPVGSPGPPPA----------ASPPAAGASPAAVASDAASS--RQAALPLSSPEETARAPSSPPAEPPPSTPPAAASP 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  697 VPQRTSSIA-------TALNTSGAGGSRPAQAVRASNPDLRRSDPGwERSDSVLPaSHGHLPQAGSLERNRVGVSSKPDS 769
Cdd:PHA03307  205 RPPRRSSPIsasasspAPAPGRSAADDAGASSSDSSSSESSGCGWG-PENECPLP-RPAPITLPTRIWEASGWNGPSSRP 282
                         250       260
                  ....*....|....*....|....
gi 578829925  770 SPVLSPGNKAKPDDhRSRPGRPAD 793
Cdd:PHA03307  283 GPASSSSSPRERSP-SPSPSSPGS 305
 
Name Accession Description Interval E-value
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
8-289 0e+00

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: 621.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    8 RSLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYG 87
Cdd:cd06636     1 RSLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   88 AFIKKSPPGNDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 167
Cdd:cd06636    81 AFIKKSPPGHDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  168 KLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR 247
Cdd:cd06636   161 KLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578829925  248 NPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06636   241 NPPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
CNH smart00036
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;
1006-1304 1.55e-94

Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;


Pssm-ID: 214481  Cd Length: 302  Bit Score: 306.20  E-value: 1.55e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1006 YKKRFNSEILCAALWgvnLLVGTENGLMLLDRSGQ-GKVYGLIGRRRFQQMDVLEGLNLLITISGKRNKLRVYYLSWLRN 1084
Cdd:smart00036    1 NTAKWNHPITCDGKW---LLVGTEEGLYVLNISDQpGTLEKLIGRRSVTQIWVLEENNVLLMISGKKPQLYSHPLSALVE 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1085 KILH--NDPEVEKKQGWTTVGDMEGCGHYRVVKYERIKFLVIALKSSVEVYAWaPKPYHKFMAFKSFADLP---HRPLLV 1159
Cdd:smart00036   78 KKEAlgSARLVIRKNVLTKIPDVKGCHLCAVVNGKRSLFLCVALQSSVVLLQW-YNPLKKFKLFKSKFLFPlisPVPVFV 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1160 DLTVEEGQRLKVIYGSS-AGFHAVDVDS--GNSYDIYIPVH-IQSQITPHAIIFLPNtdgMEMLLCYEDEGVYVNTYG-R 1234
Cdd:smart00036  157 ELVSSSFERPGICIGSDkGGGDVVQFHEslVSKEDLSLPFLsEETSLKPISVVQVPR---DEVLLCYDEFGVFVNLYGkR 233
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1235 IIKDVVLQWGEMPTSVAYIcSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVR 1304
Cdd:smart00036  234 RSRNPILHWEFMPESFAYH-SPYLLAFHDNGIEIRSIKTGELLQELADRETRKIRLLGSSDRKILLSSSP 302
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-289 5.94e-86

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 280.19  E-value: 5.94e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925     25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE--IKQEINMLKKySHHRNIATYYGAFIkksppgNDDQLW 102
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRerILREIKILKK-LKHPNIVRLYDVFE------DEDKLY 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    103 LVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTv 182
Cdd:smart00220   74 LVMEYCEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG- 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    183 GRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRL--KSKKWSK 260
Cdd:smart00220  151 EKLTTFVGTPEYMAPEVLLGKG-----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFppPEWDISP 225
                           250       260
                    ....*....|....*....|....*....
gi 578829925    261 KFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:smart00220  226 EAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
CNH pfam00780
CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished ...
1020-1294 1.66e-81

CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished observations.


Pssm-ID: 459938  Cd Length: 261  Bit Score: 267.96  E-value: 1.66e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  1020 WGVNLLVGTENGLMLLDRSGQGKVYGLIGRRRFQQMDVLEGLNLLITISGKRNKLRVYYLSWLRNKILHNDPEVekkqGW 1099
Cdd:pfam00780    1 GGQNLLLGTEEGLYVLNRSGPREPVRIIDKKRVTQLAVLEEFNLLLLLSGKDKRLYVYPLSALDSREENDRKDA----AK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  1100 TTVGDMEGCGHYRVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFaDLPHRPLLVDLTVEegqrlKVIYGSSAGF 1179
Cdd:pfam00780   77 NKLPETKGCHFFKVGRHSNGRFLVVAVKRTIKLLEWYEPLLDKFRKFKEF-YLPSPPVSIELLKS-----KLCVGCAKGF 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  1180 HAVDVDSGNSYDIYIPVHI---QSQITPHAIIFLpntDGMEMLLCYEDEGVYVNTYGRIIKDVVLQWGEMPTSVAYiCSN 1256
Cdd:pfam00780  151 EIVSLDSKATESLLTSLLFanrQENLKPLAVVRL---DRSEFLLCYNEFGVYVNLQGRRSRPWEIEWEGAPEAVAY-LYP 226
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 578829925  1257 QIMGWGEKAIEIRSVETGHLDGVFmhkRAQRLKFLCER 1294
Cdd:pfam00780  227 YLLAFHDNFIEIRDVETGELVQEI---AGRKIRFLNSG 261
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
22-280 7.09e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.61  E-value: 7.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   22 AGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEI----KQEINMLKKySHHRNIATYYGAFIkksppgN 97
Cdd:COG0515     6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEArerfRREARALAR-LNHPNIVRVYDVGE------E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 DDQLWLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:COG0515    79 DGRPYLVMEYVEGESLADLLR--RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRT-VGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSK 256
Cdd:COG0515   157 LGGAtLTQTGTVVGTPGYMAPEQARGEP-----VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSEL 231
                         250       260
                  ....*....|....*....|....*.
gi 578829925  257 KW--SKKFIDFIDTCLIKTYLSRPPT 280
Cdd:COG0515   232 RPdlPPALDAIVLRALAKDPEERYQS 257
Pkinase pfam00069
Protein kinase domain;
25-289 1.54e-44

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 160.87  E-value: 1.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ---EINMLKKYShHRNIATYYGAFIkksppgNDDQL 101
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNilrEIKILKKLN-HPNIVRLYDAFE------DKDNL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   102 WLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLhahkvihrdikgqnvlltenaevklvdfgvsaqldrt 181
Cdd:pfam00069   74 YLVLEYVEGGSLFDLLSEKG--AFSEREAKFIMKQILEGLESG------------------------------------- 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   182 vGRRNTFIGTPYWMAPEVIacDENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNP-PPRLKSKKWSK 260
Cdd:pfam00069  115 -SSLTTFVGTPWYMAPEVL--GGNP---YGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPyAFPELPSNLSE 188
                          250       260
                   ....*....|....*....|....*....
gi 578829925   261 KFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:pfam00069  189 EAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
2-297 5.72e-30

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 123.01  E-value: 5.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    2 GDPAPARSLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKySHH 79
Cdd:PLN00034   53 SSSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQICREIEILRD-VNH 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   80 RNIATYYGAFikksppGNDDQLWLVMEFCGAGSVtdlvKNTKGNalKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNV 159
Cdd:PLN00034  132 PNVVKCHDMF------DHNGEIQVLLEFMDGGSL----EGTHIA--DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  160 LLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENpDATYD-YRSDIWSLGITAIEMAEGAPPLC---- 234
Cdd:PLN00034  200 LINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTDLN-HGAYDgYAGDIWSLGVSILEFYLGRFPFGvgrq 278
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  235 -DMHP-MRALFLI-PRNPPPRLkskkwSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI-RDQPTERQ 297
Cdd:PLN00034  279 gDWASlMCAICMSqPPEAPATA-----SREFRHFISCCLQREPAKRWSAMQLLQHPFIlRAQPGQGQ 340
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
133-232 6.99e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 85.62  E-value: 6.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  133 ICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG----VSAQldrTVGRRNTFIGTPYWMAPEVIAcdenpDA 208
Cdd:NF033483  112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaraLSST---TMTQTNSVLGTVHYLSPEQAR-----GG 183
                          90       100
                  ....*....|....*....|....
gi 578829925  209 TYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:NF033483  184 TVDARSDIYSLGIVLYEMLTGRPP 207
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
537-793 3.07e-12

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 71.74  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  537 GRGMNPADKPAWAREVEERTRMNKQQNSPLAKSKPGSTGPEPPIPQASPGPPGPLSqTPPMQRPVEPQEGPHKSLVAHRV 616
Cdd:PHA03307   58 GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSS-PDPPPPTPPPASPPPSPAPDLSE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  617 PLKPYAAPVPRSQslqdqptrnlAAFPASHDPDPAIPAPTATPsaRGAVIRQNSDPTSEGPGPSPNPPAWVRPDNEAPPK 696
Cdd:PHA03307  137 MLRPVGSPGPPPA----------ASPPAAGASPAAVASDAASS--RQAALPLSSPEETARAPSSPPAEPPPSTPPAAASP 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  697 VPQRTSSIA-------TALNTSGAGGSRPAQAVRASNPDLRRSDPGwERSDSVLPaSHGHLPQAGSLERNRVGVSSKPDS 769
Cdd:PHA03307  205 RPPRRSSPIsasasspAPAPGRSAADDAGASSSDSSSSESSGCGWG-PENECPLP-RPAPITLPTRIWEASGWNGPSSRP 282
                         250       260
                  ....*....|....*....|....
gi 578829925  770 SPVLSPGNKAKPDDhRSRPGRPAD 793
Cdd:PHA03307  283 GPASSSSSPRERSP-SPSPSSPGS 305
 
Name Accession Description Interval E-value
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
8-289 0e+00

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: 621.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    8 RSLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYG 87
Cdd:cd06636     1 RSLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   88 AFIKKSPPGNDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 167
Cdd:cd06636    81 AFIKKSPPGHDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  168 KLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR 247
Cdd:cd06636   161 KLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578829925  248 NPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06636   241 NPPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
18-313 0e+00

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: 565.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   18 LRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPPGN 97
Cdd:cd06637     1 LRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPPGM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 DDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd06637    81 DDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKK 257
Cdd:cd06637   161 LDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKSKK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVRIQLKDHIDRSRKKR 313
Cdd:cd06637   241 WSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQPNERQVRIQLKDHIDRTKKKR 296
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
18-289 0e+00

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: 549.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   18 LRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPPGN 97
Cdd:cd06608     1 LPDPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFSNHPNIATFYGAFIKKDPPGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 DDQLWLVMEFCGAGSVTDLVKNT--KGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd06608    81 DDQLWLVMEYCGGGSVTDLVKGLrkKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS 255
Cdd:cd06608   161 AQLDSTLGRRNTFIGTPYWMAPEVIACDQQPDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPPPTLKS 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578829925  256 -KKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06608   241 pEKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
24-289 1.07e-123

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: 383.58  E-value: 1.07e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTED-EEEEIKQEINMLKKYSHhRNIATYYGAFIKksppgnDDQLW 102
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGdDFEIIQQEISMLKECRH-PNIVAYFGSYLR------RDKLW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd06613    74 IVMEYCGGGSLQDIYQVT--GPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIGTPYWMAPEVIAcdENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR--NPPPRLKSK-KWS 259
Cdd:cd06613   152 AKRKSFIGTPYWMAPEVAA--VERKGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKsnFDPPKLKDKeKWS 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06613   230 PDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
24-289 6.58e-122

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: 378.47  E-value: 6.58e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV-TEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKksppgnDDQLW 102
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLeSKEKKESILNEIAILKKCKH-PNIVKYYGSYLK------KDELW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd05122    74 IVMEFCSGGSLKDLLKNTNK-TLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GrRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS-KKWSKK 261
Cdd:cd05122   153 T-RNTFVGTPYWMAPEVIQGKP-----YGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNpKKWSKE 226
                         250       260
                  ....*....|....*....|....*...
gi 578829925  262 FIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd05122   227 FKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
21-289 7.06e-113

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: 354.26  E-value: 7.06e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKqEINMLKKySHHRNIATYYGAFIKksppgnDDQ 100
Cdd:cd06612     1 PEEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIK-EISILKQ-CDSPYIVKYYGSYFK------NTD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd06612    73 LWIVMEYCGAGSVSDIMKIT-NKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS-KKWS 259
Cdd:cd06612   152 TMAKRNTVIGTPFWMAPEVIQ--EIG---YNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDpEKWS 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06612   227 PEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
24-290 6.60e-110

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: 346.92  E-value: 6.60e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV--TEDEEEEIKQEINMLKKySHHRNIATYYGAFIKKSppgnddQL 101
Cdd:cd06609     2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLeeAEDEIEDIQQEIQFLSQ-CDSPYITKYYGSFLKGS------KL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd06609    75 WIIMEYCGGGSVLDLLKPGP---LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTST 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKK 261
Cdd:cd06609   152 MSKRNTFVGTPFWMAPEVIKQSG-----YDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGNKFSKP 226
                         250       260
                  ....*....|....*....|....*....
gi 578829925  262 FIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06609   227 FKDFVELCLNKDPKERPSAKELLKHKFIK 255
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
20-289 1.03e-106

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: 338.91  E-value: 1.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPPgNDD 99
Cdd:cd06638    15 DPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKFYGMYYKKDVK-NGD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKN--TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd06638    94 QLWLVLELCNGGSVTDLVKGflKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKK 257
Cdd:cd06638   174 LTSTRLRRNTSVGTPFWMAPEVIACEQQLDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPTLHQPE 253
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578829925  258 -WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06638   254 lWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
13-290 4.65e-102

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: 326.18  E-value: 4.65e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   13 IDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKk 92
Cdd:cd06639    12 LGLESLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLPNHPNVVKFYGMFYK- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 SPPGNDDQLWLVMEFCGAGSVTDLVKN--TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV 170
Cdd:cd06639    91 ADQYVGGQLWLVLELCNGGSVTELVKGllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  171 DFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPP 250
Cdd:cd06639   171 DFGVSAQLTSARLRRNTSVGTPFWMAPEVIACEQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNPP 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578829925  251 PRLKS-KKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06639   251 PTLLNpEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
24-289 3.06e-98

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: 314.53  E-value: 3.06e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKySHHRNIATYYGAFIKksppgnDDQLWL 103
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILIMKE-CKHPNIVDYYDSYLV------GDELWV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVG 183
Cdd:cd06614    74 VMEYMDGGSLTDIITQNP-VRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  184 RRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLK-SKKWSKKF 262
Cdd:cd06614   153 KRNSVVGTPYWMAPEVIKRKD-----YGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKGIPPLKnPEKWSPEF 227
                         250       260
                  ....*....|....*....|....*..
gi 578829925  263 IDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06614   228 KDFLNKCLVKDPEKRPSAEELLQHPFL 254
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
20-302 5.47e-97

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: 312.06  E-value: 5.47e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE-EEIKQEINMLKKYSHhRNIATYYGAFIkksppgND 98
Cdd:cd06611     2 NPNDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEElEDFMVEIDILSECKH-PNIVGLYEAYF------YE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06611    75 NKLWILIEFCDGGALDSIMLEL-ERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRL-KSKK 257
Cdd:cd06611   154 KSTLQKRDTFIGTPYWMAPEVVACETFKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTLdQPSK 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVRIQL 302
Cdd:cd06611   234 WSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKAIKDLL 278
CNH smart00036
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;
1006-1304 1.55e-94

Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;


Pssm-ID: 214481  Cd Length: 302  Bit Score: 306.20  E-value: 1.55e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1006 YKKRFNSEILCAALWgvnLLVGTENGLMLLDRSGQ-GKVYGLIGRRRFQQMDVLEGLNLLITISGKRNKLRVYYLSWLRN 1084
Cdd:smart00036    1 NTAKWNHPITCDGKW---LLVGTEEGLYVLNISDQpGTLEKLIGRRSVTQIWVLEENNVLLMISGKKPQLYSHPLSALVE 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1085 KILH--NDPEVEKKQGWTTVGDMEGCGHYRVVKYERIKFLVIALKSSVEVYAWaPKPYHKFMAFKSFADLP---HRPLLV 1159
Cdd:smart00036   78 KKEAlgSARLVIRKNVLTKIPDVKGCHLCAVVNGKRSLFLCVALQSSVVLLQW-YNPLKKFKLFKSKFLFPlisPVPVFV 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1160 DLTVEEGQRLKVIYGSS-AGFHAVDVDS--GNSYDIYIPVH-IQSQITPHAIIFLPNtdgMEMLLCYEDEGVYVNTYG-R 1234
Cdd:smart00036  157 ELVSSSFERPGICIGSDkGGGDVVQFHEslVSKEDLSLPFLsEETSLKPISVVQVPR---DEVLLCYDEFGVFVNLYGkR 233
                           250       260       270       280       290       300       310
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   1235 IIKDVVLQWGEMPTSVAYIcSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVR 1304
Cdd:smart00036  234 RSRNPILHWEFMPESFAYH-SPYLLAFHDNGIEIRSIKTGELLQELADRETRKIRLLGSSDRKILLSSSP 302
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-289 5.94e-86

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 280.19  E-value: 5.94e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925     25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE--IKQEINMLKKySHHRNIATYYGAFIkksppgNDDQLW 102
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRerILREIKILKK-LKHPNIVRLYDVFE------DEDKLY 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    103 LVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTv 182
Cdd:smart00220   74 LVMEYCEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPG- 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    183 GRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRL--KSKKWSK 260
Cdd:smart00220  151 EKLTTFVGTPEYMAPEVLLGKG-----YGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFppPEWDISP 225
                           250       260
                    ....*....|....*....|....*....
gi 578829925    261 KFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:smart00220  226 EAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
19-289 1.06e-85

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: 280.38  E-value: 1.06e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   19 RDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE-EEIKQEINMLKKYSHHrNIATYYGAFIKKsppgn 97
Cdd:cd06646     5 RNPQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDfSLIQQEIFMVKECKHC-NIVAYFGSYLSR----- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 dDQLWLVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd06646    79 -EKLWICMEYCGGGSLQDIYHVT--GPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIACDENpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRN--PPPRLKS 255
Cdd:cd06646   156 ITATIAKRKSFIGTPYWMAPEVAAVEKN--GGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSnfQPPKLKD 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578829925  256 K-KWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06646   234 KtKWSSTFHNFVKISLTKNPKKRPTAERLLTHLFV 268
CNH pfam00780
CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished ...
1020-1294 1.66e-81

CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished observations.


Pssm-ID: 459938  Cd Length: 261  Bit Score: 267.96  E-value: 1.66e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  1020 WGVNLLVGTENGLMLLDRSGQGKVYGLIGRRRFQQMDVLEGLNLLITISGKRNKLRVYYLSWLRNKILHNDPEVekkqGW 1099
Cdd:pfam00780    1 GGQNLLLGTEEGLYVLNRSGPREPVRIIDKKRVTQLAVLEEFNLLLLLSGKDKRLYVYPLSALDSREENDRKDA----AK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  1100 TTVGDMEGCGHYRVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFaDLPHRPLLVDLTVEegqrlKVIYGSSAGF 1179
Cdd:pfam00780   77 NKLPETKGCHFFKVGRHSNGRFLVVAVKRTIKLLEWYEPLLDKFRKFKEF-YLPSPPVSIELLKS-----KLCVGCAKGF 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  1180 HAVDVDSGNSYDIYIPVHI---QSQITPHAIIFLpntDGMEMLLCYEDEGVYVNTYGRIIKDVVLQWGEMPTSVAYiCSN 1256
Cdd:pfam00780  151 EIVSLDSKATESLLTSLLFanrQENLKPLAVVRL---DRSEFLLCYNEFGVYVNLQGRRSRPWEIEWEGAPEAVAY-LYP 226
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 578829925  1257 QIMGWGEKAIEIRSVETGHLDGVFmhkRAQRLKFLCER 1294
Cdd:pfam00780  227 YLLAFHDNFIEIRDVETGELVQEI---AGRKIRFLNSG 261
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
25-289 8.52e-80

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: 263.45  E-value: 8.52e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE--EIKQEINMLKKySHHRNIATYYGAFIKksppgnDDQLW 102
Cdd:cd06610     3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSmdELRKEIQAMSQ-CNHPNVVSYYTSFVV------GDELW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNT-KGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--- 178
Cdd:cd06610    76 LVMPLLSGGSLLDIMKSSyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLatg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 -DRTVGRRNTFIGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS-- 255
Cdd:cd06610   156 gDRTRKVRKTFVGTPCWMAPEVM----EQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETga 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  256 --KKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06610   232 dyKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
24-292 1.05e-79

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: 263.57  E-value: 1.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLK--KYSHHRNIATYYGAFIKksppgnDD 99
Cdd:cd06917     2 LYRRLELVGRGSYGAVYRGYHVKTGRVVALKVlnLDTDDDDVSDIQKEVALLSqlKLGQPKNIIKYYGSYLK------GP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKntkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd06917    76 SLWIIMDYCEGGSIRTLMR---AGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWS 259
Cdd:cd06917   153 QNSSKRSTFVGTPYWMAPEVIT----EGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRLEGNGYS 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQ 292
Cdd:cd06917   229 PLLKEFVAACLDEEPKDRLSADELLKSKWIKQH 261
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
13-289 1.98e-79

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: 262.67  E-value: 1.98e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   13 IDLSAlRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE-EEIKQEINMLKKySHHRNIATYYGAFIK 91
Cdd:cd06645     2 LDLSR-RNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDfAVVQQEIIMMKD-CKHSNIVAYFGSYLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   92 KsppgndDQLWLVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVD 171
Cdd:cd06645    80 R------DKLWICMEFCGGGSLQDIYHVT--GPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLAD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  172 FGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRN--P 249
Cdd:cd06645   152 FGVSAQITATIAKRKSFIGTPYWMAPEVAAVERK--GGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSnfQ 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578829925  250 PPRLKSK-KWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06645   230 PPKLKDKmKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFV 270
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
24-290 5.16e-79

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: 260.84  E-value: 5.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE----IKQEINMLKKYSHhRNIATYYGAFIKksppgnDD 99
Cdd:cd06607     2 IFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEkwqdIIKEVKFLRQLRH-PNTIEYKGCYLR------EH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCgAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvSAQLd 179
Cdd:cd06607    75 TAWLVMEYC-LGSASDIVEVHK-KPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG-SASL- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 rtVGRRNTFIGTPYWMAPEVI-ACDENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKW 258
Cdd:cd06607   151 --VCPANSFVGTPYWMAPEVIlAMDEGQ---YDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNDSPTLSSGEW 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  259 SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06607   226 SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
20-299 1.54e-77

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: 258.04  E-value: 1.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV-TEDEEEEIKQEINMLKKYSHHrNIATYYGAFIkksppgND 98
Cdd:cd06644     9 DPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETkSEEELEDYMVEIEILATCNHP-YIVKLLGAFY------WD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVtDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06644    82 GKLWIMIEFCPGGAV-DAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS-KK 257
Cdd:cd06644   161 VKTLQRRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQpSK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVR 299
Cdd:cd06644   241 WSMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVTSNRPLR 282
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
25-289 3.73e-75

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: 250.13  E-value: 3.73e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEI---KQEINMLKKYSHHrNIATYYGAFIKKsppgndDQL 101
Cdd:cd06606     2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELealEREIRILSSLKHP-NIVRYLGTERTE------NTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD-- 179
Cdd:cd06606    75 NIFLEYVPGGSLASLLK--KFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAei 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMH-PMRALFLI-----PRNPPPRL 253
Cdd:cd06606   153 ATGEGTKSLRGTPYWMAPEVIRGEG-----YGRAADIWSLGCTVIEMATGKPPWSELGnPVAALFKIgssgePPPIPEHL 227
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  254 kskkwSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06606   228 -----SEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
20-299 1.60e-74

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: 249.17  E-value: 1.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV-TEDEEEEIKQEINMLKKySHHRNIATYYGAFIKKSppgnd 98
Cdd:cd06643     2 NPEDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTkSEEELEDYMVEIDILAS-CDHPNIVKLLDAFYYEN----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dQLWLVMEFCGAGSVtDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06643    76 -NLWILIEFCAGGAV-DAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS-KK 257
Cdd:cd06643   154 TRTLQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQpSR 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVR 299
Cdd:cd06643   234 WSPEFKDFLRKCLEKNVDARWTTSQLLQHPFVSVLVSNKPLR 275
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
20-308 5.07e-74

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: 247.66  E-value: 5.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE--EIKQEINMLKKySHHRNIATYYGAFIKKSppgn 97
Cdd:cd06642     1 DPEELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEieDIQQEITVLSQ-CDSPYITRYYGSYLKGT---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 ddQLWLVMEFCGAGSVTDLVKNtkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd06642    76 --KLWIIMEYLGGGSALDLLKP---GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSkK 257
Cdd:cd06642   151 LTDTQIKRNTFVGTPFWMAPEVIK-----QSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEG-Q 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVRIQLKDHIDR 308
Cdd:cd06642   225 HSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFLTELIDRYKR 275
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
25-289 1.80e-72

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: 242.13  E-value: 1.80e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM---DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikKSPpgndDQL 101
Cdd:cd06627     2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQIsleKIPKSDLKSVMGEIDLLKKL-NHPNIVKYIGSV--KTK----DSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd06627    75 YIILEYVENGSLASIIK--KFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTFIGTPYWMAPEVIacDENPDATydyRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLkSKKWSKK 261
Cdd:cd06627   153 EKDENSVVGTPYWMAPEVI--EMSGVTT---ASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQDDHPPL-PENISPE 226
                         250       260
                  ....*....|....*....|....*...
gi 578829925  262 FIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06627   227 LRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
20-311 3.13e-72

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: 242.65  E-value: 3.13e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE--EIKQEINMLKKySHHRNIATYYGAFIKKSppgn 97
Cdd:cd06640     1 DPEELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEieDIQQEITVLSQ-CDSPYVTKYYGSYLKGT---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 ddQLWLVMEFCGAGSVTDLVKntkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd06640    76 --KLWIIMEYLGGGSALDLLR---AGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLkSKK 257
Cdd:cd06640   151 LTDTQIKRNTFVGTPFWMAPEVIQ-----QSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTL-VGD 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVriqLKDHIDRSRK 311
Cdd:cd06640   225 FSKPFKEFIDACLNKDPSFRPTAKELLKHKFIVKNAKKTSY---LTELIDRFKR 275
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
20-308 3.00e-71

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: 239.59  E-value: 3.00e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE--EIKQEINMLKKySHHRNIATYYGAFIKksppgn 97
Cdd:cd06641     1 DPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEieDIQQEITVLSQ-CDSPYVTKYYGSYLK------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 DDQLWLVMEFCGAGSVTDLVKNtkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd06641    74 DTKLWIIMEYLGGGSALDLLEP---GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSkK 257
Cdd:cd06641   151 LTDTQIKRN*FVGTPFWMAPEVIK-----QSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEG-N 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVRIQLKDHIDR 308
Cdd:cd06641   225 YSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKR 275
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
25-290 3.66e-68

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 230.17  E-value: 3.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKySHHRNIATYYGAFIKKSppgnddQLW 102
Cdd:cd06623     3 LERVKVLGQGSSGVVYKVRHKPTGKIYALKKihVDGDEEFRKQLLRELKTLRS-CESPYVVKCYGAFYKEG------EIS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHA-HKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd06623    76 IVLEYMDGGSLADLLKKVGK--IPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCD---MHPMRALFLIPRNPPPRLKSKKW 258
Cdd:cd06623   154 LDQCNTFVGTVTYMSPERIQGE-----SYSYAADIWSLGLTLLECALGKFPFLPpgqPSFFELMQAICDGPPPSLPAEEF 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  259 SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06623   229 SPEFRDFISACLQKDPKKRPSAAELLQHPFIK 260
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
20-290 1.04e-66

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 226.17  E-value: 1.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK-QEINMLKKYsHHRNIATYYGAFIKksppgnD 98
Cdd:cd06648     4 DPRSDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLfNEVVIMRDY-QHPNIVEMYSSYLV------G 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06648    77 DELWVVMEFLEGGALTDIVTHTR---MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLK-SKK 257
Cdd:cd06648   154 SKEVPRRKSLVGTPYWMAPEVIS-----RLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKnLHK 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06648   229 VSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
11-310 2.54e-66

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: 227.23  E-value: 2.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   11 DDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV----TEDEEEEIKQEINMLKKYSHHRNIAtYY 86
Cdd:cd06633     9 EIADLFYKDDPEEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYsgkqTNEKWQDIIKEVKFLQQLKHPNTIE-YK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   87 GAFIKksppgnDDQLWLVMEFCgAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE 166
Cdd:cd06633    88 GCYLK------DHTAWLVMEYC-LGSASDLLEVHK-KPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  167 VKLVDFGVSAqldrTVGRRNTFIGTPYWMAPEVI-ACDEnpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLI 245
Cdd:cd06633   160 VKLADFGSAS----IASPANSFVGTPYWMAPEVIlAMDE---GQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHI 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  246 PRNPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRdqpTERQVRIqLKDHIDRSR 310
Cdd:cd06633   233 AQNDSPTLQSNEWTDSFRGFVDYCLQKIPQERPSSAELLRHDFVR---RERPPRV-LIDLIQRTK 293
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
25-289 2.07e-64

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: 219.52  E-value: 2.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKySHHRNIATYYGAFIkksppgNDDQLW 102
Cdd:cd06605     3 LEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIrlEIDEALQKQILRELDVLHK-CNSPYIVGFYGAFY------SEGDIS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLH-AHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd06605    76 ICMEYMDGGSLDKILK--EVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGrrNTFIGTPYWMAPEVIacdeNPDaTYDYRSDIWSLGITAIEMAEG----APPLCD--MHPMRALFLIPRNPPPRLKS 255
Cdd:cd06605   154 LA--KTFVGTRSYMAPERI----SGG-KYTVKSDIWSLGLSLVELATGrfpyPPPNAKpsMMIFELLSYIVDEPPPLLPS 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  256 KKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06605   227 GKFSPDFQDFVSQCLQKDPTERPSYKELMEHPFI 260
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
20-290 3.20e-63

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: 216.33  E-value: 3.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE-IKQEINMLKKySHHRNIATYYGAFIKksppgnD 98
Cdd:cd06647     4 DPKKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKElIINEILVMRE-NKNPNIVNYLDSYLV------G 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTkgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06647    77 DELWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSK-K 257
Cdd:cd06647   154 TPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPeK 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06647   229 LSAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
25-289 1.08e-62

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: 214.25  E-value: 1.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE---EEIKQEINMLKKYsHHRNIATYYGAFIkksppgNDDQL 101
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEkerEEALNEVKLLSKL-KHPNIVKYYESFE------ENGKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNA--LKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd08215    75 CIVMEYADGGDLAQKIKKQKKKGqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFIGTPYWMAPEViaCDENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHpMRALFL-IPRNPPPRLkSKKW 258
Cdd:cd08215   155 STTDLAKTVVGTPYYLSPEL--CENKP---YNYKSDIWALGCVLYELCTLKHPFEANN-LPALVYkIVKGQYPPI-PSQY 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578829925  259 SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd08215   228 SSELRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
7-293 1.19e-62

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: 216.84  E-value: 1.19e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    7 ARSLDDIDLSAL---RDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE----IKQEINMLKKYSHH 79
Cdd:cd06635     6 AGSLKDPDIAELffkEDPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEkwqdIIKEVKFLQRIKHP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   80 RNIAtYYGAFIKksppgnDDQLWLVMEFCgAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNV 159
Cdd:cd06635    86 NSIE-YKGCYLR------EHTAWLVMEYC-LGSASDLLEVHK-KPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  160 LLTENAEVKLVDFGVSAqldrTVGRRNTFIGTPYWMAPEVI-ACDEnpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHP 238
Cdd:cd06635   157 LLTEPGQVKLADFGSAS----IASPANSFVGTPYWMAPEVIlAMDE---GQYDGKVDVWSLGITCIELAERKPPLFNMNA 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  239 MRALFLIPRNPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI-RDQP 293
Cdd:cd06635   230 MSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVlRERP 285
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
23-292 4.41e-59

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: 205.35  E-value: 4.41e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   23 GIFELvEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSppgnDDQ 100
Cdd:cd06621     2 KIVEL-SSLGEGAGGSVTKCRLRNTKTIFALKTIttDPNPDVQKQILRELEINKSC-ASPYIVKYYGAFLDEQ----DSS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTK--GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06621    76 IGIAMEYCEGGSLDSIYKKVKkkGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGEL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMA--------EGAPPLCdmhPMRALFLIPRNPP 250
Cdd:cd06621   156 VNSLA--GTFTGTSYYMAPERIQ-----GGPYSITSDVWSLGLTLLEVAqnrfpfppEGEPPLG---PIELLSYIVNMPN 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  251 PRLKSK-----KWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQ 292
Cdd:cd06621   226 PELKDEpengiKWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQ 272
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
20-293 8.48e-59

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: 205.26  E-value: 8.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE----IKQEINMLKKYsHHRNIATYYGAFIKkspp 95
Cdd:cd06634    12 DPEKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEkwqdIIKEVKFLQKL-RHPNTIEYRGCYLR---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 gnDDQLWLVMEFCgAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd06634    87 --EHTAWLVMEYC-LGSASDLLEVHK-KPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AqldrTVGRRNTFIGTPYWMAPEVI-ACDEnpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLK 254
Cdd:cd06634   163 S----IMAPANSFVGTPYWMAPEVIlAMDE---GQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQ 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578829925  255 SKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI-RDQP 293
Cdd:cd06634   236 SGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLlRERP 275
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
29-289 5.52e-56

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: 195.35  E-value: 5.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRhVKTGQLAAIKV-------MDVTEDEEEEIKQEINMLKKYSHHrNIATYYGAFIKksppgnDDQL 101
Cdd:cd06631     7 NVLGKGAYGTVYCGL-TSTGQLIAVKQveldtsdKEKAEKEYEKLQEEVDLLKTLKHV-NIVGYLGTCLE------DNVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--D 179
Cdd:cd06631    79 SIFMEFVPGGSIASILA--RFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLciN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFI----GTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLI--PRNPPPRL 253
Cdd:cd06631   157 LSSGSQSQLLksmrGTPYWMAPEVIN-----ETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIgsGRKPVPRL 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  254 kSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06631   232 -PDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
29-289 6.53e-56

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: 194.93  E-value: 6.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE------IKQEINMLKKYsHHRNIATYYGAfikkspPGNDDQLW 102
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSresvkqLEQEIALLSKL-RHPNIVQYYGT------EREEDNLY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDrTV 182
Cdd:cd06632    79 IFLEYVPGGSIHKLLQ--RYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVE-AF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIGTPYWMAPEVIAcdeNPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKF 262
Cdd:cd06632   156 SFAKSFKGSPYWMAPEVIM---QKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPPIPDHLSPDA 232
                         250       260
                  ....*....|....*....|....*..
gi 578829925  263 IDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06632   233 KDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
20-290 1.80e-55

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: 195.33  E-value: 1.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKksppgnDD 99
Cdd:cd06656    16 DPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV------GD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKNTkgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd06656    90 ELWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS-KKW 258
Cdd:cd06656   167 PEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNpERL 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  259 SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06656   242 SAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 273
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
20-290 5.42e-55

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: 193.79  E-value: 5.42e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKksppgnDD 99
Cdd:cd06654    17 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV------GD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKNTkgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd06654    91 ELWVVMEYLAGGSLTDVVTET---CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS-KKW 258
Cdd:cd06654   168 PEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNpEKL 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  259 SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06654   243 SAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 274
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
32-287 2.53e-54

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: 188.63  E-value: 2.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHVKTGQLAAIKVMDV--TEDEEEEIKQEINMLKKySHHRNIATYYGAFIKksppgnDDQLWLVMEFCG 109
Cdd:cd00180     2 GKGSFGKVYKARDKETGKKVAVKVIPKekLKKLLEELLREIEILKK-LNHPNIVKLYDVFET------ENFLYLVMEYCE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  110 AGSVTDLVKNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFI 189
Cdd:cd00180    75 GGSLKDLLKENKGP-LSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  190 G--TPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEgapplcdmhpmralfliprnppprlkskkwskkFIDFID 267
Cdd:cd00180   154 GttPPYYAPPELLGGRY-----YGPKVDIWSLGVILYELEE---------------------------------LKDLIR 195
                         250       260
                  ....*....|....*....|
gi 578829925  268 TCLIKTYLSRPPTEQLLKFP 287
Cdd:cd00180   196 RMLQYDPKKRPSAKELLEHL 215
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
25-270 1.38e-53

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: 188.18  E-value: 1.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK----QEINMLKKYSHhRNIATYYGAFIkksppgNDDQ 100
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRerflREARALARLSH-PNIVRVYDVGE------DDGR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd14014    75 PYIVMEYVEGGSLADLLR--ERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRR-NTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS--KK 257
Cdd:cd14014   153 SGLTQtGSVLGTPAYMAPEQAR-----GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPlnPD 227
                         250
                  ....*....|...
gi 578829925  258 WSKKFIDFIDTCL 270
Cdd:cd14014   228 VPPALDAIILRAL 240
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
20-289 3.91e-53

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: 188.66  E-value: 3.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK-QEINMLKKYSHHRNIATYYGAFIkksppgnD 98
Cdd:cd06659    18 DPRQLLENYVKIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLfNEVVIMRDYQHPNVVEMYKSYLV-------G 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06659    91 EELWVLMEYLQGGALTDIVSQTR---LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLK-SKK 257
Cdd:cd06659   168 SKDVPKRKSLVGTPYWMAPEVIS-----RCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKnSHK 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06659   243 ASPVLRDFLERMLVRDPQERATAQELLDHPFL 274
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
17-290 4.52e-53

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: 188.39  E-value: 4.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   17 ALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE-IKQEINMLKKYSHhRNIATYYGAFIKkspp 95
Cdd:cd06655    13 SIGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKElIINEILVMKELKN-PNIVNFLDSFLV---- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 gnDDQLWLVMEFCGAGSVTDLVKNTkgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd06655    88 --GDELFVVMEYLAGGSLTDVVTET---CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS 255
Cdd:cd06655   163 AQITPEQSKRSTMVGTPYWMAPEVVT-----RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQN 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  256 -KKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06655   238 pEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
30-289 5.98e-53

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: 186.41  E-value: 5.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMDV------TEDEEEEIKQEINMLKKYSHHRnIATYYGAfikksppGNDDQ-LW 102
Cdd:cd06625     7 LLGQGAFGQVYLCYDADTGRELAVKQVEIdpinteASKEVKALECEIQLLKNLQHER-IVQYYGC-------LQDEKsLS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD--R 180
Cdd:cd06625    79 IFMEYMPGGSVKDEIKAY--GALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQtiC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPP-PRLKSKKwS 259
Cdd:cd06625   157 SSTGMKSVTGTPYWMSPEVINGE-----GYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTnPQLPPHV-S 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06625   231 EDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
22-280 7.09e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.61  E-value: 7.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   22 AGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEI----KQEINMLKKySHHRNIATYYGAFIkksppgN 97
Cdd:COG0515     6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEArerfRREARALAR-LNHPNIVRVYDVGE------E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 DDQLWLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:COG0515    79 DGRPYLVMEYVEGESLADLLR--RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRT-VGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSK 256
Cdd:COG0515   157 LGGAtLTQTGTVVGTPGYMAPEQARGEP-----VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSEL 231
                         250       260
                  ....*....|....*....|....*.
gi 578829925  257 KW--SKKFIDFIDTCLIKTYLSRPPT 280
Cdd:COG0515   232 RPdlPPALDAIVLRALAKDPEERYQS 257
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
25-289 8.37e-51

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: 181.08  E-value: 8.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSppgnddQLW 102
Cdd:cd06617     3 LEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIraTVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREG------DVW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAgSVTDLVKNT--KGNALKEDCIAYICREILRGLAHLHAH-KVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd06617    77 ICMEVMDT-SLDKFYKKVydKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFIGTPYwMAPEVIACDENPDAtYDYRSDIWSLGITAIEMAEGAPPLCDMH-PMRALFLIPRNPPPRLKSKKW 258
Cdd:cd06617   156 DSVAKTIDAGCKPY-MAPERINPELNQKG-YDVKSDVWSLGITMIELATGRFPYDSWKtPFQQLKQVVEEPSPQLPAEKF 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578829925  259 SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06617   234 SPEFQDFVNKCLKKNYKERPNYPELLQHPFF 264
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
25-288 2.89e-50

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: 178.82  E-value: 2.89e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTEDEEEEIKQEINMLKKYSHHrNIATYYGAFIkksppgNDDQL 101
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDkkkLKSEDEEMLRREIEILKRLDHP-NIVKLYEVFE------DDKNL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTD-LVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVSAQ 177
Cdd:cd05117    75 YLVMELCTGGELFDrIVKKGS---FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdPDSPIKIIDFGLAKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTvGRRNTFIGTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIpRNPPPRLKSKK 257
Cdd:cd05117   152 FEEG-EKLKTVCGTPYYVAPEVLKG-----KGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKI-LKGKYSFDSPE 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  258 W---SKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd05117   225 WknvSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
25-290 2.00e-49

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: 176.13  E-value: 2.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINmLKKYSHHRNIATYYGAFIkksppgNDDQ 100
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISksqlQKSGLEHQLRREIE-IQSHLRHPNILRLYGYFE------DKKR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSV-TDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd14007    75 IYLILEYAPNGELyKELKKQKR---FDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RtvGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIpRNPPPRLKSkKWS 259
Cdd:cd14007   152 S--NRRKTFCGTLDYLPPEMVEGKE-----YDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRI-QNVDIKFPS-SVS 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd14007   223 PEAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
25-287 5.45e-49

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 174.91  E-value: 5.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEIN---MLKKYSHhRNIATYYGAFIKKSppgnddQL 101
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDearVLSKLNS-PYVIKYYDSFVDKG------KL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd08529    75 NIVMEYAENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTFIGTPYWMAPEViaCDENPdatYDYRSDIWSLGITAIEMAEGAPPLcDMHPMRALFL-IPRNPPPRLkSKKWSK 260
Cdd:cd08529   155 TNFAQTIVGTPYYLSPEL--CEDKP---YNEKSDVWALGCVLYELCTGKHPF-EAQNQGALILkIVRGKYPPI-SASYSQ 227
                         250       260
                  ....*....|....*....|....*..
gi 578829925  261 KFIDFIDTCLIKTYLSRPPTEQLLKFP 287
Cdd:cd08529   228 DLSQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
31-290 1.03e-48

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: 175.61  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK-QEINMLKKYsHHRNIATYYGAFIKksppgnDDQLWLVMEFCG 109
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLfNEVVIMRDY-HHENVVDMYNSYLV------GDELWVVMEFLE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  110 AGSVTDLVKNTKGNalkEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFI 189
Cdd:cd06658   103 GGALTDIVTHTRMN---EEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  190 GTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLK-SKKWSKKFIDFIDT 268
Cdd:cd06658   180 GTPYWMAPEVIS-----RLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKdSHKVSSVLRGFLDL 254
                         250       260
                  ....*....|....*....|..
gi 578829925  269 CLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06658   255 MLVREPSQRATAQELLQHPFLK 276
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
20-289 1.20e-48

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: 175.21  E-value: 1.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK-QEINMLKKYsHHRNIATYYGAFIKksppgnD 98
Cdd:cd06657    17 DPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDY-QHENVVEMYNSYLV------G 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTKGNalkEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06657    90 DELWVVMEFLEGGALTDIVTHTRMN---EEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS-KK 257
Cdd:cd06657   167 SKEVPRRKSLVGTPYWMAPELIS-----RLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNlHK 241
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06657   242 VSPSLKGFLDRLLVRDPAQRATAAELLKHPFL 273
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
25-289 1.36e-48

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: 174.27  E-value: 1.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ---EINMLKKYsHHRNIATYYGAFIKKSppgnDDQL 101
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQlvsEVNILREL-KHPNIVRYYDRIVDRA----NTTL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTK--GNALKEDCIAYICREILRGLAHLHA-----HKVIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd08217    77 YIVMEYCEGGDLAQLIKKCKkeNQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFLDSDNNVKLGDFGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  175 SAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLcDMHPMRALF-LIPRNPPPRL 253
Cdd:cd08217   157 ARVLSHDSSFAKTYVGTPYYMSPELLN-----EQSYDEKSDIWSLGCLIYELCALHPPF-QAANQLELAkKIKEGKFPRI 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  254 KSkKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd08217   231 PS-RYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
25-288 1.80e-48

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: 173.47  E-value: 1.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSppgnddQL 101
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDkskLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETEN------KI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNtkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLdRT 181
Cdd:cd14003    75 YLVMEYASGGELFDYIVN--NGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEF-RG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTFIGTPYWMAPEVIACDEnpdatYDYR-SDIWSLGITAIEMAEGAPPLcDMHPMRALF-LIPR---NPPPRLksk 256
Cdd:cd14003   152 GSLLKTFCGTPAYAAPEVLLGRK-----YDGPkADVWSLGVILYAMLTGYLPF-DDDNDSKLFrKILKgkyPIPSHL--- 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  257 kwSKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14003   223 --SPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
31-289 2.81e-48

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: 173.26  E-value: 2.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVM---DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKsppgndDQLWLVMEF 107
Cdd:cd06626     8 IGEGTFGKVYTAVNLDTGELMAMKEIrfqDNDPKTIKEIADEMKVLEGL-DHPNLVRYYGVEVHR------EEVYIFMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNtkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV----- 182
Cdd:cd06626    81 CQEGTLEELLRH--GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTttmap 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIGTPYWMAPEVIAcdENPDATYDYRSDIWSLGITAIEMAEGAPPLCDM-HPMRALFLI-PRNPPPRLKSKKWSK 260
Cdd:cd06626   159 GEVNSLVGTPAYMAPEVIT--GNKGEGHGRAADIWSLGCVVLEMATGKRPWSELdNEWAIMYHVgMGHKPPIPDSLQLSP 236
                         250       260
                  ....*....|....*....|....*....
gi 578829925  261 KFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06626   237 EGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
31-285 4.15e-48

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: 171.95  E-value: 4.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVktGQLAAIKVMDVTEDEEEEIK---QEINMLKKySHHRNIATYYGAFIKKSPpgnddqLWLVMEF 107
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKefrREVSILSK-LRHPNIVQFIGACLSPPP------LCIVTEY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKGN-----ALKedciayICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd13999    72 MPGGSLYDLLHKKKIPlswslRLK------IALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTT 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKF 262
Cdd:cd13999   146 EKMTGVVGTPRWMAPEVLRGEP-----YTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIPPDCPPEL 220
                         250       260
                  ....*....|....*....|...
gi 578829925  263 IDFIDTCLIKTYLSRPPTEQLLK 285
Cdd:cd13999   221 SKLIKRCWNEDPEKRPSFSEIVK 243
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
10-301 1.64e-47

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: 171.85  E-value: 1.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   10 LDDIDLSALRDpagifelvevVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKySHHRNIATYYG 87
Cdd:cd06620     2 LKNQDLETLKD----------LGAGNGGSVSKVLHIPTGTIMAKKVIhiDAKSSVRKQILRELQILHE-CHSPYIVSFYG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   88 AFIKKSPpgnddQLWLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLH-AHKVIHRDIKGQNVLLTENAE 166
Cdd:cd06620    71 AFLNENN-----NIIICMEYMDCGSLDKILK--KKGPFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSKGQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  167 VKLVDFGVSAQLDRTVGrrNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCD--------MHP 238
Cdd:cd06620   144 IKLCDFGVSGELINSIA--DTFVGTSTYMSPERIQGGK-----YSVKSDVWSLGLSIIELALGEFPFAGsnddddgyNGP 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  239 MRALFLIPR---NPPPRL-KSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVRIQ 301
Cdd:cd06620   217 MGILDLLQRivnEPPPRLpKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRASDVDLR 283
Pkinase pfam00069
Protein kinase domain;
25-289 1.54e-44

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 160.87  E-value: 1.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ---EINMLKKYShHRNIATYYGAFIkksppgNDDQL 101
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNilrEIKILKKLN-HPNIVRLYDAFE------DKDNL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   102 WLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLhahkvihrdikgqnvlltenaevklvdfgvsaqldrt 181
Cdd:pfam00069   74 YLVLEYVEGGSLFDLLSEKG--AFSEREAKFIMKQILEGLESG------------------------------------- 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   182 vGRRNTFIGTPYWMAPEVIacDENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNP-PPRLKSKKWSK 260
Cdd:pfam00069  115 -SSLTTFVGTPWYMAPEVL--GGNP---YGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPyAFPELPSNLSE 188
                          250       260
                   ....*....|....*....|....*....
gi 578829925   261 KFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:pfam00069  189 EAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
32-289 2.78e-44

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: 161.95  E-value: 2.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHVKTGQLAAIKVMD---------------VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikKSPPG 96
Cdd:cd14008     2 GRGSFGKVKLALDTETGQLYAIKIFNksrlrkrregkndrgKIKNALDDVRREIAIMKKL-DHPNIVRLYEVI--DDPES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 ndDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA 176
Cdd:cd14008    79 --DKLYLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  177 QLDRTVGRRNTFIGTPYWMAPEviACDENpDATYDYR-SDIWSLGITAIEMAEGAPP--------LCDMhpmralflIPR 247
Cdd:cd14008   157 MFEDGNDTLQKTAGTPAFLAPE--LCDGD-SKTYSGKaADIWALGVTLYCLVFGRLPfngdnileLYEA--------IQN 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578829925  248 NPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14008   226 QNDEFPIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
30-289 3.55e-44

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: 161.55  E-value: 3.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE----------IKQEINMLKKYsHHRNIATYYGAFIkksppgNDD 99
Cdd:cd06628     7 LIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENkdrkksmldaLQREIALLREL-QHENIVQYLGSSS------DAN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd06628    80 HLNIFLEYVPGGSVATLLNNY--GAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTV------GRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRL 253
Cdd:cd06628   158 ANSlstknnGARPSLQGSVFWMAPEVVK-----QTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTI 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  254 KSKKwSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06628   233 PSNI-SSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
25-287 5.74e-44

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 160.63  E-value: 5.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ---EINMLKKYSHHrNIATYYGAFIkksppgNDDQL 101
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDsvnEIRLLASVNHP-NIIRYKEAFL------DGNRL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTK--GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd08530    75 CIVMEYAPFGDLSKLISKRKkkRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRrnTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLC--DMHPMRALFLIPRNPPPrlkSKK 257
Cdd:cd08530   155 KNLAK--TQIGTPLYAAPEVWK-----GRPYDYKSDIWSLGCLLYEMATFRPPFEarTMQELRYKVCRGKFPPI---PPV 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLLKFP 287
Cdd:cd08530   225 YSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
30-289 6.90e-44

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: 160.65  E-value: 6.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKksppgnDDQLWLVMEFCG 109
Cdd:cd06624    15 VLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSE------DGFFKIFMEQVP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  110 AGSVTDLVKNTKGNAL-KEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL-TENAEVKLVDFGVSAQLDRTVGRRNT 187
Cdd:cd06624    89 GGSLSALLRSKWGPLKdNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSKRLAGINPCTET 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  188 FIGTPYWMAPEVIacDENPDAtYDYRSDIWSLGITAIEMAEGAPPLCDM-HPMRALFLI------PRNPpprlksKKWSK 260
Cdd:cd06624   169 FTGTLQYMAPEVI--DKGQRG-YGPPADIWSLGCTIIEMATGKPPFIELgEPQAAMFKVgmfkihPEIP------ESLSE 239
                         250       260
                  ....*....|....*....|....*....
gi 578829925  261 KFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06624   240 EAKSFILRCFEPDPDKRATASDLLQDPFL 268
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
25-308 3.20e-43

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: 159.85  E-value: 3.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE--IKQEINMLKKYSHHRNIATYYGAFIKKSppgnddQLW 102
Cdd:cd06618    17 LENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENkrILMDLDVVLKSHDCPYIVKCYGYFITDS------DVF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEfCGAGSVTDLVKNTKGnALKEDCIAYICREILRGLAHL-HAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd06618    91 ICME-LMSTCLDKLLKRIQG-PIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRLVDS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTfIGTPYWMAPEVIACDENPDatYDYRSDIWSLGITAIEMAEGAPP--LCDMHpMRALFLIPRNPPPRLKSKK-W 258
Cdd:cd06618   169 KAKTRS-AGCAAYMAPERIDPPDNPK--YDIRADVWSLGISLVELATGQFPyrNCKTE-FEVLTKILNEEPPSLPPNEgF 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  259 SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRD-QPTERQVRIQLKDHIDR 308
Cdd:cd06618   245 SPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRyETAEVDVASWFQDVMAE 295
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
31-288 1.96e-42

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: 155.75  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIkksppgNDDQLWLVME 106
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRkkeiIKRKEVEHTLNERNILERVNH-PFIVKLHYAFQ------TEEKLYLVLD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRN 186
Cdd:cd05123    74 YVPGGELFSHLS--KEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  187 TFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDmHPMRALF-LIPRNPP--PRlkskKWSKKFI 263
Cdd:cd05123   152 TFCGTPEYLAPEVLL-----GKGYGKAVDWWSLGVLLYEMLTGKPPFYA-ENRKEIYeKILKSPLkfPE----YVSPEAK 221
                         250       260
                  ....*....|....*....|....*...
gi 578829925  264 DFIDTCLIK---TYLSRPPTEQLLKFPF 288
Cdd:cd05123   222 SLISGLLQKdptKRLGSGGAEEIKAHPF 249
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
25-289 2.12e-42

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: 155.87  E-value: 2.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV---TEDEEEEIKQEINMLKKYsHHRNIATYYGAFikksppGNDDQL 101
Cdd:cd14002     3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKrgkSEKELRNLRQEIEILRKL-NHPNIIEMLDSF------ETKKEF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFcGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDrt 181
Cdd:cd14002    76 VVVTEY-AQGELFQILEDDG--TLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMS-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 vgrRNTFI-----GTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPpprlksK 256
Cdd:cd14002   151 ---CNTLVltsikGTPLYMAPELVQ--EQP---YDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDP------V 216
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578829925  257 KW----SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14002   217 KWpsnmSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
31-291 2.34e-42

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: 157.14  E-value: 2.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHHRNIATYYGAFIkksppgNDDQLWLVMEFC 108
Cdd:cd06616    14 IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRllMDLDVVMRSSDCPYIVKFYGALF------REGDCWICMELM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAgSVTDLVK----NTKGNaLKEDCIAYICREILRGLAHL-HAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVG 183
Cdd:cd06616    88 DI-SLDKFYKyvyeVLDSV-IPEEILGKIAVATVKALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVDSIA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  184 RRNTFIGTPYwMAPEVIACDENPDAtYDYRSDIWSLGITAIEMAEGAPPLCD-MHPMRALFLIPRNPPPRLKS---KKWS 259
Cdd:cd06616   166 KTRDAGCRPY-MAPERIDPSASRDG-YDVRSDVWSLGITLYEVATGKFPYPKwNSVFDQLTQVVKGDPPILSNseeREFS 243
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRD 291
Cdd:cd06616   244 PSFVNFVNLCLIKDESKRPKYKELLKHPFIKM 275
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
25-289 5.14e-41

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: 151.62  E-value: 5.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLK---KYSHHRNIATYYGAFikKSPPGNDdqL 101
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKhlnDVEGHPNIVKLLDVF--EHRGGNH--L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAgSVTDLVKNTkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT-ENAEVKLVDFGVSAQLDR 180
Cdd:cd05118    77 CLVFELMGM-NLYELIKDY-PRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARSFTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGrrNTFIGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRnppprlksKKWSK 260
Cdd:cd05118   155 PPY--TPYVATRWYRAPEVL----LGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVR--------LLGTP 220
                         250       260
                  ....*....|....*....|....*....
gi 578829925  261 KFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd05118   221 EALDLLSKMLKYDPAKRITASQALAHPYF 249
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
25-251 8.24e-41

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: 151.50  E-value: 8.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    25 FELVEVVGNGTYGQVYKGR----HVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYSHHrNIATYYGAFIKKSPpgnd 98
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTLkeGADEEEREDFLEEASIMKKLDHP-NIVKLLGVCTQGEP---- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    99 dqLWLVMEFCGAGSVTDLVKNtKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:pfam07714   76 --LYIVTEYMPGGDLLDFLRK-HKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDI 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925   179 DRTVGRRNTFIG-TPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAE-GAPPLCDMHPMRALFLI---PRNPPP 251
Cdd:pfam07714  153 YDDDYYRKRGGGkLPIkWMAPESLK-----DGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLedgYRLPQP 226
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
25-289 2.26e-40

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: 150.40  E-value: 2.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEInMLKKYSHHRNIATYYGAFikksppGNDDQ 100
Cdd:cd14099     3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPksslTKPKQREKLKSEI-KIHRSLKHPNIVKFHDCF------EDEEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd14099    76 VYILLELCSNGSLMELLKRRK--ALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAPP--------------LCDmhpmralFLIP 246
Cdd:cd14099   154 DGERKKTLCGTPNYIAPEVLEKKKG----HSFEVDIWSLGVILYTLLVGKPPfetsdvketykrikKNE-------YSFP 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578829925  247 RNPPprlkskkWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14099   223 SHLS-------ISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
29-289 2.35e-40

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: 150.61  E-value: 2.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE-----------IKQEINMLKKYSHhRNIATYYGaFIKKsppgn 97
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRadsrqktvvdaLKSEIDTLKDLDH-PNIVQYLG-FEET----- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 DDQLWLVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd06629    80 EDYFSIFLEYVPGGSIGSCLRKYGK--FEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRR--NTFIGTPYWMAPEVIacdENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLI--PRNPPPRL 253
Cdd:cd06629   158 SDDIYGNNgaTSMQGSVFWMAPEVI---HSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgnKRSAPPVP 234
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  254 KSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd06629   235 EDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
25-290 5.34e-40

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: 151.05  E-value: 5.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKK-YSHHrnIATYYGAFIkksppgNDDQL 101
Cdd:cd06615     3 FEKLGELGAGNGGVVTKVLHRPSGLIMARKLihLEIKPAIRNQIIRELKVLHEcNSPY--IVGFYGAFY------SDGEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLH-AHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd06615    75 SICMEHMDGGSLDQVLK--KAGRIPENILGKISIAVLRGLTYLReKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEG---APP-----LCDMH--------------- 237
Cdd:cd06615   153 SMA--NSFVGTRSYMSPERLQ-----GTHYTVQSDIWSLGLSLVEMAIGrypIPPpdakeLEAMFgrpvsegeakeshrp 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  238 ----------PMrALF----LIPRNPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06615   226 vsghppdsprPM-AIFelldYIVNEPPPKLPSGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
29-290 8.62e-40

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: 149.26  E-value: 8.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKYSHHRnIATYYGAFIKksppgnDDQLWLVME 106
Cdd:cd06619     7 EILGHGNGGTVYKAYHLLTRRILAVKVipLDITVELQKQIMSELEILYKCDSPY-IIGFYGAFFV------ENRISICTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVtDLVKNtkgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRrn 186
Cdd:cd06619    80 FMDGGSL-DVYRK-----IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAK-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  187 TFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPL-------CDMHPMRALFLIPRNPPPRLKSKKWS 259
Cdd:cd06619   152 TYVGTNAYMAPERISGEQ-----YGIHSDVWSLGISFMELALGRFPYpqiqknqGSLMPLQLLQCIVDEDPPVLPVGQFS 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06619   227 EKFVHFITQCMRKQPKERPAPENLMDHPFIV 257
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
25-289 5.75e-39

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: 146.34  E-value: 5.75e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV------TEDEEEEIKQEINMLKKYSHHRnIATYYGaFIKKSPpgnD 98
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFdpespeTSKEVNALECEIQLLKNLLHER-IVQYYG-CLRDPQ---E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06652    79 RTLSIFMEYMPGGSIKDQLKSY--GALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 dRTVGRRNTFI----GTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLI---PRNP-- 249
Cdd:cd06652   157 -QTICLSGTGMksvtGTPYWMSPEVISGE-----GYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIatqPTNPql 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578829925  250 PPRLkskkwSKKFIDFIDTCLIKTYLsRPPTEQLLKFPFI 289
Cdd:cd06652   231 PAHV-----SDHCRDFLKRIFVEAKL-RPSADELLRHTFV 264
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
26-308 1.48e-38

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: 146.15  E-value: 1.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKySHHRNIATYYGAFIKKSppgnddQLWL 103
Cdd:cd06622     4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEirLELDESKFNQIIMELDILHK-AVSPYIVDFYGAFFIEG------AVYM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKGNALK-EDCIAYICREILRGLAHL-HAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd06622    77 CMEYMDAGSLDKLYAGGVATEGIpEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNtfIGTPYWMAPEVIAcDENPDA--TYDYRSDIWSLGITAIEMAEGA---PPLCDMHPMRALFLIPRNPPPRLKSk 256
Cdd:cd06622   157 LAKTN--IGCQSYMAPERIK-SGGPNQnpTYTVQSDVWSLGLSILEMALGRypyPPETYANIFAQLSAIVDGDPPTLPS- 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578829925  257 KWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI-RDQPTERQVRIQLKDHIDR 308
Cdd:cd06622   233 GYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLvKYKNADVDMAEWVTGALKR 285
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
30-286 1.48e-38

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: 145.55  E-value: 1.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE-EEIKQEINMLKKYSHHRNIATYYGAFIKKSPPGNddQLWLVMEFC 108
Cdd:cd13985     7 QLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQlRVAIKEIEIMKRLCGHPNIVQYYDSAILSSEGRK--EVLLLMEYC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GaGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLTENAEVKLVDFGvSA-----QLDRT 181
Cdd:cd13985    85 P-GSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG-SAttehyPLERA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VG--------RRNTfigTPYWMAPEVIacDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRAL---FLIPRNPp 250
Cdd:cd13985   163 EEvniieeeiQKNT---TPMYRAPEMI--DLYSKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVagkYSIPEQP- 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  251 prlkskKWSKKFIDFIDTCLIKTYLSRPPTEQLLKF 286
Cdd:cd13985   237 ------RYSPELHDLIRHMLTPDPAERPDIFQVINI 266
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
31-283 2.50e-38

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: 144.29  E-value: 2.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDV---TEDEEEEIKQEINMLKKYsHHRNIATYYGafIKKSPpgndDQLWLVMEF 107
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRkklNKKLQENLESEIAILKSI-KHPNIVRLYD--VQKTE----DFIYLVLEY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVSAQLDrTVGR 184
Cdd:cd14009    74 CAGGDLSQYIRKRGR--LPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLStsgDDPVLKIADFGFARSLQ-PASM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  185 RNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPL-CDMHP------MRALFLIPRNPPPRLKSkk 257
Cdd:cd14009   151 AETLCGSPLYMAPEILQFQK-----YDAKADLWSVGAILFEMLVGKPPFrGSNHVqllrniERSDAVIPFPIAAQLSP-- 223
                         250       260
                  ....*....|....*....|....*.
gi 578829925  258 wskkfiDFIDtcLIKTYLSRPPTEQL 283
Cdd:cd14009   224 ------DCKD--LLRRLLRRDPAERI 241
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
26-286 1.66e-37

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: 141.92  E-value: 1.66e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925     26 ELVEVVGNGTYGQVYKGR----HVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSPpgndd 99
Cdd:smart00221    2 TLGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLkeDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEP----- 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    100 qLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS---- 175
Cdd:smart00221   76 -LMIVMEYMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSrdly 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    176 -AQLDRTVGRRntfigTPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAE-GAPPLCDMHPMRALFLIP---RNP 249
Cdd:smart00221  155 dDDYYKVKGGK-----LPIrWMAPESLK-----EGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKkgyRLP 224
                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 578829925    250 PPRLKskkwSKKFIDFIDTCLIKTYLSRPPTEQLLKF 286
Cdd:smart00221  225 KPPNC----PPELYKLMLQCWAEDPEDRPTFSELVEI 257
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
32-304 1.92e-37

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 143.59  E-value: 1.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKgrHVKTGQLAAIKVMDVTEDEEEEIK---QEINMLKKYSHhRNIATYYGAFIkksppgNDDQLWLVMEFC 108
Cdd:cd08216    11 KGGGVVHLAK--HKPTNTLVAVKKINLESDSKEDLKflqQEILTSRQLQH-PNILPYVTSFV------VDNDLYVVTPLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTvGRRNTF 188
Cdd:cd08216    82 AYGSCRDLLKTHFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKH-GKRQRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  189 IGTP--------YWMAPEVIACDEnpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRL------- 253
Cdd:cd08216   161 VHDFpksseknlPWLSPEVLQQNL---LGYNEKSDIYSVGITACELANGVVPFSDMPATQMLLEKVRGTTPQLldcstyp 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  254 --------------------------KSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRdQPTERQVRI--QLKD 304
Cdd:cd08216   238 leedsmsqsedsstehpnnrdtrdipYQRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFK-QCRRSNTSLldLLKP 315
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
25-289 3.58e-37

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: 141.32  E-value: 3.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV------TEDEEEEIKQEINMLKKYSHHRnIATYYGAFikKSPpgND 98
Cdd:cd06653     4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFdpdsqeTSKEVNALECEIQLLKNLRHDR-IVQYYGCL--RDP--EE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06653    79 KKLSIFVEYMPGGSVKDQLKAY--GALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 dRTVGRRNTFI----GTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPP-PRL 253
Cdd:cd06653   157 -QTICMSGTGIksvtGTPYWMSPEVISGE-----GYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTkPQL 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  254 KSKKwSKKFIDFIDTCLIKTYLsRPPTEQLLKFPFI 289
Cdd:cd06653   231 PDGV-SDACRDFLRQIFVEEKR-RPTAEFLLRHPFV 264
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
25-286 7.54e-37

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: 140.10  E-value: 7.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYSHHrNIATYYGAFIKksppgnDDQ 100
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQdclkEIDLLQQLNHP-NIIKYLASFIE------NNE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTK--GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd08224    75 LNIVLELADAGDLSRLIKHFKkqKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIacDENPdatYDYRSDIWSLGITAIEMAEGAPPLC-DMHPMRALF-LIPRNPPPRLKSK 256
Cdd:cd08224   155 SSKTTAAHSLVGTPYYMSPERI--REQG---YDFKSDIWSLGCLLYEMAALQSPFYgEKMNLYSLCkKIEKCEYPPLPAD 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 578829925  257 KWSKKFIDFIDTCLIKTYLSRPPTEQLLKF 286
Cdd:cd08224   230 LYSQELRDLVAACIQPDPEKRPDISYVLDV 259
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
26-286 1.72e-36

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 138.82  E-value: 1.72e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925     26 ELVEVVGNGTYGQVYKGR----HVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSPpgndd 99
Cdd:smart00219    2 TLGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLkeDASEQQIEEFLREARIMRKL-DHPNVVKLLGVCTEEEP----- 75
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    100 qLWLVMEFCGAGSVTDLVKNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS---- 175
Cdd:smart00219   76 -LYIVMEYMEGGDLLSYLRKNRPK-LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSrdly 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    176 -AQLDRTVGRRntfigTPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAE-GAPPLCDMHPMRALFLIP---RNP 249
Cdd:smart00219  154 dDDYYRKRGGK-----LPIrWMAPESLK-----EGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKngyRLP 223
                           250       260       270
                    ....*....|....*....|....*....|....*..
gi 578829925    250 PPRLKskkwSKKFIDFIDTCLIKTYLSRPPTEQLLKF 286
Cdd:smart00219  224 QPPNC----PPELYDLMLQCWAEDPEDRPTFSELVEI 256
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
25-288 1.93e-36

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: 139.76  E-value: 1.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM---DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKsppgndDQL 101
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFkesEDDEDVKKTALREVKVLRQL-RHENIVNLKEAFRRK------GRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd07833    76 YLVFEYVERTLLELLEASPGG--LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNT-FIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAPPL---CDM----HPMRALF-LIPRN---- 248
Cdd:cd07833   154 PASPLTdYVATRWYRAPELLVGDTN----YGKPVDVWAIGCIMAELLDGEPLFpgdSDIdqlyLIQKCLGpLPPSHqelf 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  249 -----------PPP-------RLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd07833   230 ssnprfagvafPEPsqpesleRRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
25-236 2.91e-36

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: 138.89  E-value: 2.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEINMLKK------------YSHHRNIATYYGAFikk 92
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLD---------KRHIIKEKKvkyvtiekevlsRLAHPGIVKLYYTF--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 sppGNDDQLWLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 172
Cdd:cd05581    71 ---QDESKLYFVLEYAPNGDLLEYIR--KYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  173 GVSAQLDRT-----------------VGRRNTFIGTPYWMAPEVIacDENPdatYDYRSDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd05581   146 GTAKVLGPDsspestkgdadsqiaynQARAASFVGTAEYVSPELL--NEKP---AGKSSDLWALGCIIYQMLTGKPPFRG 220

                  .
gi 578829925  236 M 236
Cdd:cd05581   221 S 221
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
25-289 4.90e-36

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: 137.57  E-value: 4.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK---QEINMLKKYSHhRNIATYygafiKKSPPGNDDQL 101
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKaaeQEAKLLSKLKH-PNIVSY-----KESFEGEDGFL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd08223    76 YIVMGFCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMA--EGAPPLCDMHPMRALFLIPRNPPprlKSKKWS 259
Cdd:cd08223   156 SDMATTLIGTPYYMSPELFS-----NKPYNHKSDVWALGCCVYEMAtlKHAFNAKDMNSLVYKILEGKLPP---MPKQYS 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd08223   228 PELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
29-289 2.09e-35

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: 135.82  E-value: 2.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAA---IKVMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSppgnDDQLWLVM 105
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEGIEVAwneIKLRKLPKAERQRFKQEIEILKSL-KHPNIIKFYDSWESKS----KKEVIFIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLTENA-EVKLVDFGVSAQLDrtV 182
Cdd:cd13983    82 ELMTSGTLKQYLKRFK--RLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTgEVKIGDLGLATLLR--Q 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIGTPYWMAPEVIacDENpdatYDYRSDIWSLGITAIEMAEGAPPLCD-MHPMRALFLIPRNPPPRLKSKKWSKK 261
Cdd:cd13983   158 SFAKSVIGTPEFMAPEMY--EEH----YDEKVDIYAFGMCLLEMATGEYPYSEcTNAAQIYKKVTSGIKPESLSKVKDPE 231
                         250       260
                  ....*....|....*....|....*...
gi 578829925  262 FIDFIDTClIKTYLSRPPTEQLLKFPFI 289
Cdd:cd13983   232 LKDFIEKC-LKPPDERPSARELLEHPFF 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
25-288 5.24e-35

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: 134.91  E-value: 5.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD-----VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikksppGNDD 99
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVkrkvaGNDKNLQLFQREINILKSL-EHPGIVRLIDWY------EDDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE--VKLVDFGVsAQ 177
Cdd:cd14098    75 HIYLVMEYVEGGDLMDFI--MAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGL-AK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVI-ACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRN--PPPRLK 254
Cdd:cd14098   152 VIHTGTFLVTFCGTMAYLAPEILmSKEQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGryTQPPLV 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  255 SKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14098   232 DFNISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
33-291 1.01e-34

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: 134.27  E-value: 1.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   33 NGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYgAFIkksppgNDDQLWLVMEFC 108
Cdd:cd05579     3 RGAYGRVYLAKKKSTGDLYAIKVIKkrdmIRKNQVDSVLAERNILSQAQNPFVVKLYY-SFQ------GKKNLYLVMEYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS------------- 175
Cdd:cd05579    76 PGGDLYSLLENV--GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSkvglvrrqiklsi 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 --AQLDRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMrALF---LIPRNPP 250
Cdd:cd05579   154 qkKSNGAPEKEDRRIVGTPDYLAPEILLGQG-----HGKTVDWWSLGVILYEFLVGIPPFHAETPE-EIFqniLNGKIEW 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578829925  251 PRLKSKkwSKKFIDFIDTCLIKTYLSRP---PTEQLLKFPFIRD 291
Cdd:cd05579   228 PEDPEV--SDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFKG 269
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
25-288 1.30e-34

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: 133.96  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtEDEEEEIKQEINMLKKYsHHRNIATYYgAFIKKSppgndDQLWLV 104
Cdd:cd14010     2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVD--KSKRPEVLNEVRLTHEL-KHPNVLKFY-EWYETS-----NHLWLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS--------- 175
Cdd:cd14010    73 VEYCTGGDLETLLRQDGN--LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeilke 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 -------AQLDRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPP--------LCDMhpmr 240
Cdd:cd14010   151 lfgqfsdEGNVNKVSKKQAKRGTPYYMAPELFQGGV-----HSFASDLWALGCVLYEMFTGKPPfvaesfteLVEK---- 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  241 alflIPRNPPPRLKSK---KWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14010   222 ----ILNEDPPPPPPKvssKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
29-236 1.46e-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: 1.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGR---HVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSPpgnddqLWL 103
Cdd:cd00192     1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLkeDASESERKDFLKEARVMKKL-GHPNVVRLLGVCTEEEP------LYL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGS-------VTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA 176
Cdd:cd00192    74 VMEYMEGGDlldflrkSRPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  177 QLDRTVGRRNTfIGTP---YWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAE-GAPPLCDM 236
Cdd:cd00192   154 DIYDDDYYRKK-TGGKlpiRWMAPESLK-----DGIFTSKSDVWSFGVLLWEIFTlGATPYPGL 211
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
28-289 2.03e-34

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 133.01  E-value: 2.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE---EEIKQEINMLKKYSHhRNIATYYGAFIKKsppGNddqLWLV 104
Cdd:cd08218     5 IKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPkerEESRKEVAVLSKMKH-PNIVQYQESFEEN---GN---LYIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGR 184
Cdd:cd08218    78 MDYCDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  185 RNTFIGTPYWMAPEViaCDENPdatYDYRSDIWSLGITAIEMAEGAPPLcDMHPMRALFL--IPRNPPPrlKSKKWSKKF 262
Cdd:cd08218   158 ARTCIGTPYYLSPEI--CENKP---YNNKSDIWALGCVLYEMCTLKHAF-EAGNMKNLVLkiIRGSYPP--VPSRYSYDL 229
                         250       260
                  ....*....|....*....|....*..
gi 578829925  263 IDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd08218   230 RSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
29-288 2.73e-34

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: 133.28  E-value: 2.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDV------TEDEEEEIKQEINMLKKYSHHRnIATYYGAFIKKSppgnDDQLW 102
Cdd:cd06651    13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFdpespeTSKEVSALECEIQLLKNLQHER-IVQYYGCLRDRA----EKTLT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLdRTV 182
Cdd:cd06651    88 IFMEYMPGGSVKDQLKAY--GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRL-QTI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFI----GTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLI---PRNPPPRLKS 255
Cdd:cd06651   165 CMSGTGIrsvtGTPYWMSPEVISGE-----GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatqPTNPQLPSHI 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578829925  256 KKWSKKFIdfidTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd06651   240 SEHARDFL----GCIFVEARHRPSAEELLRHPF 268
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
25-238 4.22e-34

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: 132.00  E-value: 4.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE---EIKQEINMLKKYSHhRNIATYYGAFIKksppgnDDQL 101
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKekeASKKEVILLAKMKH-PNIVTFFASFQE------NGRL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV-KLVDFGVSAQLDR 180
Cdd:cd08225    75 FIVMEYCDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLND 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  181 TVGRRNTFIGTPYWMAPEViaCDENPdatYDYRSDIWSLGITAIEmaegappLCDM-HP 238
Cdd:cd08225   155 SMELAYTCVGTPYYLSPEI--CQNRP---YNNKTDIWSLGCVLYE-------LCTLkHP 201
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
25-234 5.88e-34

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: 132.61  E-value: 5.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVmdvtedeeeeIKQ-------------EINMLKKYSHhRNIATYYGAFIK 91
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKK----------IRLdneeegipstalrEISLLKELKH-PNIVKLLDVIHT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   92 KSppgnddQLWLVMEFCGagsvTDLVK--NTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 169
Cdd:cd07829    70 EN------KLYLVFEYCD----QDLKKylDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKL 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  170 VDFGvsaqLDRTVG---RRNTF-IGTPYWMAPEVIACDENpdatYDYRSDIWSLG-ITAiEMAEGAPPLC 234
Cdd:cd07829   140 ADFG----LARAFGiplRTYTHeVVTLWYRAPEILLGSKH----YSTAVDIWSVGcIFA-ELITGKPLFP 200
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
25-226 1.12e-33

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: 131.26  E-value: 1.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYsHHRNIATYYGAFIKksppgnDDQLW 102
Cdd:cd13996     8 FEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKvlREVKALAKL-NHPNIVRYYTAWVE------EPPLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTD-LVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA-EVKLVDFGV------ 174
Cdd:cd13996    81 IQMELCEGGTLRDwIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDlQVKIGDFGLatsign 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  175 ----SAQLDRTVGRRN----TFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEM 226
Cdd:cd13996   161 qkreLNNLNNNNNGNTsnnsVGIGTPLYASPEQLDGEN-----YNEKADIYSLGIILFEM 215
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
25-231 1.44e-33

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 131.50  E-value: 1.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdvtedeeeeiKQ------------EINMLKKYSHHRNIATYYGAFIKK 92
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKM----------KKkfysweecmnlrEVKSLRKLNEHPNIVKLKEVFREN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 sppgndDQLWLVMEFCgAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 172
Cdd:cd07830    71 ------DELYFVFEYM-EGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADF 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  173 GvsaqLDRTVGRRNTF---IGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07830   144 G----LAREIRSRPPYtdyVSTRWYRAPEILLRSTS----YSSPVDIWALGCIMAELYTLRP 197
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
25-289 2.88e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 129.85  E-value: 2.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK---VMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKksppgnDDQL 101
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKqipVEQMTKEERQAALNEVKVLSML-HHPNIIEYYESFLE------DKAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE-VKLVDFGVSAQLDr 180
Cdd:cd08220    75 MIVMEYAPGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKILS- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNTFIGTPYWMAPEViaCDENPdatYDYRSDIWSLGITAIEMA------EGAP-PLCDMHPMRALFliprNPPprl 253
Cdd:cd08220   154 SKSKAYTVVGTPCYISPEL--CEGKP---YNQKSDIWALGCVLYELAslkrafEAANlPALVLKIMRGTF----API--- 221
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  254 kSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd08220   222 -SDRYSEELRHLILSMLHLDPNKRPTLSEIMAQPII 256
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
25-295 1.40e-32

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: 129.79  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLkkysHHRN---IATYYGAFIkksppgNDD 99
Cdd:cd06650     7 FEKISELGAGNGGVVFKVSHKPSGLVMARKLihLEIKPAIRNQIIRELQVL----HECNspyIVGFYGAFY------SDG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHL-HAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd06650    77 EISICMEHMDGGSLDQVLK--KAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL------------------------- 233
Cdd:cd06650   155 IDSMA--NSFVGTRSYMSPERLQ-----GTHYSVQSDIWSMGLSLVEMAVGRYPIpppdakelelmfgcqvegdaaetpp 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  234 -------------CDMHPMRALF----LIPRNPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTE 295
Cdd:cd06650   228 rprtpgrplssygMDSRPPMAIFelldYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAE 306
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
25-224 2.17e-32

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: 127.47  E-value: 2.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM----DVTEDEEEEIK----QEINMLKKYSHHRNIATYYGAFikksppG 96
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksgPNSKDGNDFQKlpqlREIDLHRRVSRHPNIITLHDVF------E 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 NDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE-VKLVDFGVS 175
Cdd:cd13993    76 TEVAIYIVLEYCPNGDLFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGtVKLCDFGLA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  176 AQLDRTvgrRNTFIGTPYWMAPEVIacDENPD--ATYDYRS-DIWSLGITAI 224
Cdd:cd13993   156 TTEKIS---MDFGVGSEFYMAPECF--DEVGRslKGYPCAAgDIWSLGIILL 202
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
25-241 5.05e-32

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: 126.24  E-value: 5.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFikksppGNDDQLW 102
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEirLPKSSSAVEDSRKEAVLLAKMKH-PNIVAFKESF------EADGHLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd08219    75 IVMEYCDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIGTPYWMAPEVIacdENpdATYDYRSDIWSLGITAIEmaegappLCDM-HPMRA 241
Cdd:cd08219   155 AYACTYVGTPYYVPPEIW---EN--MPYNNKSDIWSLGCILYE-------LCTLkHPFQA 202
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
25-286 6.16e-32

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 126.33  E-value: 6.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK--VMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKksppgnDDQLW 102
Cdd:cd14046     8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKkiKLRSESKNNSRILREVMLLSRL-NHQHVVRYYQAWIE------RANLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNtkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd14046    81 IQMEYCEKSTLRDLIDS--GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFI------------------GTPYWMAPEVIAcdeNPDATYDYRSDIWSLGITAIEMAEgaPPLCDM---HPMRA 241
Cdd:cd14046   159 ELATQDInkstsaalgssgdltgnvGTALYVAPEVQS---GTKSTYNEKVDMYSLGIIFFEMCY--PFSTGMervQILTA 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578829925  242 LFLIPRNPPPRLKSKKWSKKFiDFIDTCLIKTYLSRPPTEQLLKF 286
Cdd:cd14046   234 LRSVSIEFPPDFDDNKHSKQA-KLIRWLLNHDPAKRPSAQELLKS 277
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
25-288 7.05e-32

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: 126.85  E-value: 7.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK--VMDvtedeeEEIKQ-EINMLKKYsHHRNIATYYGAFIKKSPPGNDDQL 101
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKkvLQD------KRYKNrELQIMRRL-KHPNIVKLKYFFYSSGEKKDEVYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCgAGSVTDLVKNTKGNALKEDCI-----AYicrEILRGLAHLHAHKVIHRDIKGQNVLL-TENAEVKLVDFGvS 175
Cdd:cd14137    79 NLVMEYM-PETLYRVIRHYSKNKQTIPIIyvklySY---QLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDFG-S 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDAT-YDYRSDIWSLG-ITAiEMAEGAP--------------------P- 232
Cdd:cd14137   154 AKRLVPGEPNVSYICSRYYRAPELIF-----GATdYTTAIDIWSAGcVLA-ELLLGQPlfpgessvdqlveiikvlgtPt 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  233 ---LCDMHPMRALFliprnPPPRLKSKKWSKKF--------IDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14137   228 reqIKAMNPNYTEF-----KFPQIKPHPWEKVFpkrtppdaIDLLSKILVYNPSKRLTALEALAHPF 289
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
25-288 1.02e-31

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: 125.95  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdVTEDEEEEIKQ----EINMLKKYSHhRNIATYYGAFIKKSppgnddQ 100
Cdd:cd07847     3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKKF-VESEDDPVIKKialrEIRMLKQLKH-PNLVNLIEVFRRKR------K 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd07847    75 LHLVFEYCDHTVLNELEKNPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAP--P----LCDMHPMRALF--LIPRN---- 248
Cdd:cd07847   153 PGDDYTDYVATRWYRAPELLV----GDTQYGPPVDVWAIGCVFAELLTGQPlwPgksdVDQLYLIRKTLgdLIPRHqqif 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  249 -------------PPPR--LKSK--KWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd07847   229 stnqffkglsipePETRepLESKfpNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
25-288 8.18e-31

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: 123.23  E-value: 8.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEI---------KQEINMLKKYSHHRNIATYYGAFikKSPP 95
Cdd:cd14093     5 YEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENeaeelreatRREIEILRQVSGHPNIIELHDVF--ESPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 gnddQLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd14093    83 ----FIFLVFELCRKGELFDYL--TEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQLDRTVGRRNtFIGTPYWMAPEVIACDENPDAT-YDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIpRNPPPRLK 254
Cdd:cd14093   157 TRLDEGEKLRE-LCGTPGYLAPEVLKCSMYDNAPgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNI-MEGKYEFG 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578829925  255 SKKW---SKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14093   235 SPEWddiSDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
29-290 1.13e-30

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: 122.54  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDV-------TEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKksppgnDDQL 101
Cdd:cd06630     6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFcrnssseQEEVVEAIREEIRMMARLNH-PNIVRMLGATQH------KSHF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE-VKLVDFGVSAQLDR 180
Cdd:cd06630    79 NIFVEWMAGGSVASLLSKY--GAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAAARLAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNTF----IGTPYWMAPEVIAcDENpdatYDYRSDIWSLGITAIEMAEGAPPL--CDMHPMRALFL---------- 244
Cdd:cd06630   157 KGTGAGEFqgqlLGTIAFMAPEVLR-GEQ----YGRSCDVWSVGCVIIEMATAKPPWnaEKISNHLALIFkiasattppp 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578829925  245 IPRNPPPRLKskkwskkfiDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd06630   232 IPEHLSPGLR---------DVTLRCLELQPEDRPPARELLKHPVFT 268
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
32-232 1.79e-30

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: 121.22  E-value: 1.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikKSPPGnddqLWLVMEFCGAG 111
Cdd:cd14006     2 GRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQL-QHPRIIQLHEAY--ESPTE----LVLILELCSGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  112 SVTDLVkNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE--VKLVDFGVSAQLDRTVGRRNTFi 189
Cdd:cd14006    75 ELLDRL-AERGS-LSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARKLNPGEELKEIF- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578829925  190 GTPYWMAPEVIacDENPDATYdyrSDIWSLGITAIEMAEGAPP 232
Cdd:cd14006   152 GTPEFVAPEIV--NGEPVSLA---TDMWSIGVLTYVLLSGLSP 189
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
28-289 2.61e-30

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: 121.00  E-value: 2.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYS--HHRNIATYYGAFIkksppgNDDQLWLVM 105
Cdd:cd08221     5 VRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSllNHDNIITYYNHFL------DGESLFIEM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR 185
Cdd:cd08221    79 EYCNGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  186 NTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNpPPRLKSKKWSKKFIDF 265
Cdd:cd08221   159 ESIVGTPYYMSPELVQGVK-----YNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQG-EYEDIDEQYSEEIIQL 232
                         250       260
                  ....*....|....*....|....
gi 578829925  266 IDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd08221   233 VHDCLHQDPEDRPTAEELLERPLL 256
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
2-297 5.72e-30

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 123.01  E-value: 5.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    2 GDPAPARSLDDIDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKySHH 79
Cdd:PLN00034   53 SSSSSSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTVRRQICREIEILRD-VNH 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   80 RNIATYYGAFikksppGNDDQLWLVMEFCGAGSVtdlvKNTKGNalKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNV 159
Cdd:PLN00034  132 PNVVKCHDMF------DHNGEIQVLLEFMDGGSL----EGTHIA--DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  160 LLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENpDATYD-YRSDIWSLGITAIEMAEGAPPLC---- 234
Cdd:PLN00034  200 LINSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTDLN-HGAYDgYAGDIWSLGVSILEFYLGRFPFGvgrq 278
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  235 -DMHP-MRALFLI-PRNPPPRLkskkwSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI-RDQPTERQ 297
Cdd:PLN00034  279 gDWASlMCAICMSqPPEAPATA-----SREFRHFISCCLQREPAKRWSAMQLLQHPFIlRAQPGQGQ 340
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
25-283 6.56e-30

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: 121.15  E-value: 6.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRnIATYYGAFikksppGNDDQ 100
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKkakiIKLKQVEHVLNEKRILSEVRHPF-IVNLLGSF------QDDRN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDr 180
Cdd:cd05580    76 LYMVMEYVPGGELFSLLR--RSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 tvGRRNTFIGTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIprnppprLKSKKWSK 260
Cdd:cd05580   153 --DRTYTLCGTPEYLAPEIILS-----KGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKI-------LEGKIRFP 218
                         250       260
                  ....*....|....*....|...
gi 578829925  261 KFIDFIDTCLIKTYLSRPPTEQL 283
Cdd:cd05580   219 SFFDPDAKDLIKRLLVVDLTKRL 241
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
25-289 7.47e-30

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: 119.67  E-value: 7.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYgAFikksppGNDDQ 100
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNkqkcIEKDSVRNVLNELEILQELEHPFLVNLWY-SF------QDEED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGsvtDLVKN-TKGNALKEDCIA-YICrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd05578    75 MYMVVDLLLGG---DLRYHlQQKVKFSEETVKfYIC-EIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 drTVGRRNTFI-GTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAEGAPPLcDMHP------MRALFLIPRNPPP 251
Cdd:cd05578   151 --TDGTLATSTsGTKPYMAPEVFMR-----AGYSFAVDWWSLGVTAYEMLRGKRPY-EIHSrtsieeIRAKFETASVLYP 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578829925  252 rlksKKWSKKFIDFIDTCL---IKTYLSRPptEQLLKFPFI 289
Cdd:cd05578   223 ----AGWSEEAIDLINKLLerdPQKRLGDL--SDLKNHPYF 257
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
25-255 3.34e-29

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: 117.89  E-value: 3.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSppgnddQ 100
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDkeqvAREGMVEQIKREIAIMKLLRH-PNIVELHEVMATKT------K 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA--QL 178
Cdd:cd14663    75 IFFVMELVTGGELFSKI--AKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSAlsEQ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYD-YRSDIWSLGITAIEMAEGAPPLCDMHPM-------RALFLIPRNPP 250
Cdd:cd14663   153 FRQDGLLHTTCGTPNYVAPEVLA-----RRGYDgAKADIWSCGVILFVLLAGYLPFDDENLMalyrkimKGEFEYPRWFS 227

                  ....*
gi 578829925  251 PRLKS 255
Cdd:cd14663   228 PGAKS 232
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
25-288 3.76e-29

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: 118.82  E-value: 3.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD---------VTedeeeeIKQEINMLKKYsHHRNIATYYGAFIKKSPP 95
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRmenekegfpIT------AIREIKLLQKL-DHPNVVRLKEIVTSKGSA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 GNDDQLWLVMEFCGagsvTDL--VKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG 173
Cdd:cd07840    74 KYKGSIYMVFEYMD----HDLtgLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  174 vsaqLDRTVGRRNTFIGTP-----YWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAPPLC---DMH-------- 237
Cdd:cd07840   150 ----LARPYTKENNADYTNrvitlWYRPPELLLGATR----YGPEVDMWSVGCILAELFTGKPIFQgktELEqlekifel 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  238 ---------------PMRALFLIPRNPPPRLK---SKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd07840   222 cgspteenwpgvsdlPWFENLKPKKPYKRRLRevfKNVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
25-288 6.80e-29

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: 117.91  E-value: 6.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK---QEINMLKKYsHHRNIATYYGAFIKKSppgnddQL 101
Cdd:cd07846     3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKiamREIKMLKQL-RHENLVNLIEVFRRKK------RW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd07846    76 YLVFEFVDHTVLDDLEKYPNG--LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAPPL---CDM----HPMRAL-FLIPR------ 247
Cdd:cd07846   154 GEVYTDYVATRWYRAPELLV----GDTKYGKAVDVWAVGCLVTEMLTGEPLFpgdSDIdqlyHIIKCLgNLIPRhqelfq 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  248 -NP--------------PPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd07846   230 kNPlfagvrlpevkevePLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
24-288 9.91e-29

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 116.93  E-value: 9.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKtGQLAAIKVMDVTEDEEEEI---KQEINMLKKYSHHRNIATYYGAFIKksppGNDDQ 100
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVLNPK-KKIYALKRVDLEGADEQTLqsyKNEIELLKKLKGSDRIIQLYDYEVT----DEDDY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEfCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAeVKLVDFGVSAQL-- 178
Cdd:cd14131    77 LYMVME-CGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGR-LKLIDFGIAKAIqn 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIACDEN-----PDATYDYRSDIWSLGITAIEMAEGAPPLCD-MHPMRALFLIPrNPPPR 252
Cdd:cd14131   155 DTTSIVRDSQVGTLNYMSPEAIKDTSAsgegkPKSKIGRPSDVWSLGCILYQMVYGKTPFQHiTNPIAKLQAII-DPNHE 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578829925  253 LKSKKWSKKF-IDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14131   234 IEFPDIPNPDlIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
25-286 1.16e-28

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: 116.67  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYSHhRNIATYYGAFIKksppgnDDQ 100
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQdcvkEIDLLKQLNH-PNVIKYLDSFIE------DNE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGNA--LKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd08228    77 LNIVLELADAGDLSQMIKYFKKQKrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIacDENpdaTYDYRSDIWSLGITAIEMAEGAPPLC--DMHPMRALFLIPRNPPPRLKSK 256
Cdd:cd08228   157 SSKTTAAHSLVGTPYYMSPERI--HEN---GYNFKSDIWSLGCLLYEMAALQSPFYgdKMNLFSLCQKIEQCDYPPLPTE 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 578829925  257 KWSKKFIDFIDTCLIKTYLSRPPTEQLLKF 286
Cdd:cd08228   232 HYSEKLRELVSMCIYPDPDQRPDIGYVHQI 261
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
31-283 1.37e-28

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: 116.17  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKySHHRNIATYYGAFikksppgNDDQ-LWLVM 105
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKkrhiVQTRQQEHIFSEKEILEE-CNSPFIVKLYRTF-------KDKKyLYMLM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNtKGNALKEDCIAYI-CreILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRtvGR 184
Cdd:cd05572    73 EYCLGGELWTILRD-RGLFDEYTARFYTaC--VVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGS--GR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  185 RN-TFIGTPYWMAPEVIacdENpdATYDYRSDIWSLGITAIEMAEGAPPLC--DMHPMRALFLIPRNppprlKSKKWSKK 261
Cdd:cd05572   148 KTwTFCGTPEYVAPEII---LN--KGYDFSVDYWSLGILLYELLTGRPPFGgdDEDPMKIYNIILKG-----IDKIEFPK 217
                         250       260
                  ....*....|....*....|..
gi 578829925  262 FIDFIDTCLIKTYLSRPPTEQL 283
Cdd:cd05572   218 YIDKNAKNLIKQLLRRNPEERL 239
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
25-309 1.66e-28

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: 118.54  E-value: 1.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEINMLKKYSHHRN------------IATYYGAFikk 92
Cdd:cd05573     3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILR---------KSDMLKREQIAHVRAerdiladadspwIVRLHYAF--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 sppGNDDQLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 172
Cdd:cd05573    71 ---QDEDHLYLVMEYMPGGDLMNLL--IKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  173 GVSAQLD------------------------------RTVgRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGIT 222
Cdd:cd05573   146 GLCTKMNksgdresylndsvntlfqdnvlarrrphkqRRV-RAYSAVGTPDYIAPEVLRGTG-----YGPECDWWSLGVI 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  223 AIEMAEGAPPLCDMHPM---------RALFLIPRNPPprlkskkWSKKFIDFIDTCLI--KTYLSRppTEQLLKFPF--- 288
Cdd:cd05573   220 LYEMLYGFPPFYSDSLVetyskimnwKESLVFPDDPD-------VSPEAIDLIRRLLCdpEDRLGS--AEEIKAHPFfkg 290
                         330       340
                  ....*....|....*....|....*.
gi 578829925  289 -----IRDQPTErqVRIQLKDHIDRS 309
Cdd:cd05573   291 idwenLRESPPP--FVPELSSPTDTS 314
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
31-283 2.43e-28

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: 115.49  E-value: 2.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKqeinmLKKYSHHRNIATYYGAFIKksppgnDDQLWLVMEFCGA 110
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVE-----IQACFRHENIAELYGALLW------EETVHLFMEAGEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVkLVDFGVSAQLDRTVGRRNTFIG 190
Cdd:cd13995    81 GSV--LEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLRG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  191 TPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRA----LFLIPRNPPPrlkskkwskkFIDFI 266
Cdd:cd13995   158 TEIYMSPEVILC-----RGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQAPP----------LEDIA 222
                         250       260
                  ....*....|....*....|...
gi 578829925  267 DTC------LIKTYLSRPPTEQL 283
Cdd:cd13995   223 QDCspamreLLEAALERNPNHRS 245
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
24-287 2.71e-28

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: 115.10  E-value: 2.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKV-MDVTEDEEEEIKQ--EINMLKKYSHHRNIATYYGAFIKKsppgndDQ 100
Cdd:cd14050     2 CFTILSKLGEGSFGEVFKVRSREDGKLYAVKRsRSRFRGEKDRKRKleEVERHEKLGEHPNCVRFIKAWEEK------GI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGagsvTDLVKNTKGN-ALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd14050    76 LYIQTELCD----TSLQQYCEEThSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RtVGRRNTFIGTPYWMAPEVIacdenpDATYDYRSDIWSLGITAIEMAegapplCDMHpmralflIPRNPP--------- 250
Cdd:cd14050   152 K-EDIHDAQEGDPRYMAPELL------QGSFTKAADIFSLGITILELA------CNLE-------LPSGGDgwhqlrqgy 211
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578829925  251 -PRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFP 287
Cdd:cd14050   212 lPEEFTAGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
25-287 6.25e-28

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: 114.02  E-value: 6.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV---TEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKksppgnDDQL 101
Cdd:cd13997     2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKpfrGPKERARALREVEAHAALGQHPNIVRYYSSWEE------GGHL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLV-KNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd13997    76 YIQMELCENGSLQDALeELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLET 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNtfiGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPplcdMHPMRALFLIPRN-PPPRLKSKKWS 259
Cdd:cd13997   156 SGDVEE---GDSRYLAPELL----NENYTHLPKADIFSLGVTVYEAATGEP----LPRNGQQWQQLRQgKLPLPPGLVLS 224
                         250       260
                  ....*....|....*....|....*...
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFP 287
Cdd:cd13997   225 QELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
31-232 7.73e-28

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: 114.00  E-value: 7.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVK-TGQLAAIKVMDVTEDEEEE--IKQEINMLKKYsHHRNIATYYgaFIKKSPpgndDQLWLVMEF 107
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQnlLGKEIKILKEL-SHENVVALL--DCQETS----SSVYLVMEY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKnTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE---------VKLVDFGVSAQL 178
Cdd:cd14120    74 CNGGDLADYLQ-AKGT-LSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndirLKIADFGFARFL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  179 DRTVgRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14120   152 QDGM-MAATLCGSPMYMAPEVIMSLQ-----YDAKADLWSIGTIVYQCLTGKAP 199
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
31-232 8.70e-28

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: 114.11  E-value: 8.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQE--INMLKKYSHhrNIATYYGAFIKKsppgndDQLWLV 104
Cdd:cd05611     4 ISKGAFGSVYLAKKRSTGDYFAIKVLKksdmIAKNQVTNVKAEraIMMIQGESP--YVAKLYYSFQSK------DYLYLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLdrTVGR 184
Cdd:cd05611    76 MEYLNGGDCASLIKTLGG--LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNG--LEKR 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578829925  185 RNT-FIGTPYWMAPEVIacDENPDatyDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05611   152 HNKkFVGTPDYLAPETI--LGVGD---DKMSDWWSLGCVIFEFLFGYPP 195
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
24-310 8.90e-28

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: 114.70  E-value: 8.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIK-VMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSppgnddQLW 102
Cdd:cd14166     4 TFIFMEVLGSGAFSEVYLVKQRSTGKLYALKcIKKSPLSRDSSLENEIAVLKRIKH-ENIVTLEDIYESTT------HYY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNtKGNALKEDCiAYICREILRGLAHLHAHKVIHRDIKGQNVL-LT--ENAEVKLVDFGVSAQLD 179
Cdd:cd14166    77 LVMQLVSGGELFDRILE-RGVYTEKDA-SRVINQVLSAVKYLHENGIVHRDLKPENLLyLTpdENSKIMITDFGLSKMEQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RtvGRRNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRaLFLIPRNPPPRLKSKKW- 258
Cdd:cd14166   155 N--GIMSTACGTPGYVAPEVLA--QKP---YSKAVDCWSIGVITYILLCGYPPFYEETESR-LFEKIKEGYYEFESPFWd 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  259 --SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI-------RDqpTERQVRIQLKDHIDRSR 310
Cdd:cd14166   227 diSESAKDFIRHLLEKNPSKRYTCEKALSHPWIigntalhRD--IYPSVSEQIQKNFAKSK 285
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
30-232 1.14e-27

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: 114.03  E-value: 1.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMD---------VTEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKsppgnDDQ 100
Cdd:cd14084    13 TLGSGACGEVKLAYDKSTCKKVAIKIINkrkftigsrREINKPRNIETEIEILKKLSHPCIIKIE--DFFDA-----EDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE---VKLVDFGVSAQ 177
Cdd:cd14084    86 YYIVLELMEGGELFDRVVSNKR--LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKI 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  178 LDRTVGRRnTFIGTPYWMAPEVIAcdENPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14084   164 LGETSLMK-TLCGTPTYLAPEVLR--SFGTEGYTRAVDCWSLGVILFICLSGYPP 215
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
25-232 2.24e-27

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: 112.48  E-value: 2.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikksppGNDDQ 100
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKkdkiEDEQDMVRIRREIEIMSSL-NHPHIIRIYEVF------ENKDK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA--QL 178
Cdd:cd14073    76 IVIVMEYASGGELYDYISERRR--LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNlySK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  179 DRTVGrrnTFIGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14073   154 DKLLQ---TFCGSPLYASPEIV----NGTPYQGPEVDCWSLGVLLYTLVYGTMP 200
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
25-283 2.72e-27

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


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 112.98  E-value: 2.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGR-HVKTGQLAAIKVMDVTEDEEEEIKQ-----------EINMLKKYSHHRNIATYYGAFIKk 92
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRkKSNGQTLLALKEINMTNPAFGRTEQerdksvgdiisEVNIIKEQLRHPNIVRYYKTFLE- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 sppgnDDQLWLVMEFCGAGSVTDLVKN--TKGNALKEDCIAYICREILRGLAHLHAHK-VIHRDIKGQNVLLTENAEVKL 169
Cdd:cd08528    81 -----NDRLYIVMELIEGAPLGEHFSSlkEKNEHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGEDDKVTI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  170 VDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLcdmHPMRALFLIPR-- 247
Cdd:cd08528   156 TDFGLAKQKGPESSKMTSVVGTILYSCPEIVQ-----NEPYGEKADIWALGCILYQMCTLQPPF---YSTNMLTLATKiv 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578829925  248 ----NPPPrlkSKKWSKKFIDFIDTCLIKTYLSRPPTEQL 283
Cdd:cd08528   228 eaeyEPLP---EGMYSDDITFVIRSCLTPDPEARPDIVEV 264
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
31-232 2.91e-27

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: 112.43  E-value: 2.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK---QEINMLKKYsHHRNIATYYGAFIKKSppgnddQLWLVMEF 107
Cdd:cd14075    10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRllsREISSMEKL-HHPNIIRLYEVVETLS------KLHLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTvGRRNT 187
Cdd:cd14075    83 ASGGEL--YTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRG-ETLNT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578829925  188 FIGTPYWMAPEVIaCDENPDATYdyrSDIWSLGITAIEMAEGAPP 232
Cdd:cd14075   160 FCGSPPYAAPELF-KDEHYIGIY---VDIWALGVLLYFMVTGVMP 200
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
29-232 5.16e-27

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: 111.61  E-value: 5.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHvKTG--QLAAIKVMD---VTEDEEEEIKQEINMLKKYsHHRNIATYygafikKSPPGNDDQLWL 103
Cdd:cd14121     1 EKLGSGTYATVYKAYR-KSGarEVVAVKCVSkssLNKASTENLLTEIELLKKL-KHPHIVEL------KDFQWDEEHIYL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKgnALKEdciaYICREILRGLA----HLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVsAQ 177
Cdd:cd14121    73 IMEYCSGGDLSRFIRSRR--TLPE----STVRRFLQQLAsalqFLREHNISHMDLKPQNLLLSsrYNPVLKLADFGF-AQ 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14121   146 HLKPNDEAHSLRGSPLYMAPEMILKK-----KYDARVDLWSVGVILYECLFGRAP 195
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
29-238 5.92e-27

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: 111.71  E-value: 5.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQV----YKGRHVktgqlaAIKVMDV---TEDEEEEIKQEINMLkkYSHHRNIATYYGAfikKSPPGNDDQL 101
Cdd:cd13979     9 EPLGSGGFGSVykatYKGETV------AVKIVRRrrkNRASRQSFWAELNAA--RLRHENIVRVLAA---ETGTDFASLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR- 180
Cdd:cd13979    78 LIIMEYCGNGTLQQLIYEGSEPLPLAHRILISL-DIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEg 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 --TVGRRNTFIGTPYWMAPEVIaCDENPDAtydyRSDIWSLGITAIEMAEGAPPLCDMHP 238
Cdd:cd13979   157 neVGTPRSHIGGTYTYRAPELL-KGERVTP----KADIYSFGITLWQMLTRELPYAGLRQ 211
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
23-251 8.16e-27

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: 110.81  E-value: 8.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   23 GIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSppgnd 98
Cdd:cd14081     1 GPYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNkeklSKESVLMKVEREIAIMKLIEH-PNVLKLYDVYENKK----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dQLWLVMEFCGAGSVTD-LVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVsAQ 177
Cdd:cd14081    75 -YLYLVLEYVSGGELFDyLVKKGR---LTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGM-AS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYR-SDIWSLGITAIEMAEGAPPLcDMHPMRAL--------FLIPRN 248
Cdd:cd14081   150 LQPEGSLLETSCGSPHYACPEVIKGEK-----YDGRkADIWSCGVILYALLVGALPF-DDDNLRQLlekvkrgvFHIPHF 223

                  ...
gi 578829925  249 PPP 251
Cdd:cd14081   224 ISP 226
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
25-289 8.26e-27

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 111.21  E-value: 8.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHH-----RNIATYYGAFIKKsppgndD 99
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNKKdkadkYHIVRLKDVFYFK------N 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA--EVKLVDFGVSAQ 177
Cdd:cd14133    75 HLCIVFELLSQ-NLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDFGSSCF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRtvgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPM----RALFLIPRnPPPRL 253
Cdd:cd14133   154 LTQ---RLYSYIQSRYYRAPEVIL-----GLPYDEKIDMWSLGCILAELYTGEPLFPGASEVdqlaRIIGTIGI-PPAHM 224
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578829925  254 --KSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14133   225 ldQGKADDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
25-233 8.46e-27

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: 111.11  E-value: 8.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEI-NMLKKYSH--HRNIATYYGAFikksppGNDDQL 101
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVrNEVEIHCQlkHPSILELYNYF------EDSNYV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd14186    77 YLVLEMCHNGEMSRYLKNRK-KPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMP 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  182 VGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14186   156 HEKHFTMCGTPNYISPEIAT-----RSAHGLESDVWSLGCMFYTLLVGRPPF 202
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
25-289 1.26e-26

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 111.87  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHH-----RNIATYYGAFIKKSppgndd 99
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALVEVKILKHLNDNdpddkHNIVRYKDSFIFRG------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN--AEVKLVDFGVSAQ 177
Cdd:cd14210    89 HLCIVFELLSI-NLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPskSSIKVIDFGSSCF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVgrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL----------CDM----HPMRAL- 242
Cdd:cd14210   168 EGEKV---YTYIQSRFYRAPEVIL-----GLPYDTAIDMWSLGCILAELYTGYPLFpgeneeeqlaCIMevlgVPPKSLi 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  243 ---------FLIPRNPPP---------RLKSKKWS-------KKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14210   240 dkasrrkkfFDSNGKPRPttnskgkkrRPGSKSLAqvlkcddPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
25-283 1.45e-26

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 112.22  E-value: 1.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEINMLKKYSH------------HRNIATYYGAFIkk 92
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLK---------KREILKMKQVQHvaqeksilmelsHPFIVNMMCSFQ-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 sppgNDDQLWLVMEFCGAGSV-TDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVD 171
Cdd:PTZ00263   89 ----DENRVYFLLEFVVGGELfTHLRKAGR---FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  172 FGVSAQL-DRTVgrrnTFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNpp 250
Cdd:PTZ00263  162 FGFAKKVpDRTF----TLCGTPEYLAPEVIQSKGHGKAV-----DWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAG-- 230
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578829925  251 pRLKSKKWskkfIDFIDTCLIKTYLSRPPTEQL 283
Cdd:PTZ00263  231 -RLKFPNW----FDGRARDLVKGLLQTDHTKRL 258
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
31-284 2.16e-26

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: 109.79  E-value: 2.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKySHHRNIATYYGAFIKksppgndDQLWLVMEFCGA 110
Cdd:cd14062     1 IGSGSFGTVYKGRWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRK-TRHVNILLFMGYMTK-------PQLAIVTQWCEG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDL--VKNTKGNALKedcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNT- 187
Cdd:cd14062    73 SSLYKHlhVLETKFEMLQ---LIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQFe 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  188 -FIGTPYWMAPEVIAC-DENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPM-RALFLIPR---NPPPRLKSKKWSKK 261
Cdd:cd14062   150 qPTGSILWMAPEVIRMqDENP---YSFQSDVYAFGIVLYELLTGQLPYSHINNRdQILFMVGRgylRPDLSKVRSDTPKA 226
                         250       260
                  ....*....|....*....|...
gi 578829925  262 FIDFIDTCLIKTYLSRPPTEQLL 284
Cdd:cd14062   227 LRRLMEDCIKFQRDERPLFPQIL 249
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
23-221 2.58e-26

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


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 109.39  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   23 GIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTE--DEEEEIKQEINMLKKYSHhRNIATYYgAFIKksppgNDDQ 100
Cdd:cd14078     3 KYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlgDDLPRVKTEIEALKNLSH-QHICRLY-HVIE-----TDNK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd14078    76 IFMVLEYCPGGELFDYI--VAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578829925  181 TVGRR-NTFIGTPYWMAPEVIACDEnpdatydY---RSDIWSLGI 221
Cdd:cd14078   154 GMDHHlETCCGSPAYAAPELIQGKP-------YigsEADVWSMGV 191
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
66-240 5.58e-26

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: 108.99  E-value: 5.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   66 IKQEINMLKKYSHhRNIATYYGafIKKSPpgNDDQLWLVMEFCGAGSVTDLVKNtkgNALKEDCIAYICREILRGLAHLH 145
Cdd:cd14118    61 VYREIAILKKLDH-PNVVKLVE--VLDDP--NEDNLYMVFELVDKGAVMEVPTD---NPLSEETARSYFRDIVLGIEYLH 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  146 AHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENpdaTYDYRS-DIWSLGITAI 224
Cdd:cd14118   133 YQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRK---KFSGKAlDIWAMGVTLY 209
                         170
                  ....*....|....*.
gi 578829925  225 EMAEGAPPLCDMHPMR 240
Cdd:cd14118   210 CFVFGRCPFEDDHILG 225
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
29-233 5.85e-26

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: 108.56  E-value: 5.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINM---LKKYSHHRNIATYYGAFIKKsppgndDQLWLVM 105
Cdd:cd14188     7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKeieLHRILHHKHVVQFYHYFEDK------ENIYILL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR 185
Cdd:cd14188    81 EYCSRRSMAHILKARK--VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  186 NTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14188   159 RTICGTPNYLSPEVLN-----KQGHGCESDIWALGCVMYTMLLGRPPF 201
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
29-289 6.17e-26

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: 108.94  E-value: 6.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRH-VKTGQLAAIKVMDVTEDEEEEI--KQEINMLKKYSHHRNIATYYgafIKKSPpgndDQLWLVM 105
Cdd:cd14201    12 DLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQIllGKEIKILKELQHENIVALYD---VQEMP----NSVFLVM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKnTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---------ENAEVKLVDFGVSA 176
Cdd:cd14201    85 EYCNGGDLADYLQ-AKGT-LSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFAR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  177 QLDRTVgRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHP--MRALFLIPRNPPPRLK 254
Cdd:cd14201   163 YLQSNM-MAATLCGSPMYMAPEVIMSQH-----YDAKADLWSIGTVIYQCLVGKPPFQANSPqdLRMFYEKNKNLQPSIP 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578829925  255 SKKwSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14201   237 RET-SPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
25-295 7.45e-26

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: 110.14  E-value: 7.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKySHHRNIATYYGAFIkksppgNDDQLW 102
Cdd:cd06649     7 FERISELGAGNGGVVTKVQHKPSGLIMARKLihLEIKPAIRNQIIRELQVLHE-CNSPYIVGFYGAFY------SDGEIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHL-HAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd06649    80 ICMEHMDGGSLDQVLKEAK--RIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL---------------------------- 233
Cdd:cd06649   158 MA--NSFVGTRSYMSPERLQ-----GTHYSVQSDIWSMGLSLVELAIGRYPIpppdakeleaifgrpvvdgeegephsis 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  234 --------------CDMHPMRALF----LIPRNPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTE 295
Cdd:cd06649   231 prprppgrpvsghgMDSRPAMAIFelldYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLMNHTFIKRSEVE 310
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
25-226 1.07e-25

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: 107.96  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVtedEEEEIKQEINMLKKYSHhRNIATYYGAFI---------KKSPP 95
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKL---NNEKAEREVKALAKLDH-PNIVRYNGCWDgfdydpetsSSNSS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 GNDDQ-LWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd14047    84 RSKTKcLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGL 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  175 SAQLdRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEM 226
Cdd:cd14047   164 VTSL-KNDGKRTKSKGTLSYMSPEQISSQ-----DYGKEVDIYALGLILFEL 209
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
24-231 1.24e-25

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 109.69  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK---QEINMLKkYSHHRNIATYYGAFIKKSPPGNDDQ 100
Cdd:cd07851    16 RYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKrtyRELRLLK-HMKHENVIGLLDVFTPASSLEDFQD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAgsvtDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd07851    95 VYLVTHLMGA----DLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDD 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  181 TVgrrNTFIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07851   171 EM---TGYVATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLTGKT 214
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
32-287 1.61e-25

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: 107.34  E-value: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHVKTGQLAAIKVMDVT-----EDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKsppgNDDQLWLVME 106
Cdd:cd14119     2 GEGSYGKVKEVLDTETLCRRAVKILKKRklrriPNGEANVKREIQILRRL-NHRNVIKLVDVLYNE----EKQKLYMVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGaGSVTDLVKNTKGNALKedcI----AYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd14119    77 YCV-GGLQEMLDSAPDKRLP---IwqahGYFV-QLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 --GRRNTFIGTPYWMAPEvIAcdeNPDATYD-YRSDIWSLGITAIEMAEGAPPLCDMHPMRaLF--------LIPRNPPP 251
Cdd:cd14119   152 edDTCTTSQGSPAFQPPE-IA---NGQDSFSgFKVDIWSAGVTLYNMTTGKYPFEGDNIYK-LFenigkgeyTIPDDVDP 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  252 RLKskkwskkfiDFIDTCLIKTYLSRPPTEQLLKFP 287
Cdd:cd14119   227 DLQ---------DLLRGMLEKDPEKRFTIEQIRQHP 253
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
25-226 1.86e-25

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: 107.75  E-value: 1.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE---EEIKQEINMLKK--YSHHRNIATYYGAFIKKSPpGNDD 99
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEgipLSTIREIALLKQleSFEHPNVVRLLDVCHGPRT-DREL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd07838    80 KLTLVFEHVDQ-DLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  180 RTVgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd07838   159 FEM-ALTSVVVTLWYRAPEVLL-----QSSYATPVDMWSVGCIFAEL 199
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
31-232 2.00e-25

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: 107.01  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQV--YKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYS-----HHRNIATYYGAFIKKSppgndDQLWL 103
Cdd:cd13994     1 IGKGATSVVriVTKKNPRSGVLYAVKEYRRRDDESKRKDYVKRLTSEYIissklHHPNIVKVLDLCQDLH-----GKWCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKG-NALKEDCiaYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL---- 178
Cdd:cd13994    76 VMEYCPGGDLFTLIEKADSlSLEEKDC--FFK-QILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFgmpa 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRS-DIWSLGITAIEMAEGAPP 232
Cdd:cd13994   153 EKESPMSAGLCGSEPYMAPEVFT-----SGSYDGRAvDVWSCGIVLFALFTGRFP 202
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
25-289 2.25e-25

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: 106.74  E-value: 2.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQ------LAAIKVMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKsppgnd 98
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATAdeelkvLKEISVGELQPDETVDANREAKLLSKLDH-PAIVKFHDSFVEK------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTK--GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAeVKLVDFGVSA 176
Cdd:cd08222    75 ESFCIVTEYCEGGDLDDKISEYKksGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  177 QLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAegapplCDMHP------MRALFLIPRNPP 250
Cdd:cd08222   154 ILMGTSDLATTFTGTPYYMSPEVLK-----HEGYNSKSDIWSLGCILYEMC------CLKHAfdgqnlLSVMYKIVEGET 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578829925  251 PRLkSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd08222   223 PSL-PDKYSKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
25-308 2.74e-25

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 107.33  E-value: 2.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEeikQEINMLKKYSHHRNIATYYGAFIkksppgNDDQLWLV 104
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPS---EEIEILLRYGQHPNIITLRDVYD------DGNSVYLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL---TENAE-VKLVDFGVSAQLdr 180
Cdd:cd14091    73 TELLRGGELLDRILRQK--FFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYadeSGDPEsLRICDFGFAKQL-- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 tvgrR--NTFIGTP-Y---WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPlcdmhpmralFLIPRNPPP--- 251
Cdd:cd14091   149 ----RaeNGLLMTPcYtanFVAPEVLK-----KQGYDAACDIWSLGVLLYTMLAGYTP----------FASGPNDTPevi 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  252 --RLKSKKwskkfIDFI----DTC------LIKTYLS-----RPPTEQLLKFPFIRDQPTERQVRIQLKDHIDR 308
Cdd:cd14091   210 laRIGSGK-----IDLSggnwDHVsdsakdLVRKMLHvdpsqRPTAAQVLQHPWIRNRDSLPQRQLTDPQDAAL 278
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
25-290 5.46e-25

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: 106.15  E-value: 5.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----------EINMLKKYSHHRNIATYYGAFIKKSp 94
Cdd:cd14182     5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEEvqelreatlkEIDILRKVSGHPNIIQLKDTYETNT- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   95 pgnddQLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd14182    84 -----FFFLVFDLMKKGELFDYL--TEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  175 SAQLDRTvGRRNTFIGTPYWMAPEVIACDENPD-ATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIpRNPPPRL 253
Cdd:cd14182   157 SCQLDPG-EKLREVCGTPGYLAPEIIECSMDDNhPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMI-MSGNYQF 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578829925  254 KSKKW---SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd14182   235 GSPEWddrSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
25-231 7.26e-25

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 107.23  E-value: 7.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK-VMDVTEDEEEE--IKQEINMLKkYSHHRNIATYYGAFIKKSPPGNDDqL 101
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKkISNVFDDLIDAkrILREIKILR-HLKHENIIGLLDILRPPSPEEFND-V 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGagsvTDLVKNTK-GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvsaqLDR 180
Cdd:cd07834    80 YIVTELME----TDLHKVIKsPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFG----LAR 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  181 TVGRRNTFIG-TPY----WM-APEVIACDENpdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07834   152 GVDPDEDKGFlTEYvvtrWYrAPELLLSSKK----YTKAIDIWSVGCIFAELLTRKP 204
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
25-231 7.36e-25

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: 106.03  E-value: 7.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFikksppGNDDQLW 102
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEihLDAEEGTPSTAIREISLMKELKH-ENIVRLHDVI------HTENKLM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGagsvTDLVK--NTKGN--ALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvsaqL 178
Cdd:cd07836    75 LVFEYMD----KDLKKymDTHGVrgALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFG----L 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  179 DRTVG-RRNTF---IGTPYWMAPEVIACDEnpdaTYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07836   147 ARAFGiPVNTFsneVVTLWYRAPDVLLGSR----TYSTSIDIWSVGCIMAEMITGRP 199
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
25-309 9.86e-25

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 106.54  E-value: 9.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKySHHRNIATYYGAFikksppGNDDQ 100
Cdd:cd05599     3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRksemLEKEQVAHVRAERDILAE-ADNPWVVKLYYSF------QDEEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVknTKGNALKEDCIA-YICREILrGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd05599    76 LYLIMEFLPGGDMMTLL--MKKDTLTEEETRfYIAETVL-AIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTfIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPM---------RALFLIPrnPP 250
Cdd:cd05599   153 KSHLAYST-VGTPDYIAPEVFLQK-----GYGKECDWWSLGVIMYEMLIGYPPFCSDDPQetcrkimnwRETLVFP--PE 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  251 PRLkskkwSKKFIDFIDT--CLIKTYLSRPPTEQLLKFPF--------IRDQPTErqVRIQLKDHIDRS 309
Cdd:cd05599   225 VPI-----SPEAKDLIERllCDAEHRLGANGVEEIKSHPFfkgvdwdhIRERPAP--ILPEVKSILDTS 286
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
25-289 1.23e-24

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: 104.78  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD---------VTEDEEEEIKQEINMLKKYSH--HRNIATYYGAFikks 93
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFkerilvdtwVRDRKLGTVPLEIHILDTLNKrsHPNIVKLLDFF---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   94 ppGNDDQLWLVMEFCGAG-SVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 172
Cdd:cd14004    78 --EDDEFYYLVMEKHGSGmDLFDFIERKPN--MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  173 GVSAQLDRtvGRRNTFIGTPYWMAPEVIAcdENPdatydYRS---DIWSLGITAIEMAEGAPPLCDM-HPMRALFLIPrn 248
Cdd:cd14004   154 GSAAYIKS--GPFDTFVGTIDYAAPEVLR--GNP-----YGGkeqDIWALGVLLYTLVFKENPFYNIeEILEADLRIP-- 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578829925  249 ppprlksKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14004   223 -------YAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
29-288 1.30e-24

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: 105.44  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE---------EEEIKQEINMLKKYSHHRNIATYYGAFIKKSppgndd 99
Cdd:cd14181    16 EVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERlspeqleevRSSTLKEIHILRQVSGHPSIITLIDSYESST------ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd14181    90 FIFLVFDLMRRGELFDYL--TEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNtFIGTPYWMAPEVIAC--DENPDAtYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIpRNPPPRLKSKK 257
Cdd:cd14181   168 PGEKLRE-LCGTPGYLAPEILKCsmDETHPG-YGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMI-MEGRYQFSSPE 244
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  258 W---SKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14181   245 WddrSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
29-253 1.80e-24

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: 104.06  E-value: 1.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAFIKKSPpgnddqLWLVME 106
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKflQEARILKQYDH-PNIVKLIGVCVQKQP------IMIVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKNtKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV---- 182
Cdd:cd05041    74 LVPGGSLLTFLRK-KGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEytvs 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  183 -GRRNTFIGtpyWMAPEVIACdenpdATYDYRSDIWSLGITAIEM-AEGAPPLCDMHPMRALFLIPRN---PPPRL 253
Cdd:cd05041   153 dGLKQIPIK---WTAPEALNY-----GRYTSESDVWSFGILLWEIfSLGATPYPGMSNQQTREQIESGyrmPAPEL 220
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
31-288 2.11e-24

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: 104.24  E-value: 2.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINM---LKKYSHHRNIATYYGAFikksppGNDDQLWLVMEF 107
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMeiaIHRSLAHQHVVGFHGFF------EDNDFVYVVLEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNT 187
Cdd:cd14187    89 CRRRSLLELHKRRK--ALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  188 FIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLcDMHPMRALFLiprnpppRLKSKKWS-KKFIDFI 266
Cdd:cd14187   167 LCGTPNYIAPEVLS-----KKGHSFEVDIWSIGCIMYTLLVGKPPF-ETSCLKETYL-------RIKKNEYSiPKHINPV 233
                         250       260
                  ....*....|....*....|....*..
gi 578829925  267 DTCLIKTYL-----SRPPTEQLLKFPF 288
Cdd:cd14187   234 AASLIQKMLqtdptARPTINELLNDEF 260
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
25-248 2.76e-24

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: 103.94  E-value: 2.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQL-AAIKVMDVT--EDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSppgnddqL 101
Cdd:cd14202     4 FSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKnlAKSQTLLGKEIKILKELKHENIVALYDFQEIANS-------V 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---------ENAEVKLVDF 172
Cdd:cd14202    77 YLVMEYCNGGDLADYLHTMR--TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADF 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  173 GVSAQLDRTVgRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRN 248
Cdd:cd14202   155 GFARYLQNNM-MAATLCGSPMYMAPEVIMSQH-----YDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKN 224
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
25-284 2.88e-24

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: 104.30  E-value: 2.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKvmDVTEDEEEEIKQ---EINMLKKYSHHRNIATYYGAFIKKSPPGNddQL 101
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALK--KILCHSKEDVKEamrEIENYRLFNHPNILRLLDSQIVKEAGGKK--EV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNT--KGNALKEDCIAYICREILRGLAHLHAHK---VIHRDIKGQNVLLTENAEVKLVDFGVSA 176
Cdd:cd13986    78 YLLLPYYKRGSLQDEIERRlvKGTFFPEDRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLSEDDEPILMDLGSMN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  177 QLDRTV-GRRN--------TFIGTPYWMAPEViaCDENPDATYDYRSDIWSLGITAIEMAEGAPPLcDMHPMR------- 240
Cdd:cd13986   158 PARIEIeGRREalalqdwaAEHCTMPYRAPEL--FDVKSHCTIDEKTDIWSLGCTLYALMYGESPF-ERIFQKgdslala 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  241 ---ALFLIPRNPPprlkskkWSKKFIDFIDTCLIKTYLSRPPTEQLL 284
Cdd:cd13986   235 vlsGNYSFPDNSR-------YSEELHQLVKSMLVVNPAERPSIDDLL 274
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
25-293 2.95e-24

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 105.47  E-value: 2.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYgAFikksppGNDDQ 100
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKksetLAQEEVSFFEEERDIMAKANSPWITKLQY-AF------QDSEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVkNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd05601    76 LYLVMEYHPGGDLLSLL-SRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNTF-IGTPYWMAPEVI-ACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIpRNPPPRLK---S 255
Cdd:cd05601   155 DKTVTSKMpVGTPDYIAPEVLtSMNGGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNI-MNFKKFLKfpeD 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578829925  256 KKWSKKFIDFIdTCLIKTYLSRPPTEQLLKFPF--------IRDQP 293
Cdd:cd05601   234 PKVSESAVDLI-KGLLTDAKERLGYEGLCCHPFfsgidwnnLRQTV 278
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
25-232 3.10e-24

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: 103.37  E-value: 3.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ---EINMLKKYsHHRNIATYYGAFikksppGNDDQL 101
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKlfrEVRIMKIL-NHPNIVKLFEVI------ETEKTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTD-LVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLdr 180
Cdd:cd14072    75 YLVMEYASGGEVFDyLVAHGR---MKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEF-- 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  181 TVGRR-NTFIGTPYWMAPEVIACDEnpdatYD-YRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14072   150 TPGNKlDTFCGSPPYAAPELFQGKK-----YDgPEVDVWSLGVILYTLVSGSLP 198
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
25-289 4.07e-24

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: 103.11  E-value: 4.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINM---LKKYSHHRNIATYYGAFIKKSppgnddQL 101
Cdd:cd14116     7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRReveIQSHLRHPNILRLYGYFHDAT------RV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSV-TDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd14116    81 YLILEYAPLGTVyRELQKLSK---FDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TvgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL-CDMH--PMRALFLIPRNPPPRLkskk 257
Cdd:cd14116   158 S--RRTTLCGTLDYLPPEMIE-----GRMHDEKVDLWSLGVLCYEFLVGKPPFeANTYqeTYKRISRVEFTFPDFV---- 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  258 wSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14116   227 -TEGARDLISRLLKHNPSQRPMLREVLEHPWI 257
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
25-278 4.47e-24

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: 103.96  E-value: 4.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYSHhRNIATYYGAFIKksppgnDDQ 100
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARAdcikEIDLLKQLNH-PNVIKYYASFIE------DNE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGNA--LKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd08229    99 LNIVLELADAGDLSRMIKHFKKQKrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFF 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIacDENpdaTYDYRSDIWSLGITAIEMAEGAPPLC--DMHPMRALFLIPRNPPPRLKSK 256
Cdd:cd08229   179 SSKTTAAHSLVGTPYYMSPERI--HEN---GYNFKSDIWSLGCLLYEMAALQSPFYgdKMNLYSLCKKIEQCDYPPLPSD 253
                         250       260
                  ....*....|....*....|..
gi 578829925  257 KWSKKFIDFIDTCLIKTYLSRP 278
Cdd:cd08229   254 HYSEELRQLVNMCINPDPEKRP 275
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
25-232 5.12e-24

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: 102.79  E-value: 5.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV---TEDEEEEIKQEINMLKKYSHhRNIATYYGAfiKKSPPGnddqL 101
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMkraPGDCPENIKKEVCIQKMLSH-KNVVRFYGH--RREGEF----Q 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd14069    76 YLFLEYASGGELFDKIEPDVG--MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  182 VGRR--NTFIGTPYWMAPEVIACDEnpdatydYRS---DIWSLGITAIEMAEGAPP 232
Cdd:cd14069   154 GKERllNKMCGTLPYVAPELLAKKK-------YRAepvDVWSCGIVLFAMLAGELP 202
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
31-236 6.72e-24

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: 101.80  E-value: 6.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRhVKTGQLAAIKVMDVTedeeeeiKQEINMLKKYSHhRNIATYYGAFIKkSPPgnddqLWLVMEFCGA 110
Cdd:cd14059     1 LGSGAQGAVFLGK-FRGEEVAVKKVRDEK-------ETDIKHLRKLNH-PNIIKFKGVCTQ-APC-----YCILMEYCPY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLdRTVGRRNTFIG 190
Cdd:cd14059    66 GQLYEVLR--AGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL-SEKSTKMSFAG 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578829925  191 TPYWMAPEVI---ACDEnpdatydyRSDIWSLGITAIEMAEGAPPLCDM 236
Cdd:cd14059   143 TVAWMAPEVIrnePCSE--------KVDIWSFGVVLWELLTGEIPYKDV 183
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
25-221 8.17e-24

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: 102.26  E-value: 8.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTG--QLAAIKVMDVTEDEEEEIKQ----EINMLKKYsHHRNIATYYGAFIKKSppgnd 98
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAEYTKSGlkEKVACKIIDKKKAPKDFLEKflprELEILRKL-RHPNIIQVYSIFERGS----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dQLWLVMEFCGAGSVTDLVKnTKGnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd14080    76 -KVFIFMEYAEHGDLLEYIQ-KRG-ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLC 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578829925  179 DRTVGRRN--TFIGTPYWMAPEVIAcdENPdatYD-YRSDIWSLGI 221
Cdd:cd14080   153 PDDDGDVLskTFCGSAAYAAPEILQ--GIP---YDpKKYDIWSLGV 193
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
31-232 9.40e-24

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: 102.02  E-value: 9.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKksppgNDDQLWLVMEFCGA 110
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFE-----TEDYYVFAQEYAPY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN--AEVKLVDFGVSAQLDRTVGRRNTF 188
Cdd:cd13987    76 GDLFSIIPPQVG--LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKdcRRVKLCDFGLTRRVGSTVKRVSGT 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578829925  189 IgtPYwMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd13987   154 I--PY-TAPEVCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFP 194
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
25-234 9.54e-24

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 103.47  E-value: 9.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEINMLKKYSH------------HRNIATYYGAFikk 92
Cdd:cd05574     3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLD---------KEEMIKRNKVKRvltereilatldHPFLPTLYASF--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 sppGNDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 172
Cdd:cd05574    71 ---QTSTHLCFVMDYCPGGELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  173 GVSAQLDRTVGRR-----------------------------NTFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITA 223
Cdd:cd05574   148 DLSKQSSVTPPPVrkslrkgsrrssvksieketfvaepsarsNSFVGTEEYIAPEVIKGDGHGSAV-----DWWTLGILL 222
                         250
                  ....*....|.
gi 578829925  224 IEMAEGAPPLC 234
Cdd:cd05574   223 YEMLYGTTPFK 233
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
25-287 1.19e-23

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 101.54  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD-------VTEDEEEEIKQEINMLKKYS--HHRNIATYYGAFikkspp 95
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPksrvtewAMINGPVPVPLEIALLLKASkpGVPGVIRLLDWY------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 GNDDQLWLVMEFcgAGSVTDLVK--NTKGnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT-ENAEVKLVDF 172
Cdd:cd14005    76 ERPDGFLLIMER--PEPCQDLFDfiTERG-ALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  173 GVSAQLDRTVGRrnTFIGTPYWMAPEVIACDE---NPdATydyrsdIWSLGITAIEMAEGAPPL-CDMHPMRALFLIPRn 248
Cdd:cd14005   153 GCGALLKDSVYT--DFDGTRVYSPPEWIRHGRyhgRP-AT------VWSLGILLYDMLCGDIPFeNDEQILRGNVLFRP- 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578829925  249 ppprlkskKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFP 287
Cdd:cd14005   223 --------RLSKECCDLISRCLQFDPSKRPSLEQILSHP 253
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
26-288 1.48e-23

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 101.98  E-value: 1.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEI-KQEINMLKKYSHHRNIATYYGAFIKKSPPGNDDQLwLV 104
Cdd:cd14037     6 TIEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVcKREIEIMKRLSGHKNIVGYIDSSANRSGNGVYEVL-LL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVkNTK-GNALKEDCIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd14037    85 MEYCKGGGVIDLM-NQRlQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSATTKILP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VG------------RRNTfigTPYWMAPEVIacDENPDATYDYRSDIWSLGI---------TAIEMAeGAPPLCDMHpmr 240
Cdd:cd14037   164 PQtkqgvtyveediKKYT---TLQYRAPEMI--DLYRGKPITEKSDIWALGCllyklcfytTPFEES-GQLAILNGN--- 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  241 alFLIPRNPpprlkskKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14037   235 --FTFPDNS-------RYSKRLHKLIRYMLEEDPEKRPNIYQVSYEAF 273
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
25-233 1.73e-23

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 102.39  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVK---TGQLAAIKVMDvtedeeeeiKQEINMLKKYSHHRNIATYYGAFIKKSPP------ 95
Cdd:cd05613     2 FELLKVLGTGAYGKVFLVRKVSghdAGKLYAMKVLK---------KATIVQKAKTAEHTRTERQVLEHIRQSPFlvtlhy 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 --GNDDQLWLVMEFCGAGSV-TDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 172
Cdd:cd05613    73 afQTDTKLHLILDYINGGELfTHLSQRER---FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDF 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  173 GVSAQ-LDRTVGRRNTFIGTPYWMAPEVIacdENPDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05613   150 GLSKEfLLDENERAYSFCGTIEYMAPEIV---RGGDSGHDKAVDWWSLGVLMYELLTGASPF 208
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
31-226 1.86e-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: 101.03  E-value: 1.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKvMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKksppgnDDQLWLVMEFCGA 110
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMK-ELKRFDEQRSFLKEVKLMRRLSH-PNILRFIGVCVK------DNKLNFITEYVNG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE---NAEVKLVDFGVSAQL--------D 179
Cdd:cd14065    73 GTLEELLKSMD-EQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREanrGRNAVVADFGLAREMpdektkkpD 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  180 RtvGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEM 226
Cdd:cd14065   152 R--KKRLTVVGSPYWMAPEMLRGE-----SYDEKVDVFSFGIVLCEI 191
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
21-284 2.33e-23

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: 101.29  E-value: 2.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKySHHRNIATYYGAFIKKsppgnddQ 100
Cdd:cd14151     6 PDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRK-TRHVNILLFMGYSTKP-------Q 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDL--VKNTKGNALKedcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd14151    78 LAIVTQWCEGSSLYHHlhIIETKFEMIK---LIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRN--TFIGTPYWMAPEVIAC-DENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPM-RALFLIPRNPPPRLK 254
Cdd:cd14151   155 SRWSGSHQfeQLSGSILWMAPEVIRMqDKNP---YSFQSDVYAFGIVLYELMTGQLPYSNINNRdQIIFMVGRGYLSPDL 231
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578829925  255 SKKWS---KKFIDFIDTCLIKTYLSRPPTEQLL 284
Cdd:cd14151   232 SKVRSncpKAMKRLMAECLKKKRDERPLFPQIL 264
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
24-226 2.38e-23

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: 101.81  E-value: 2.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV---TEDEEEEIKQEINMLKKYSHhRNIATYYGAFikksppGNDDQ 100
Cdd:cd07860     1 NFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLdteTEGVPSTAIREISLLKELNH-PNIVKLLDVI------HTENK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGagsvTDLVK---NTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd07860    74 LYLVFEFLH----QDLKKfmdASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEV-IACdenpdATYDYRSDIWSLGITAIEM 226
Cdd:cd07860   150 FGVPVRTYTHEVVTLWYRAPEIlLGC-----KYYSTAVDIWSLGCIFAEM 194
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
23-221 2.58e-23

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: 100.81  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   23 GIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKkYSHHRNIATYYGafIKKSPpgnd 98
Cdd:cd14079     2 GNYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNrqkiKSLDMEEKIRREIQILK-LFRHPHIIRLYE--VIETP---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTD-LVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaq 177
Cdd:cd14079    75 TDIFMVMEYVSGGELFDyIVQKGR---LSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLS-- 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 ldrTVGRRNTFI----GTPYWMAPEVIACD--ENPDAtydyrsDIWSLGI 221
Cdd:cd14079   150 ---NIMRDGEFLktscGSPNYAAPEVISGKlyAGPEV------DVWSCGV 190
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
32-232 2.61e-23

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 101.76  E-value: 2.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYSHHRNIATyygafiKKSPPG----NDDQL-W 102
Cdd:cd13989     2 GSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRErwclEVQIMKKLNHPNVVSA------RDVPPEleklSPNDLpL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGS---VTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE-NAEV--KLVDFGVSA 176
Cdd:cd13989    76 LAMEYCSGGDlrkVLNQPENCCG--LKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQgGGRViyKLIDLGYAK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  177 QLDRtvGRRNT-FIGTPYWMAPEVIACDeNPDATYDYrsdiWSLGITAIEMAEGAPP 232
Cdd:cd13989   154 ELDQ--GSLCTsFVGTLQYLAPELFESK-KYTCTVDY----WSFGTLAFECITGYRP 203
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
29-269 3.43e-23

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 101.19  E-value: 3.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEEEIKQEI---NMLkkysHHRNIATYYGAFIKKSppGNDDQLWLVM 105
Cdd:cd14056     1 KTIGKGRYGEVWLGKY--RGEKVAVKIFSSRDEDSWFRETEIyqtVML----RHENILGFIAADIKST--GSWTQLWLIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNtkgNALKEDCIAYICREILRGLAHLHAH--------KVIHRDIKGQNVLLTENAEVKLVDFG--VS 175
Cdd:cd14056    73 EYHEHGSLYDYLQR---NTLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCIADLGlaVR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQLDRTVGR--RNTFIGTPYWMAPEVIACDENPDATYDY-RSDIWSLGITAIEMA----------EGAPPLCDMHP---- 238
Cdd:cd14056   150 YDSDTNTIDipPNPRVGTKRYMAPEVLDDSINPKSFESFkMADIYSFGLVLWEIArrceiggiaeEYQLPYFGMVPsdps 229
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578829925  239 ---MRALFLIPR---NPPPRLKSKKWSKKFIDFIDTC 269
Cdd:cd14056   230 feeMRKVVCVEKlrpPIPNRWKSDPVLRSMVKLMQEC 266
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
24-289 3.89e-23

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: 100.49  E-value: 3.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSppgnddQL 101
Cdd:cd14167     4 IYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIakKALEGKETSIENEIAVLHKIKH-PNIVALDDIYESGG------HL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNtKGNALKEDCIAYICrEILRGLAHLHAHKVIHRDIKGQNVL---LTENAEVKLVDFGVSaQL 178
Cdd:cd14167    77 YLIMQLVSGGELFDRIVE-KGFYTERDASKLIF-QILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLS-KI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRaLFLIPRNPPPRLKSKKW 258
Cdd:cd14167   154 EGSGSVMSTACGTPGYVAPEVLA--QKP---YSKAVDCWSIGVIAYILLCGYPPFYDENDAK-LFEQILKAEYEFDSPYW 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  259 ---SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14167   228 ddiSDSAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
30-305 3.96e-23

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: 100.39  E-value: 3.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE----EEIKQEINmLKKYSHHRNIATYYGAFikksppGNDDQLWLVM 105
Cdd:cd14189     8 LLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKphqrEKIVNEIE-LHRDLHHKHVVKFSHHF------EDAENIYIFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR 185
Cdd:cd14189    81 ELCSRKSLAHIWKAR--HTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  186 NTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGitaiemaegapplCDMHPmralfLIPRNPPPRLKSKKWSKKFIDF 265
Cdd:cd14189   159 KTICGTPNYLAPEVLL-----RQGHGPESDVWSLG-------------CVMYT-----LLCGNPPFETLDLKETYRCIKQ 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578829925  266 IDTCLiKTYLSrPPTEQLLKfPFIRDQPTERQVRIQLKDH 305
Cdd:cd14189   216 VKYTL-PASLS-LPARHLLA-GILKRNPGDRLTLDQILEH 252
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
25-233 4.54e-23

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 100.97  E-value: 4.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK---VMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIkksppgNDDQL 101
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKrvrLDDDDEGVPSSALREICLLKEL-KHKNIVRLYDVLH------SDKKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGagsvTDLVKNTkgNALKEDCIAYICR----EILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd07839    75 TLVFEYCD----QDLKKYF--DSCNGDIDPEIVKsfmfQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARA 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDAT-YDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd07839   149 FGIPVRCYSAEVVTLWYRPPDVLF-----GAKlYSTSIDMWSAGCIFAELANAGRPL 200
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
28-285 5.18e-23

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: 100.04  E-value: 5.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV-TEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSppgnddQLWLVME 106
Cdd:cd14192     9 HEVLGGGRFGQVHKCTELSTGLTLAAKIIKVkGAKEREEVKNEINIMNQLNH-VNLIQLYDAFESKT------NLTLIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKNTKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLTENA--EVKLVDFGVSAQLDRTVGR 184
Cdd:cd14192    82 YVDGGELFDRITDESYQLTELDAILFT-RQICEGVHYLHQHYILHLDLKPENILCVNSTgnQIKIIDFGLARRYKPREKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  185 RNTFiGTPYWMAPEVIacdenpdaTYDYRS---DIWSLGITAIEMAEGAPPLC---DMHPMRALFliprnppprlkSKKW 258
Cdd:cd14192   161 KVNF-GTPEFLAPEVV--------NYDFVSfptDMWSVGVITYMLLSGLSPFLgetDAETMNNIV-----------NCKW 220
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578829925  259 ----------SKKFIDFIDTCLIKTYLSRPPTEQLLK 285
Cdd:cd14192   221 dfdaeafenlSEEAKDFISRLLVKEKSCRMSATQCLK 257
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
30-284 5.60e-23

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: 100.66  E-value: 5.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIK-VMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGA-FIKKSPPGN-DDQLWLVME 106
Cdd:cd14036     7 VIAEGGFAFVYEAQDVGTGKEYALKrLLSNEEEKNKAIIQEINFMKKLSGHPNIVQFCSAaSIGKEESDQgQAEYLLLTE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLTENAEVKLVDFGV---------- 174
Cdd:cd14036    87 LCKGQLVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSatteahypdy 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  175 --SAQLDRTVGRRNTFIGTPYWMAPEVIacDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMR---ALFLIPRNP 249
Cdd:cd14036   167 swSAQKRSLVEDEITRNTTPMYRTPEMI--DLYSNYPIGEKQDIWALGCILYLLCFRKHPFEDGAKLRiinAKYTIPPND 244
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578829925  250 pprlksKKWsKKFIDFIDTCLIKTYLSRPPTEQLL 284
Cdd:cd14036   245 ------TQY-TVFHDLIRSTLKVNPEERLSITEIV 272
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
32-284 5.69e-23

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: 99.26  E-value: 5.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHVKTGQLAAIKVMdvtedeeEEIKQEINMLKKYSHhRNIATYYGAFIKksPPgNDDqlwLVMEFCGAG 111
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKL-------LKIEKEAEILSVLSH-RNIIQFYGAILE--AP-NYG---IVTEYASYG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  112 SVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAH---KVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVgrRNTF 188
Cdd:cd14060    68 SLFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTT--HMSL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  189 IGTPYWMAPEVIACDENPDAtydyrSDIWSLGITAIEMAEGAPPLCDMHPMR-ALFLIPRNPPPRLKSkKWSKKFIDFID 267
Cdd:cd14060   146 VGTFPWMAPEVIQSLPVSET-----CDTYSYGVVLWEMLTREVPFKGLEGLQvAWLVVEKNERPTIPS-SCPRSFAELMR 219
                         250
                  ....*....|....*..
gi 578829925  268 TCLIKTYLSRPPTEQLL 284
Cdd:cd14060   220 RCWEADVKERPSFKQII 236
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
30-232 6.57e-23

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 101.14  E-value: 6.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVM---------DVtedeeEEIKQEINMLKKYSHHRNIATYYGAFikksppGNDDQ 100
Cdd:cd05570     2 VLGKGSFGKVMLAERKKTDELYAIKVLkkeviieddDV-----ECTMTEKRVLALANRHPFLTGLHACF------QTEDR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGsvtDLVKNT-KGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaQLD 179
Cdd:cd05570    71 LYFVMEYVNGG---DLMFHIqRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMC-KEG 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  180 RTVGRR-NTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05570   147 IWGGNTtSTFCGTPDYIAPEILR--EQD---YGFSVDWWALGVLLYEMLAGQSP 195
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
31-221 8.24e-23

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


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 99.22  E-value: 8.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDV-TEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKsppgndDQLWLVMEFCG 109
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCrKAKDREDVRNEIEIMNQL-RHPRLLQLYDAFETP------REMVLVMEYVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  110 AGSVTDLVKNTKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLL--TENAEVKLVDFGVSAQLDRTVGRRNT 187
Cdd:cd14103    74 GGELFERVVDDDFELTERDCILFM-RQICEGVQYMHKQGILHLDLKPENILCvsRTGNQIKIIDFGLARKYDPDKKLKVL 152
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 578829925  188 FiGTPYWMAPEVIacdenpdaTYD---YRSDIWSLGI 221
Cdd:cd14103   153 F-GTPEFVAPEVV--------NYEpisYATDMWSVGV 180
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
25-238 8.29e-23

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: 100.20  E-value: 8.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTE----DEEEEIKQEINMLKKYSHhrniatyygAFIKKSPPGNDDQ 100
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEvirlKQEQHVHNEKRVLKEVSH---------PFIIRLFWTEHDQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 --LWLVMEFCGAGSVTDLVKN----TKGNALkedciaYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd05612    74 rfLYMLMEYVPGGELFSYLRNsgrfSNSTGL------FYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGF 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  175 SAQL-DRTVgrrnTFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPLCDMHP 238
Cdd:cd05612   148 AKKLrDRTW----TLCGTPEYLAPEVIQSKGHNKAV-----DWWALGILIYEMLVGYPPFFDDNP 203
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
25-220 1.22e-22

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: 99.95  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE--IKQ----EINMLKKySHHRNIATYYGAFIKKSppgnd 98
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKdgINFtalrEIKLLQE-LKHPNIIGLLDVFGHKS----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dQLWLVMEFCGagsvTDL---VKNTKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvs 175
Cdd:cd07841    76 -NINLVFEFME----TDLekvIKDKSIVLTPADIKSYM-LMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFG-- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  176 aqLDRTVGRRNTFigtpywMAPEVIacdenpdaTYDYRS--------------DIWSLG 220
Cdd:cd07841   148 --LARSFGSPNRK------MTHQVV--------TRWYRApellfgarhygvgvDMWSVG 190
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
25-242 2.03e-22

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: 98.10  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHvKTGQLAAIKVMDVTEDEEEE----IKQEINMLKKYSHhRNIATYYGAFikksppGNDDQ 100
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARD-SSGRLVAIKSIRKDRIKDEQdllhIRREIEIMSSLNH-PHIISVYEVF------ENSSK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaQLDR 180
Cdd:cd14161    77 IVIVMEYASRGDLYDYISERQ--RLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLS-NLYN 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPPLcDMHPMRAL 242
Cdd:cd14161   154 QDKFLQTYCGSPLYASPEIV----NGRPYIGPEVDSWSLGVLLYILVHGTMPF-DGHDYKIL 210
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
27-284 2.15e-22

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: 98.95  E-value: 2.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKySHHRNIATYYGAFIKksppgndDQLWLVME 106
Cdd:cd14149    16 LSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRK-TRHVNILLFMGYMTK-------DNLAIVTQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDL--VKNTKGNALKedcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGR 184
Cdd:cd14149    88 WCEGSSLYKHlhVQETKFQMFQ---LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  185 RNT--FIGTPYWMAPEVIAC-DENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPM-RALFLIPR---NPPPRLKSKK 257
Cdd:cd14149   165 QQVeqPTGSILWMAPEVIRMqDNNP---FSFQSDVYSYGIVLYELMTGELPYSHINNRdQIIFMVGRgyaSPDLSKLYKN 241
                         250       260
                  ....*....|....*....|....*..
gi 578829925  258 WSKKFIDFIDTCLIKTYLSRPPTEQLL 284
Cdd:cd14149   242 CPKAMKRLVADCIKKVKEERPLFPQIL 268
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
25-231 2.17e-22

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


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 98.90  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKV----MDVTEDEEEEIKqEINMLKKYsHHRNIATYYGAFIKksppgnDDQ 100
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKirleTEDEGVPSTAIR-EISLLKEL-NHPNIVRLLDVVHS------ENK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGagsvTDLVK---NTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvsaq 177
Cdd:cd07835    73 LYLVFEFLD----LDLKKymdSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFG---- 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  178 LDRTVG---RRNTF-IGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07835   145 LARAFGvpvRTYTHeVVTLWYRAPEILL----GSKHYSTPVDIWSVGCIFAEMVTRRP 198
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
25-291 2.78e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 104.43  E-value: 2.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQL---AAIKVMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSppgnDDQL 101
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFfcwKAISYRGLKEREKSQLVIEVNVMRELKH-KNIVRYIDRFLNKA----NQKL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGsvtDLVKNTKG-----NALKEDCIAYICREILRGLAHLH-------AHKVIHRDIKGQNVLLTENAE--- 166
Cdd:PTZ00266   90 YILMEFCDAG---DLSRNIQKcykmfGKIEEHAIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLSTGIRhig 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  167 --------------VKLVDFGVSAQLDrTVGRRNTFIGTPYWMAPEVIAcdeNPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:PTZ00266  167 kitaqannlngrpiAKIGDFGLSKNIG-IESMAHSCVGTPYYWSPELLL---HETKSYDDKSDMWALGCIIYELCSGKTP 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  233 LCDMHPMRALFL-IPRNPPPRLKSKkwSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRD 291
Cdd:PTZ00266  243 FHKANNFSQLISeLKRGPDLPIKGK--SKELNILIKNLLNLSAKERPSALQCLGYQIIKN 300
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
24-232 3.39e-22

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: 98.00  E-value: 3.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK---QEINMLKKYSHHRNIatyYGAFIKKSPpgndDQ 100
Cdd:cd14097     2 IYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKlleREVDILKHVNHAHII---HLEEVFETP----KR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVkNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVL----LTENAE---VKLVDFG 173
Cdd:cd14097    75 MYLVMELCEDGELKELL-LRKGF-FSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILvkssIIDNNDklnIKVTDFG 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578829925  174 VSAQldrTVGRRNTFI----GTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14097   153 LSVQ---KYGLGEDMLqetcGTPIYMAPEVISAHG-----YSQQCDIWSIGVIMYMLLCGEPP 207
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
31-231 3.66e-22

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: 99.64  E-value: 3.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLK--KYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEFC 108
Cdd:cd07880    23 VGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRllKHMKHENVIGLLDVFTPDLSLDRFHDFYLVMPFM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GagsvTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVgrrNTF 188
Cdd:cd07880   103 G----TDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSEM---TGY 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578829925  189 IGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07880   176 VVTRWYRAPEVILNWMH----YTQTVDIWSVGCIMAEMLTGKP 214
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
111-294 3.68e-22

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


Pssm-ID: 214801  Cd Length: 176  Bit Score: 95.16  E-value: 3.68e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    111 GSVTDLVKnTKGNALKEDCIAYICREILRGLahlhahKVIHRDIKGQNVLLTENAEVKLvdFGVSAQLDRTVGRrntfiG 190
Cdd:smart00750    1 VSLADILE-VRGRPLNEEEIWAVCLQCLGAL------RELHRQAKSGNILLTWDGLLKL--DGSVAFKTPEQSR-----P 66
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    191 TPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKS------KKWS--KKF 262
Cdd:smart00750   67 DPYFMAPEVIQGQS-----YTEKADIYSLGITLYEALDYELPYNEERELSAILEILLNGMPADDPrdrsnlEGVSaaRSF 141
                           170       180       190
                    ....*....|....*....|....*....|..
gi 578829925    263 IDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPT 294
Cdd:smart00750  142 EDFMRLCASRLPQRREAANHYLAHCRALFAET 173
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-232 4.14e-22

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 98.53  E-value: 4.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVM----DVTedeeeeikQEINMLKKYSHHRNIATYYGAFikksppgnDDQL--W 102
Cdd:cd14092    12 EALGDGSFSVCRKCVHKKTGQEFAVKIVsrrlDTS--------REVQLLRLCQGHPNIVKLHEVF--------QDELhtY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVsAQLD 179
Cdd:cd14092    76 LVMELLRGGELLERIR--KKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTdedDDAEIKIVDFGF-ARLK 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIACDENPDaTYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14092   153 PENQPLKTPCFTLPYAAPEVLKQALSTQ-GYDESCDLWSLGVILYTMLSGQVP 204
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
29-289 4.63e-22

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: 97.29  E-value: 4.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDV-TEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKsppgNDdqLWLVMEF 107
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKArSQKEKEEVKNEIEVMNQLNH-ANLIQLYDAFESR----ND--IVLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDRTVGRR 185
Cdd:cd14193    83 VDGGELFDRIIDENYNLTELDTILFI-KQICEGIQYMHQMYILHLDLKPENILCVsrEANQVKIIDFGLARRYKPREKLR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  186 NTFiGTPYWMAPEVIacdenpdaTYDYRS---DIWSLGITAIEMAEGAPPLCDMHPMRAL--FLIPRNPPPRLKSKKWSK 260
Cdd:cd14193   162 VNF-GTPEFLAPEVV--------NYEFVSfptDMWSLGVIAYMLLSGLSPFLGEDDNETLnnILACQWDFEDEEFADISE 232
                         250       260
                  ....*....|....*....|....*....
gi 578829925  261 KFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14193   233 EAKDFISKLLIKEKSWRMSASEALKHPWL 261
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
13-287 4.87e-22

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 101.48  E-value: 4.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   13 IDLSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV---TEDEEEEIKQEINMLKKYSHHrNIATYYGAF 89
Cdd:PTZ00283   22 KDEATAKEQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMegmSEADKNRAQAEVCCLLNCDFF-SIVKCHEDF 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   90 IKKSP--PGNDDQLWLVMEFCGAGSVTDLVKN--TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA 165
Cdd:PTZ00283  101 AKKDPrnPENVLMIALVLDYANAGDLRQEIKSraKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  166 EVKLVDFGVSAQLDRT----VGRrnTFIGTPYWMAPEViaCDENPdatYDYRSDIWSLGITAIEMAEGAPPL--CDMHPM 239
Cdd:PTZ00283  181 LVKLGDFGFSKMYAATvsddVGR--TFCGTPYYVAPEI--WRRKP---YSKKADMFSLGVLLYELLTLKRPFdgENMEEV 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  240 RALFLIPR-NP-PPRLkskkwSKKFIDFIDTCLIKTYLSRPPTEQLLKFP 287
Cdd:PTZ00283  254 MHKTLAGRyDPlPPSI-----SPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
27-232 6.28e-22

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: 96.94  E-value: 6.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGRHVKTGQLAaIKVMDVTEDEEEEIKQEINMLKKYSHHRnIATYYGAFIKKSPpgnddqLWLVME 106
Cdd:cd05112     8 FVQEIGSGQFGLVHLGYWLNKDKVA-IKTIREGAMSEEDFIEEAEVMMKLSHPK-LVQLYGVCLEQAP------ICLVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKNTKGNALKEDCIAyICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaqldRTV--GR 184
Cdd:cd05112    80 FMEHGCLSDYLRTQRGLFSAETLLG-MCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMT----RFVldDQ 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  185 RNTFIGTPY---WMAPEVIACdenpdATYDYRSDIWSLGITAIEM-AEGAPP 232
Cdd:cd05112   155 YTSSTGTKFpvkWSSPEVFSF-----SRYSSKSDVWSFGVLMWEVfSEGKIP 201
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
32-226 6.38e-22

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: 97.34  E-value: 6.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ--EINMLKKYSHHRNIATYYgAFIKKSPPGNddqLWLVMEFCg 109
Cdd:cd07831     8 GEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNNlrEIQALRRLSPHPNILRLI-EVLFDRKTGR---LALVFELM- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  110 AGSVTDLVKNTKGnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENaEVKLVDFGvSAqldRTVGRRNTF- 188
Cdd:cd07831    83 DMNLYELIKGRKR-PLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG-SC---RGIYSKPPYt 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578829925  189 --IGTPYWMAPEVIACdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd07831   157 eyISTRWYRAPECLLT----DGYYGPKMDIWAVGCVFFEI 192
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
29-289 7.88e-22

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: 96.65  E-value: 7.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVM-------DVtedeEEEIKQEINMLKKYSHHRNIATYYGAFIKKSppgnddQL 101
Cdd:cd14106    14 TPLGRGKFAVVRKCIHKETGKEYAAKFLrkrrrgqDC----RNEILHEIAVLELCKDCPRVVNLHEVYETRS------EL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNtkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE---NAEVKLVDFGVSAQL 178
Cdd:cd14106    84 ILILELAAGGELQTLLDE--EECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSefpLGDIKLCDFGISRVI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNtFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPL---------CDMHPMRALFliprnp 249
Cdd:cd14106   162 GEGEEIRE-ILGTPDYVAPEILSYEPISLAT-----DMWSIGVLTYVLLTGHSPFggddkqetfLNISQCNLDF------ 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578829925  250 pPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14106   230 -PEELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
25-231 8.01e-22

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: 97.82  E-value: 8.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKV--MD-------VTEDeeeeikQEINMLKKYsHHRNIATyygafIKKSPP 95
Cdd:cd07845     9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKvrMDnerdgipISSL------REITLLLNL-RHPNIVE-----LKEVVV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 GND-DQLWLVMEFC--GAGSVTDLVKNTkgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 172
Cdd:cd07845    77 GKHlDSIFLVMEYCeqDLASLLDNMPTP----FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADF 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  173 GVSAQLDRTVGRRNTFIGTPYWMAPEVIACDEnpdaTYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07845   153 GLARTYGLPAKPMTPKVVTLWYRAPELLLGCT----TYTTAIDMWAVGCILAELLAHKP 207
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
24-235 1.01e-21

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: 96.29  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE--EEEIKQEINMLKKYSHhRNIATYYGAFIKKSppgnddQL 101
Cdd:cd14083     4 KYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKgkEDSLENEIAVLRKIKH-PNIVQLLDIYESKS------HL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKnTKGNALKEDCiAYICREILRGLAHLHAHKVIHRDIKGQNVL---LTENAEVKLVDFGVSAQL 178
Cdd:cd14083    77 YLVMELVTGGELFDRIV-EKGSYTEKDA-SHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSKME 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  179 DRTVgrRNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd14083   155 DSGV--MSTACGTPGYVAPEVLA--QKP---YGKAVDCWSIGVISYILLCGYPPFYD 204
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
29-227 1.04e-21

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: 97.01  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEEEIKQEInmlkkYS----HHRNIATYYGAfiKKSPPGNDDQLWLV 104
Cdd:cd14053     1 EIKARGRFGAVWKAQY--LNRLVAVKIFPLQEKQSWLTEREI-----YSlpgmKHENILQFIGA--EKHGESLEAEYWLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNtkgNALKEDCIAYICREILRGLAHLH--------AHK--VIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd14053    72 TEFHERGSLCDYLKG---NVISWNELCKIAESMARGLAYLHedipatngGHKpsIAHRDFKSKNVLLKSDLTACIADFGL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  175 SAQLDRTVGRRNTF--IGTPYWMAPEVI--ACDENPDATydYRSDIWSLGITAIEMA 227
Cdd:cd14053   149 ALKFEPGKSCGDTHgqVGTRRYMAPEVLegAINFTRDAF--LRIDMYAMGLVLWELL 203
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
25-234 1.06e-21

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 98.95  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdvtEDEEEEIKQEINMLkkySHHRNIAT----------YYgAFikksp 94
Cdd:cd05600    13 FQILTQVGQGGYGSVFLARKKDTGEICALKIM---KKKVLFKLNEVNHV---LTERDILTttnspwlvklLY-AF----- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   95 pGNDDQLWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd05600    81 -QDPENVYLAMEYVPGGDFRTLLNNSG--ILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  175 S----------------------AQLDRTVG-RRNTF--------------IGTPYWMAPEVIACDEnpdatYDYRSDIW 217
Cdd:cd05600   158 AsgtlspkkiesmkirleevkntAFLELTAKeRRNIYramrkedqnyansvVGSPDYMAPEVLRGEG-----YDLTVDYW 232
                         250
                  ....*....|....*..
gi 578829925  218 SLGITAIEMAEGAPPLC 234
Cdd:cd05600   233 SLGCILFECLVGFPPFS 249
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
31-286 1.13e-21

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: 96.57  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRhVKTGQLAAIKVMDVTEDEEEE--IKQEINMLKKySHHRNIATYYGAFIKKSPPGnddqlwLVMEFC 108
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMNCAASKkeFLTELEMLGR-LRHPNLVRLLGYCLESDEKL------LVYEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTD-LVKNTKGNALKEDCIAYICREILRGLAHLH---AHKVIHRDIKGQNVLLTENAEVKLVDFGVS--AQLDRTV 182
Cdd:cd14066    73 PNGSLEDrLHCHKGSPPLPWPQRLKIAKGIARGLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLArlIPPSESV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIGTPYWMAPEviacdenpdatYDY------RSDIWSLGITAIEMAEGAPPLcDMHPMRALFLiprnpppRLKS- 255
Cdd:cd14066   153 SKTSAVKGTIGYLAPE-----------YIRtgrvstKSDVYSFGVVLLELLTGKPAV-DENRENASRK-------DLVEw 213
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578829925  256 --KKWSKKFIDFIDTCLIKTYLSRPptEQLLKF 286
Cdd:cd14066   214 veSKGKEELEDILDKRLVDDDGVEE--EEVEAL 244
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
30-232 1.21e-21

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: 96.31  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHV---KTGQLAAIKVMDVTEDEEEEIKQEINM-----LKKYSHHRNIATYYGAFikksppGNDDQL 101
Cdd:cd05583     1 VLGTGAYGKVFLVRKVgghDAGKLYAMKVLKKATIVQKAKTAEHTMterqvLEAVRQSPFLVTLHYAF------QTDAKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSV-TDLvkNTKGNALKEDCIAYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ-LD 179
Cdd:cd05583    75 HLILDYVNGGELfTHL--YQREHFTESEVRIYIG-EIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEfLP 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIacdENPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05583   152 GENDRAYSFCGTIEYMAPEVV---RGGSDGHDKAVDWWSLGVLTYELLTGASP 201
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
25-289 2.12e-21

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: 95.34  E-value: 2.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK-VMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikksppGNDDQLWL 103
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERATGNNFAAKfIMTPHESDKETVRKEIQIMNQL-HHPKLINLHDAF------EDDNEMVL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNtKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDRT 181
Cdd:cd14114    77 ILEFLSGGELFERIAA-EHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDPK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTfIGTPYWMAPEVIacDENPDATYdyrSDIWSLGITAIEMAEGAPPLCDMHPMRALflipRNppprLKSKKW--- 258
Cdd:cd14114   156 ESVKVT-TGTAEFAAPEIV--EREPVGFY---TDMWAVGVLSYVLLSGLSPFAGENDDETL----RN----VKSCDWnfd 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578829925  259 -------SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14114   222 dsafsgiSEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
31-236 2.23e-21

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: 95.20  E-value: 2.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEEEIKqEINMLKKYSHhRNIATYYGAFIKKSPPgnddqlWLVMEFCGA 110
Cdd:cd14058     1 VGRGSFGVVCKARW--RNQIVAVKIIESESEKKAFEV-EVRQLSRVDH-PNIIKLYGACSNQKPV------CLVMEYAEG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKN-------TKGNALKedciayICREILRGLAHLHAHK---VIHRDIKGQNVLLTENAEV-KLVDFGVSA--Q 177
Cdd:cd14058    71 GSLYNVLHGkepkpiyTAAHAMS------WALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVlKICDFGTACdiS 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  178 LDRTVGRrntfiGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDM 236
Cdd:cd14058   145 THMTNNK-----GSAAWMAPEVFE-----GSKYSEKCDVFSWGIILWEVITRRKPFDHI 193
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
25-231 2.63e-21

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: 95.86  E-value: 2.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ---EINMLKKYSHHRNIATYYGAFikksPPGNDdqL 101
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQalrEIKALQACQGHPYVVKLRDVF----PHGTG--F 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGaGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd07832    76 VLVFEYML-SSLSEVLRDEE-RPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  182 VGRRNTF-IGTPYWMAPEVIACDEnpdaTYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07832   154 DPRLYSHqVATRWYRAPELLYGSR----KYDEGVDLWAVGCIFAELLNGSP 200
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
24-311 2.81e-21

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 96.07  E-value: 2.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV------TEDEEEEIKQEI---NMLKKYSHHRNIATYygafikksp 94
Cdd:cd14094     4 VYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVakftssPGLSTEDLKREAsicHMLKHPHIVELLETY--------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   95 pGNDDQLWLVMEFC-GAGSVTDLVKN-TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL--TEN-AEVKL 169
Cdd:cd14094    75 -SSDGMLYMVFEFMdGADLCFEIVKRaDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENsAPVKL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  170 VDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLC----DMHPMRALFLI 245
Cdd:cd14094   154 GGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREP-----YGKPVDVWGCGVILFILLSGCLPFYgtkeRLFEGIIKGKY 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  246 PRNPPprlKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQvRIQLKDHIDRSRK 311
Cdd:cd14094   229 KMNPR---QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAY-RIHLPETVEQLRK 290
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
26-285 3.01e-21

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 95.11  E-value: 3.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGR-HvktGQlAAIKVMDVTEDEEEEI---KQEINMLKKySHHRNIATYYGAFIKksPPgnddQL 101
Cdd:cd14063     3 EIKEVIGKGRFGRVHRGRwH---GD-VAIKLLNIDYLNEEQLeafKEEVAAYKN-TRHDNLVLFMGACMD--PP----HL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLtENAEVKLVDFGVS--AQLD 179
Cdd:cd14063    72 AIVTSLCKGRTLYSLIHERKEK-FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDFGLFslSGLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFIGTPYW---MAPEVIA-----CDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPP 251
Cdd:cd14063   150 QPGRREDTLVIPNGWlcyLAPEIIRalspdLDFEESLPFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGKKQ 229
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  252 RLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLK 285
Cdd:cd14063   230 SLSQLDIGREVKDILMQCWAYDPEKRPTFSDLLR 263
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
31-226 3.02e-21

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 95.27  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIK-VMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKksppgnDDQLWLVMEFCG 109
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKeLIRFDEEAQRNFLKEVKVMRSL-DHPNVLKFIGVLYK------DKKLNLITEYIP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  110 AGSVTDLVKNtKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD---------- 179
Cdd:cd14154    74 GGTLKDVLKD-MARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVeerlpsgnms 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  180 -----RTVG-----RRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd14154   153 psetlRHLKspdrkKRYTVVGNPYWMAPEMLN-----GRSYDEKVDIFSFGIVLCEI 204
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
22-232 3.10e-21

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 94.79  E-value: 3.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   22 AGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVT---EDEEEEIKQEINMLKKYShHRNIATYYGAFikksppgnD 98
Cdd:cd14074     2 AGLYDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTkldDVSKAHLFQEVRCMKLVQ-HPNVVRLYEVI--------D 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQ--LWLVMEFCGAGSVTDLVKNtKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE-VKLVDFGVS 175
Cdd:cd14074    73 TQtkLYLILELGDGGDMYDYIMK-HENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGlVKLTDFGFS 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  176 AQLDRtvGRR-NTFIGTPYWMAPEVIACDEnpdatYDYRS-DIWSLGITAIEMAEGAPP 232
Cdd:cd14074   152 NKFQP--GEKlETSCGSLAYSAPEILLGDE-----YDAPAvDIWSLGVILYMLVCGQPP 203
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
31-254 3.98e-21

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: 94.46  E-value: 3.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKvMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSppgnddQLWLVMEFCGA 110
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALK-MNTLSSNRANMLREVQLMNRLSH-PNILRFMGVCVHQG------QLHALTEYING 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL--TENAEVKLV-DFGVSAQLDrTVGRRN- 186
Cdd:cd14155    73 GNLEQLLDSNE--PLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYTAVVgDFGLAEKIP-DYSDGKe 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  187 --TFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALF---------LIPRNPPPRLK 254
Cdd:cd14155   150 klAVVGSPYWMAPEVLR-----GEPYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFgldydafqhMVGDCPPDFLQ 223
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
15-232 4.05e-21

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 96.68  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   15 LSALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEinMLKK-----YSHHRNIATY---- 85
Cdd:cd05596    18 ITKLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLS---------KFE--MIKRsdsafFWEERDIMAHanse 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   86 -----YGAFikksppgNDDQ-LWLVMEFCGAGsvtDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNV 159
Cdd:cd05596    87 wivqlHYAF-------QDDKyLYMVMDYMPGG---DLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNM 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  160 LLTENAEVKLVDFGVSAQLDRT-VGRRNTFIGTPYWMAPEVIAcDENPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05596   157 LLDASGHLKLADFGTCMKMDKDgLVRSDTAVGTPDYISPEVLK-SQGGDGVYGRECDWWSVGVFLYEMLVGDTP 229
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
26-232 4.34e-21

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 94.70  E-value: 4.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKySHHRNIATYYGaFIKKSppgnddQLWLVM 105
Cdd:cd14150     3 SMLKRIGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRK-TRHVNILLFMG-FMTRP------NFAIIT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDL--VKNTKGNALKEDCIAyicREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVG 183
Cdd:cd14150    75 QWCEGSSLYRHlhVTETRFDTMQLIDVA---RQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  184 RRNTF--IGTPYWMAPEVIAC-DENPdatYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14150   152 SQQVEqpSGSILWMAPEVIRMqDTNP---YSFQSDVYAYGVVLYELMSGTLP 200
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
23-289 4.41e-21

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: 94.44  E-value: 4.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   23 GIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYS---------------HHRNIATYYG 87
Cdd:cd14077     1 GNWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEISrdirtireaalssllNHPHICRLRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   88 AFIKKSppgnddQLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 167
Cdd:cd14077    81 FLRTPN------HYYMLFEYVDGGQLLDYI--ISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  168 KLVDFGVSAQLDRTvGRRNTFIGTPYWMAPEVIacDENPdatydY---RSDIWSLGITAIEMAEGAPPLCDMHpMRALFL 244
Cdd:cd14077   153 KIIDFGLSNLYDPR-RLLRTFCGSLYFAAPELL--QAQP-----YtgpEVDVWSFGVVLYVLVCGKVPFDDEN-MPALHA 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  245 -IPRNpppRLKSKKW-SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14077   224 kIKKG---KVEYPSYlSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
25-233 4.46e-21

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: 96.14  E-value: 4.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVK---TGQLAAIKVMD-----VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFikksppG 96
Cdd:cd05614     2 FELLKVLGTGAYGKVFLVRKVSghdANKLYAMKVLRkaalvQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAF------Q 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 NDDQLWLVMEFCGAGSV-TDLVKNtkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd05614    76 TDAKLHLILDYVSGGELfTHLYQR---DHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  176 AQ-LDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYrsdiWSLGITAIEMAEGAPPL 233
Cdd:cd05614   153 KEfLTEEKERTYSFCGTIEYMAPEIIRGKSGHGKAVDW----WSLGILMFELLTGASPF 207
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
69-288 4.57e-21

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: 94.35  E-value: 4.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   69 EINMLKKYSHhRNIATYYGAFIKKSPPGNDDQLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHK 148
Cdd:cd14012    48 ELESLKKLRH-PNLVSYLAFSIERRGRSDGWKVYLLTEYAPGGSLSELL--DSVGSVPLDTARRWTLQLLEALEYLHRNG 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  149 VIHRDIKGQNVLLTENAE---VKLVDFGVSAQLDRTVGRRNTFIGTP-YWMAPEVIAcdenPDATYDYRSDIWSLGITAI 224
Cdd:cd14012   125 VVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDMCSRGSLDEFKQtYWLPPELAQ----GSKSPTRKTDVWDLGLLFL 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  225 EMAEGAPPLCDMHPMRALFLIPRNPPPrlkskkwskkFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14012   201 QMLFGLDVLEKYTSPNPVLVSLDLSAS----------LQDFLSKCLSLDPKKRPTALELLPHEF 254
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
25-232 4.89e-21

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 95.88  E-value: 4.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEinMLKK--------------YSHHRNIATYYGAFi 90
Cdd:cd05597     3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILN---------KWE--MLKRaetacfreerdvlvNGDRRWITKLHYAF- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   91 kksppGNDDQLWLVMEF-CGAGSVTDLVKNtkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 169
Cdd:cd05597    71 -----QDENYLYLVMDYyCGGDLLTLLSKF--EDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRL 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  170 VDFGVSAQL--DRTVgRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05597   144 ADFGSCLKLreDGTV-QSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETP 207
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
39-250 6.52e-21

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


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 95.71  E-value: 6.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   39 VYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSppgnddQLWLVMEFCGAGSVTDL 116
Cdd:cd08226    16 VYLARHTPTGTLVTVKItnLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGS------WLWVISPFMAYGSARGL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  117 VKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTvGRRNTFI------- 189
Cdd:cd08226    90 LKTYFPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMVTN-GQRSKVVydfpqfs 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  190 -GTPYWMAPEVIACDENpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPP 250
Cdd:cd08226   169 tSVLPWLSPELLRQDLH---GYNVKSDIYSVGITACELARGQVPFQDMRRTQMLLQKLKGPP 227
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
29-227 7.20e-21

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: 94.43  E-value: 7.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRhvKTGQLAAIKVMDVTEDEEEEIKQEIN---MLKkyshHRNIAtyygAFIKKSPPGNDD--QLWL 103
Cdd:cd13998     1 EVIGKGRFGEVWKAS--LKNEPVAVKIFSSRDKQSWFREKEIYrtpMLK----HENIL----QFIAADERDTALrtELWL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKntkGNALKEDCIAYICREILRGLAHLHA-------HK--VIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd13998    71 VTAFHPNGSL*DYLS---LHTIDWVSLCRLALSVARGLAHLHSeipgctqGKpaIAHRDLKSKNILVKNDGTCCIADFGL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  175 SAQLDRTVGR----RNTFIGTPYWMAPEVIACDENPDATYDY-RSDIWSLGITAIEMA 227
Cdd:cd13998   148 AVRLSPSTGEednaNNGQVGTKRYMAPEVLEGAINLRDFESFkRVDIYAMGLVLWEMA 205
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
29-233 7.31e-21

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: 95.11  E-value: 7.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVmdVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFikksppgnDDQL--WLVME 106
Cdd:cd14179    13 KPLGEGSFSICRKCLHKKTNQEYAVKI--VSKRMEANTQREIAALKLCEGHPNIVKLHEVY--------HDQLhtFLVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVSaqldRTVG 183
Cdd:cd14179    83 LLKGGELLERIK--KKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTdesDNSEIKIIDFGFA----RLKP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  184 RRNTFIGTP----YWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14179   157 PDNQPLKTPcftlHYAAPELLNYN-----GYDESCDLWSLGVILYTMLSGQVPF 205
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
20-226 7.51e-21

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: 94.74  E-value: 7.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIK--VMD-------VTEDeeeeikQEINMLKKYSHHrNIATYYGAFI 90
Cdd:cd07865     9 DEVSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKkvLMEnekegfpITAL------REIKILQLLKHE-NVVNLIEICR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   91 KKSPPGNDD--QLWLVMEFCgAGSVTDLVKNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVK 168
Cdd:cd07865    82 TKATPYNRYkgSIYLVFEFC-EHDLAGLLSNKNVK-FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLK 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  169 LVDFGVS-AQLDRTVGRRNTFIG---TPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEM 226
Cdd:cd07865   160 LADFGLArAFSLAKNSQPNRYTNrvvTLWYRPPELLLGERD----YGPPIDMWGAGCIMAEM 217
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
25-232 8.42e-21

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: 93.54  E-value: 8.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE--EEEIKQEINMLKKYSHHrNIATYYGAFikksppGNDDQLW 102
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKgkEHMIENEVAILRRVKHP-NIVQLIEEY------DTDTELY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE----VKLVDFGVSAQL 178
Cdd:cd14095    75 LVMELVKGGDLFDAI--TSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDgsksLKLADFGLATEV 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  179 DRTVgrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLG-ITAIeMAEGAPP 232
Cdd:cd14095   153 KEPL---FTVCGTPTYVAPEILA-----ETGYGLKVDIWAAGvITYI-LLCGFPP 198
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
30-232 8.51e-21

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: 93.61  E-value: 8.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHvkTGQLAAIKVMDVTE-----DEEEEIKQEINMLKKYsHHRNIATYYGAFIKksPPgnddQLWLV 104
Cdd:cd14061     1 VIGVGGFGKVYRGIW--RGEEVAVKAARQDPdedisVTLENVRQEARLFWML-RHPNIIALRGVCLQ--PP----NLCLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSvtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHK---VIHRDIKGQNVLLTE--------NAEVKLVDFG 173
Cdd:cd14061    72 MEYARGGA---LNRVLAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFG 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  174 VSAQLDRTVgrRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14061   149 LAREWHKTT--RMSAAGTYAWMAPEVIK-----SSTFSKASDVWSYGVLLWELLTGEVP 200
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
32-226 1.15e-20

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 93.60  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHV----KTGQLAAIKVMDVTEDEEEE--IKQEINMLKKYsHHRNIATYYGafIKKSPPGNDdqLWLVM 105
Cdd:cd05038    13 GEGHFGSVELCRYDplgdNTGEQVAVKSLQPSGEEQHMsdFKREIEILRTL-DHEYIVKYKG--VCESPGRRS--LRLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKGNALKEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS--AQLDRTVG 183
Cdd:cd05038    88 EYLPSGSLRDYLQRHRDQIDLKRLLLF-ASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAkvLPEDKEYY 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578829925  184 RRNTFIGTP-YWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd05038   167 YVKEPGESPiFWYAPECLR-----ESRFSSASDVWSFGVTLYEL 205
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
30-253 1.20e-20

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: 94.78  E-value: 1.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHV---KTGQLAAIKVMD----VTEDEEEE-IKQEINMLKKYSHHRNIATYYgAFikksppGNDDQL 101
Cdd:cd05584     3 VLGKGGYGKVFQVRKTtgsDKGKIFAMKVLKkasiVRNQKDTAhTKAERNILEAVKHPFIVDLHY-AF------QTGGKL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKnTKGnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd05584    76 YLILEYLSGGELFMHLE-REG-IFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  182 VGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR---NPPPRL 253
Cdd:cd05584   154 GTVTHTFCGTIEYMAPEILT-----RSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKgklNLPPYL 223
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
28-283 1.28e-20

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: 94.64  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFikksppGNDDQLWL 103
Cdd:cd05604     1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQkkviLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSF------QTTDKLYF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS----AQLD 179
Cdd:cd05604    75 VLDFVNGGEL--FFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCkegiSNSD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVgrrnTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLC--DMHPMRALFL-IPRNPPPRLKSK 256
Cdd:cd05604   153 TTT----TFCGTPEYLAPEVIR--KQP---YDNTVDWWCLGSVLYEMLYGLPPFYcrDTAEMYENILhKPLVLRPGISLT 223
                         250       260
                  ....*....|....*....|....*..
gi 578829925  257 KWSkkfidfidtcLIKTYLSRPPTEQL 283
Cdd:cd05604   224 AWS----------ILEELLEKDRQLRL 240
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
31-231 1.35e-20

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: 94.56  E-value: 1.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIK-VMD--VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSppgndDQLWLVMEF 107
Cdd:cd07856    18 VGMGAFGLVCSARDQLTGQNVAVKkIMKpfSTPVLAKRTYRELKLLKHL-RHENIISLSDIFISPL-----EDIYFVTEL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGagsvTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVgrrNT 187
Cdd:cd07856    92 LG----TDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQM---TG 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578829925  188 FIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07856   165 YVSTRYYRAPEIMLTWQK----YDVEVDIWSAGCIFAEMLEGKP 204
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
25-312 1.54e-20

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: 94.55  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK-VMDV---------TEdeeeeikQEINMLKKYSHHRNIATYYgAFIKKSp 94
Cdd:cd07852     9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDAfrnatdaqrTF-------REIMFLQELNDHPNIIKLL-NVIRAE- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   95 pgNDDQLWLVMEFCGagsvTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd07852    80 --NDKDIYLVFEYME----TDLHAVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  175 SAQLDRTVGRRNTFIGTPY----WM-APEV-IACdenpdATYDYRSDIWSLGITAIEM---------------------A 227
Cdd:cd07852   154 ARSLSQLEEDDENPVLTDYvatrWYrAPEIlLGS-----TRYTKGVDMWSVGCILGEMllgkplfpgtstlnqlekiieV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  228 EGAPPLCDMHPMRALF---LIPRNPPPRLKS-----KKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR------DQP 293
Cdd:cd07852   229 IGRPSAEDIESIQSPFaatMLESLPPSRPKSldelfPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAqfhnpaDEP 308
                         330       340
                  ....*....|....*....|
gi 578829925  294 T-ERQVRIQLKDHIDRSRKK 312
Cdd:cd07852   309 SlPGPIVIPLDDNKKLTVDE 328
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
100-289 1.55e-20

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: 93.08  E-value: 1.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA---EVKLVDFGVSA 176
Cdd:cd14197    83 EMILVLEYAAGGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSR 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  177 QLDRTVGRRNtFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPLCDMHPMRALFLIprnppPRLKSK 256
Cdd:cd14197   163 ILKNSEELRE-IMGTPEYVAPEILSYEPISTAT-----DMWSIGVLAYVMLTGISPFLGDDKQETFLNI-----SQMNVS 231
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578829925  257 KWSKKF-------IDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14197   232 YSEEEFehlsesaIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
25-289 1.63e-20

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: 92.60  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKsppgndDQLWLV 104
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRH-TNIIQLIEVFETK------ERVYMV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKnTKGNALKEDCiAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE---NAEVKLVDFGVSAQldRT 181
Cdd:cd14087    76 MELATGGELFDRII-AKGSFTERDA-TRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHpgpDSKIMITDFGLAST--RK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRN---TFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR-----NPPPRL 253
Cdd:cd14087   152 KGPNClmkTTCGTPEYIAPEILL--RKP---YTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRakysySGEPWP 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  254 KSKKWSKkfiDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14087   227 SVSNLAK---DFIDRLLTVNPGERLSATQALKHPWI 259
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
31-235 1.70e-20

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: 92.92  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYsHHRNIATYYGAFikkspPGNDDQLWLVME 106
Cdd:cd14165     9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKflprELEILARL-NHKSIIKTYEIF-----ETSDGKVYIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR- 185
Cdd:cd14165    83 LGVQGDLLEFIK--LRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRi 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  186 ---NTFIGTPYWMAPEVIAcdenpDATYDYR-SDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd14165   161 vlsKTFCGSAAYAAPEVLQ-----GIPYDPRiYDIWSLGVILYIMVCGSMPYDD 209
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
25-231 1.74e-20

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: 93.25  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE---EEIKQEINMLKKYsHHRNIATYYGAFIKKSppgnddQL 101
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvpSTAIREISLLKEL-QHPNIVCLEDVLMQEN------RL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGagsvTDLVKNT----KGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvsaq 177
Cdd:cd07861    75 YLVFEFLS----MDLKKYLdslpKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFG---- 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  178 LDRTVG---RRNTF-IGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07861   147 LARAFGipvRVYTHeVVTLWYRAPEVLL----GSPRYSTPVDIWSIGTIFAEMATKKP 200
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
25-233 1.82e-20

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: 95.46  E-value: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEinMLKK-----YSHHRN---------IATYYGAFi 90
Cdd:cd05624    74 FEIIKVIGRGAFGEVAVVKMKNTERIYAMKILN---------KWE--MLKRaetacFREERNvlvngdcqwITTLHYAF- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   91 kksppGNDDQLWLVMEFCGAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV 170
Cdd:cd05624   142 -----QDENYLYLVMDYYVGGDLLTLLSKFE-DKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLA 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  171 DFGVSAQL--DRTVgRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05624   216 DFGSCLKMndDGTV-QSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPF 279
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
25-287 2.06e-20

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: 92.36  E-value: 2.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYsHHRNIATYYGAFIKKSppgnddQ 100
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKflprEIEVIKGL-KHPNLICFYEAIETTS------R 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd14162    75 VYIIMELAENGDLLDYIRKNG--ALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TV-GRRN---TFIGTPYWMAPEVIACDenpdaTYD-YRSDIWSLGITAIEMAEGAPPLCDMHpMRALFLIPRNPPPRLKS 255
Cdd:cd14162   153 TKdGKPKlseTYCGSYAYASPEILRGI-----PYDpFLSDIWSMGVVLYTMVYGRLPFDDSN-LKVLLKQVQRRVVFPKN 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  256 KKWSKKFidfidTCLIKTYLS----RPPTEQLLKFP 287
Cdd:cd14162   227 PTVSEEC-----KDLILRMLSpvkkRITIEEIKRDP 257
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
29-240 2.47e-20

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 92.35  E-value: 2.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVM-DVTEDeeeeiKQEINMLKKYSHHRNIA----TYYGAFikksppGNDDQLWL 103
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKVLrDNPKA-----RREVELHWRASGCPHIVriidVYENTY------QGRKCLLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE---NAEVKLVDFGVsAQLDR 180
Cdd:cd14089    76 VMECMEGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSkgpNAILKLTDFGF-AKETT 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIacdeNPDaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMR 240
Cdd:cd14089   155 TKKSLQTPCYTPYYVAPEVL----GPE-KYDKSCDMWSLGVIMYILLCGYPPFYSNHGLA 209
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
23-283 3.42e-20

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 93.93  E-value: 3.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   23 GIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE----IKQEINMLKKYSHHRNIATYYGAFIKKSppgnd 98
Cdd:cd05617    15 QDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEdidwVQTEKHVFEQASSNPFLVGLHSCFQTTS----- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dQLWLVMEFCGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd05617    90 -RLFLVIEYVNGGDL--MFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPL------CDMHPMRALFLIPRNPPPR 252
Cdd:cd05617   167 LGPGDTTSTFCGTPNYIAPEILRGEE-----YGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTEDYLFQVILEKPIR 241
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578829925  253 LkskkwsKKFIDFIDTCLIKTYLSRPPTEQL 283
Cdd:cd05617   242 I------PRFLSVKASHVLKGFLNKDPKERL 266
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
25-234 3.47e-20

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: 92.33  E-value: 3.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE---EEIKQEINMLKKYSH--HRNIATYYGAfIKKSPPGNDD 99
Cdd:cd07863     2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDglpLSTVREVALLKRLEAfdHPNIVRLMDV-CATSRTDRET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKnTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV----S 175
Cdd:cd07863    81 KVTLVFEHVDQDLRTYLDK-VPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLariyS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  176 AQLDRTvgrrnTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLC 234
Cdd:cd07863   160 CQMALT-----PVVVTLWYRAPEVLL-----QSTYATPVDMWSVGCIFAEMFRRKPLFC 208
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
24-289 3.52e-20

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: 92.80  E-value: 3.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYSHHRNIATyygAFIKKSPpgndDQL 101
Cdd:cd14168    11 IFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIpkKALKGKESSIENEIAVLRKIKHENIVAL---EDIYESP----NHL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNtKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLL---TENAEVKLVDFGVSaQL 178
Cdd:cd14168    84 YLVMQLVSGGELFDRIVE-KGFYTEKDASTLI-RQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLS-KM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRaLFLIPRNPPPRLKSKKW 258
Cdd:cd14168   161 EGKGDVMSTACGTPGYVAPEVLA--QKP---YSKAVDCWSIGVIAYILLCGYPPFYDENDSK-LFEQILKADYEFDSPYW 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  259 ---SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14168   235 ddiSDSAKDFIRNLMEKDPNKRYTCEQALRHPWI 268
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
30-233 3.53e-20

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: 92.64  E-value: 3.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEINMLKKYS------------HHRNIATYYGAFIKKSppgn 97
Cdd:cd05608     8 VLGKGGFGEVSACQMRATGKLYACKKLN---------KKRLKKRKGYEgamvekrilakvHSRFIVSLAYAFQTKT---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 ddQLWLVMEFCGAGSVTDLVKNTKGN--ALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd05608    75 --DLCLVMTIMNGGDLRYHIYNVDEEnpGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  176 AQLDRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05608   153 VELKDGQTKTKGYAGTPGFMAPELLLGEE-----YDYSVDYFTLGVTLYEMIAARGPF 205
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
31-268 5.09e-20

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: 93.18  E-value: 5.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLK--KYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEFC 108
Cdd:cd07877    25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRllKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLM 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAgsvtDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVgrrNTF 188
Cdd:cd07877   105 GA----DLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEM---TGY 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  189 IGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR---NPPPRLKSKKWSKKFIDF 265
Cdd:cd07877   178 VATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRlvgTPGAELLKKISSESARNY 253

                  ...
gi 578829925  266 IDT 268
Cdd:cd07877   254 IQS 256
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
31-229 5.49e-20

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: 93.19  E-value: 5.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMD---VTEDEEEEIKQEINMLKkYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEF 107
Cdd:cd07878    23 VGSGAYGSVCSAYDTRLRQKVAVKKLSrpfQSLIHARRTYRELRLLK-HMKHENVIGLLDVFTPATSIENFNEVYLVTNL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAgsvtDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVgrrNT 187
Cdd:cd07878   102 MGA----DLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDEM---TG 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578829925  188 FIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEG 229
Cdd:cd07878   175 YVATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLKG 212
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
29-238 5.81e-20

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: 92.05  E-value: 5.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKG--RHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYS-HHRNIATYYGAFIKKSppGNDDQLWLVM 105
Cdd:cd14055     1 KLVGKGRFAEVWKAklKQNASGQYETVAVKIFPYEEYASWKNEKDIFTDASlKHENILQFLTAEERGV--GLDRQYWLIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKntkGNALKEDCIAYICREILRGLAHLHA-------HK--VIHRDIKGQNVLLTENAEVKLVDFGVSA 176
Cdd:cd14055    79 AYHENGSLQDYLT---RHILSWEDLCKMAGSLARGLAHLHSdrtpcgrPKipIAHRDLKSSNILVKNDGTCVLADFGLAL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  177 QLDRTVgRRNTF-----IGTPYWMAPEVIACDEN-PDATYDYRSDIWSLGITAIEMAEGAPPLCDMHP 238
Cdd:cd14055   156 RLDPSL-SVDELansgqVGTARYMAPEALESRVNlEDLESFKQIDVYSMALVLWEMASRCEASGEVKP 222
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
29-270 6.39e-20

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: 90.93  E-value: 6.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVT---EDEEEEIKQEINMLKKYShHRNIATYYGAFIKKsppgndDQLWLVM 105
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLrfpTKQESQLRNEVAILQQLS-HPGVVNLECMFETP------ERVFVVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCgAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA---EVKLVDFGVSaqldRTV 182
Cdd:cd14082    82 EKL-HGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFA----RII 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GR---RNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMR-----ALFLIPRNPpprlk 254
Cdd:cd14082   157 GEksfRRSVVGTPAYLAPEVLR-----NKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINdqiqnAAFMYPPNP----- 226
                         250
                  ....*....|....*.
gi 578829925  255 SKKWSKKFIDFIDTCL 270
Cdd:cd14082   227 WKEISPDAIDLINNLL 242
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
31-285 6.88e-20

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: 90.66  E-value: 6.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDvTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKksppgnDDQLWLVMEFCGA 110
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYK-NDVDQHKIVREISLLQKLSH-PNIVRYLGICVK------DEKLHPILEYVSG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKGNALKEDCIAYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENA---EVKLVDFGvsaqLDRTVG---- 183
Cdd:cd14156    73 GCLEELLAREELPLSWREKVELAC-DISRGMVYLHSKNIYHRDLNSKNCLIRVTPrgrEAVVTDFG----LAREVGempa 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  184 ----RRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALF---------LIPRNPP 250
Cdd:cd14156   148 ndpeRKLSLVGSAFWMAPEMLRGEP-----YDRKVDVFSFGIVLCEILARIPADPEVLPRTGDFgldvqafkeMVPGCPE 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578829925  251 PrlkskkwskkFIDFIDTCLIKTYLSRPPTEQLLK 285
Cdd:cd14156   223 P----------FLDLAASCCRMDAFKRPSFAELLD 247
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
26-232 7.93e-20

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 91.71  E-value: 7.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGRHV------KTGQLAAIKV--MDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPpgn 97
Cdd:cd05053    15 TLGKPLGEGAFGQVVKAEAVgldnkpNEVVTVAVKMlkDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGP--- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 ddqLWLVMEFCGAGSVTDLVKNTK--------------GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE 163
Cdd:cd05053    92 ---LYVVVEYASKGNLREFLRARRppgeeaspddprvpEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTE 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  164 NAEVKLVDFGVSAQL-------DRTVGRrntfigTPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIE-MAEGAPP 232
Cdd:cd05053   169 DNVMKIADFGLARDIhhidyyrKTTNGR------LPVkWMAPEALF-----DRVYTHQSDVWSFGVLLWEiFTLGGSP 235
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
31-221 8.13e-20

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: 90.59  E-value: 8.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVM---DVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSPPGnddqlwLVMEF 107
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLhssPNCIEERKALLKEAEKMERARH-SYVLPLLGVCVERRSLG------LVMEY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKGNaLKEDCIAYICREILRGLAHLH--AHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVG-- 183
Cdd:cd13978    74 MENGSLKSLLEREIQD-VPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISan 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578829925  184 RRNT---FIGTPYWMAPEVIacdENPDATYDYRSDIWSLGI 221
Cdd:cd13978   153 RRRGtenLGGTPIYMAPEAF---DDFNKKPTSKSDVYSFAI 190
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
25-220 8.58e-20

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


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 91.52  E-value: 8.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKvmdvtedeeeEIK-------------QEINMLKKySHHRNIATyygafIK 91
Cdd:cd07843     7 YEKLNRIEEGTYGVVYRARDKKTGEIVALK----------KLKmekekegfpitslREINILLK-LQHPNIVT-----VK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   92 KSPPG-NDDQLWLVMEFCgAGSVTDLVKNTKGNALKEDcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV 170
Cdd:cd07843    71 EVVVGsNLDKIYMVMEYV-EHDLKSLMETMKQPFLQSE-VKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKIC 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  171 DFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACdenpDATYDYRSDIWSLG 220
Cdd:cd07843   149 DFGLAREYGSPLKPYTQLVVTLWYRAPELLLG----AKEYSTAIDMWSVG 194
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
25-226 9.70e-20

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: 91.45  E-value: 9.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdvTEDEEEEIKQEINMLKKYSHHRNIATYYGAFI---KKSPPgnddql 101
Cdd:cd14132    20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL--KPVKKKKIKREIKILQNLRGGPNIVKLLDVVKdpqSKTPS------ 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 wLVMEFcgagsvtdlVKNTK----GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT-ENAEVKLVDFGVsA 176
Cdd:cd14132    92 -LIFEY---------VNNTDfktlYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDhEKRKLRLIDWGL-A 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  177 QLDRTVGRRNTFIGTPYWMAPEVIAcdENPDatYDYRSDIWSLGITAIEM 226
Cdd:cd14132   161 EFYHPGQEYNVRVASRYYKGPELLV--DYQY--YDYSLDMWSLGCMLASM 206
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
31-226 1.03e-19

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: 90.79  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIK-VMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKksppgnDDQLWLVMEFCG 109
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKeLIRFDEETQRTFLKEVKVMRCLEH-PNVLKFIGVLYK------DKRLNFITEYIK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  110 AGSVTDLVKNTKGNALKEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS------------AQ 177
Cdd:cd14221    74 GGTLRGIIKSMDSHYPWSQRVSF-AKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdektqpegLR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  178 LDRTVGRRN--TFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd14221   153 SLKKPDRKKryTVVGNPYWMAPEMIN-----GRSYDEKVDVFSFGIVLCEI 198
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
24-232 1.21e-19

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 90.94  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELV-EVVGNGTYGQVYKGRHVKTGQLAAIKVMD-VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFikksppGNDDQL 101
Cdd:cd14090     2 LYKLTgELLGEGAYASVQTCINLYTGKEYAVKIIEkHPGHSRSRVFREVETLHQCQGHPNILQLIEYF------EDDERF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE---VKLVDFGVSAQL 178
Cdd:cd14090    76 YLVFEKMRGGPL--LSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGSGI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578829925  179 dRTVGRRNTFIGTP---------YWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14090   154 -KLSSTSMTPVTTPelltpvgsaEYMAPEVVDAFVGEALSYDKRCDLWSLGVILYIMLCGYPP 215
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
24-289 1.24e-19

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: 90.06  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV-TEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSppgnddQLW 102
Cdd:cd14191     3 FYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAySAKEKENIRQEISIMNCL-HHPKLVQCVDAFEEKA------NIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLTEN--AEVKLVDFGVSAQLDr 180
Cdd:cd14191    76 MVLEMVSGGELFERIIDEDFELTERECIKYM-RQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTKIKLIDFGLARRLE- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIacdeNPDATyDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALfliprnppPRLKSKKW-- 258
Cdd:cd14191   154 NAGSLKVLFGTPEFVAPEVI----NYEPI-GYATDMWSIGVICYILVSGLSPFMGDNDNETL--------ANVTSATWdf 220
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578829925  259 --------SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14191   221 ddeafdeiSDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
25-232 1.39e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 90.54  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEI---NMLKKYSHHRNIATY---------YGAFIKK 92
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKIN---------KQNLilrNQIQQVFVERDILTFaenpfvvsmYCSFETK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 SppgnddQLWLVMEFCGAGSVTDLVKNtkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 172
Cdd:cd05609    73 R------HLCMVMEYVEGGDCATLLKN--IGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDF 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  173 GVS--AQLDRTVGRRNTFI-------------GTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05609   145 GLSkiGLMSLTTNLYEGHIekdtrefldkqvcGTPEYIAPEVIL-----RQGYGKPVDWWAMGIILYEFLVGCVP 214
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
25-239 1.41e-19

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 90.54  E-value: 1.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEINMLKKYSHHRN-----IATYYGAFIKKSPPGND- 98
Cdd:cd14209     3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILD---------KQKVVKLKQVEHTLNekrilQAINFPFLVKLEYSFKDn 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd14209    74 SNLYMVMEYVPGGEMFSHLR--RIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  179 DrtvGRRNTFIGTPYWMAPEVIacdenPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPM 239
Cdd:cd14209   152 K---GRTWTLCGTPEYLAPEII-----LSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI 204
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
18-233 1.68e-19

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 92.76  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   18 LRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdvtedeeeeikQEINMLKK-----YSHHRNIATYYGA--FI 90
Cdd:cd05622    68 LRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLL-----------SKFEMIKRsdsafFWEERDIMAFANSpwVV 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   91 KKSPPGNDDQ-LWLVMEFCGAGSVTDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 169
Cdd:cd05622   137 QLFYAFQDDRyLYMVMEYMPGGDLVNLMSNYD---VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKL 213
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  170 VDFGVSAQLDRT-VGRRNTFIGTPYWMAPEVIAcDENPDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05622   214 ADFGTCMKMNKEgMVRCDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLYEMLVGDTPF 277
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
27-239 1.84e-19

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: 90.58  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEEEIKQEIN---MLKkyshHRNIATYYGAFI--KKSppgnDDQL 101
Cdd:cd14142     9 LVECIGKGRYGEVWRGQW--QGESVAVKIFSSRDEKSWFRETEIYntvLLR----HENILGFIASDMtsRNS----CTQL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNtkgNALKEDCIAYICREILRGLAHLHAH--------KVIHRDIKGQNVLLTENAEVKLVDFG 173
Cdd:cd14142    79 WLITHYHENGSLYDYLQR---TTLDHQEMLRLALSAASGLVHLHTEifgtqgkpAIAHRDLKSKNILVKSNGQCCIADLG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  174 -------VSAQLDrtVGrRNTFIGTPYWMAPEVIACDENPDATYDY-RSDIWSLGITAIEMA----------EGAPPLCD 235
Cdd:cd14142   156 lavthsqETNQLD--VG-NNPRVGTKRYMAPEVLDETINTDCFESYkRVDIYAFGLVLWEVArrcvsggiveEYKPPFYD 232

                  ....
gi 578829925  236 MHPM 239
Cdd:cd14142   233 VVPS 236
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
66-235 2.03e-19

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: 90.02  E-value: 2.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   66 IKQEINMLKKYSHHRNIAtyygaFIKKSPPGNDDQLWLVMEFCGAGSVTDlVKNTKgnALKEDCIAYICREILRGLAHLH 145
Cdd:cd14199    72 VYQEIAILKKLDHPNVVK-----LVEVLDDPSEDHLYMVFELVKQGPVME-VPTLK--PLSEDQARFYFQDLIKGIEYLH 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  146 AHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIAcdENPDATYDYRSDIWSLGITAIE 225
Cdd:cd14199   144 YQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLS--ETRKIFSGKALDVWAMGVTLYC 221
                         170
                  ....*....|
gi 578829925  226 MAEGAPPLCD 235
Cdd:cd14199   222 FVFGQCPFMD 231
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
66-239 2.18e-19

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: 90.15  E-value: 2.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   66 IKQEINMLKKYsHHRNIATYYgAFIKksppGNDDQLWLVMEFCGAgSVTDLV--KNTKG-NALKEDCIAYICREILRGLA 142
Cdd:cd14001    52 LKEEAKILKSL-NHPNIVGFR-AFTK----SEDGSLCLAMEYGGK-SLNDLIeeRYEAGlGPFPAATILKVALSIARALE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  143 HLHAHK-VIHRDIKGQNVLLTENAE-VKLVDFGVSAQLDRTV-GRRN---TFIGTPYWMAPEVIacDENPDATydYRSDI 216
Cdd:cd14001   125 YLHNEKkILHGDIKSGNVLIKGDFEsVKLCDFGVSLPLTENLeVDSDpkaQYVGTEPWKAKEAL--EEGGVIT--DKADI 200
                         170       180
                  ....*....|....*....|...
gi 578829925  217 WSLGITAIEMAEGAPPLCDMHPM 239
Cdd:cd14001   201 FAYGLVLWEMMTLSVPHLNLLDI 223
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
31-233 2.21e-19

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: 91.09  E-value: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEINMLKKYSH---HRNI----ATYYGAFIK--KSPPGNDDQL 101
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLS---------KKVIVAKKEVAHtigERNIlvrtALDESPFIVglKFSFQTPTDL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEF-CGAGSVTDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd05586    72 YLVTDYmSGGELFWHLQKEGR---FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLT 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05586   149 DNKTTNTFCGTTEYLAPEVLL----DEKGYTKMVDFWSLGVLVFEMCCGWSPF 197
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
29-255 2.40e-19

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 90.84  E-value: 2.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYgAFikksppGNDDQLWLV 104
Cdd:cd05595     1 KLLGKGTFGKVILVREKATGRYYAMKILRkeviIAKDEVAHTVTESRVLQNTRHPFLTALKY-AF------QTHDRLCFV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGR 184
Cdd:cd05595    74 MEYANGGEL--FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGAT 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  185 RNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLI-------PRNPPPRLKS 255
Cdd:cd05595   152 MKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELIlmeeirfPRTLSPEAKS 224
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
25-233 2.66e-19

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: 91.60  E-value: 2.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdvtedeeeeikQEINMLKK-----YSHHRNIATY---------YGAFi 90
Cdd:cd05621    54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLL-----------SKFEMIKRsdsafFWEERDIMAFanspwvvqlFCAF- 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   91 kksppGNDDQLWLVMEFCGAGSVTDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV 170
Cdd:cd05621   122 -----QDDKYLYMVMEYMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLA 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  171 DFGVSAQLDRT-VGRRNTFIGTPYWMAPEVIAcDENPDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05621   194 DFGTCMKMDETgMVHCDTAVGTPDYISPEVLK-SQGGDGYYGRECDWWSVGVFLFEMLVGDTPF 256
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
26-236 2.87e-19

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 90.77  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNG--TYGQVYKGRHVKTGQLAAIKVMDV---TEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKksppgnDDQ 100
Cdd:cd08227     1 ELLTVIGRGfeDLMTVNLARYKPTGEYVTVRRINLeacTNEMVTFLQGELHVSKLF-NHPNIVPYRATFIA------DNE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd08227    74 LWVVTSFMAYGSAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMIN 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578829925  181 TVGRRNTFIGTPY-------WMAPEVIacDENPDAtYDYRSDIWSLGITAIEMAEGAPPLCDM 236
Cdd:cd08227   154 HGQRLRVVHDFPKysvkvlpWLSPEVL--QQNLQG-YDAKSDIYSVGITACELANGHVPFKDM 213
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
25-226 3.23e-19

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: 90.50  E-value: 3.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK----VMDVTEDEEEEIKqEINMLKkYSHHRNIATYYGAFIKKSPPGNDDQ 100
Cdd:cd07855     7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKkipnAFDVVTTAKRTLR-ELKILR-HFKHDNIIAIRDILRPKVPYADFKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGagsvTDLVKNTKGNA-LKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd07855    85 VYVVLDLME----SDLHHIIHSDQpLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLC 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  180 RTVGRRNTF----IGTPYWMAPEVI-ACDENPDATydyrsDIWSLGITAIEM 226
Cdd:cd07855   161 TSPEEHKYFmteyVATRWYRAPELMlSLPEYTQAI-----DMWSVGCIFAEM 207
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
25-231 4.92e-19

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: 90.06  E-value: 4.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKkYSHHRNIATYYGafIKKspPGNDDQL- 101
Cdd:cd07849     7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRtlREIKILL-RFKHENIIGILD--IQR--PPTFESFk 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 --WLVMEFCGagsvTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS---- 175
Cdd:cd07849    82 dvYIVQELME----TDLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAriad 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  176 AQLDRTvGRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07849   158 PEHDHT-GFLTEYVATRWYRAPEIML----NSKGYTKAIDIWSVGCILAEMLSNRP 208
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
25-232 5.55e-19

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 88.47  E-value: 5.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVmDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAfikksppGNDDQ-LWL 103
Cdd:cd14017     2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKV-ESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGC-------GRTERyNYI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL---TENAE-VKLVDFGVSAQLD 179
Cdd:cd14017    74 VMTLLGP-NLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgPSDERtVYILDFGLARQYT 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVG-----RRNT--FIGTPYWMApevIACDENPDatYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14017   153 NKDGeverpPRNAagFRGTVRYAS---VNAHRNKE--QGRRDDLWSWFYMLIEFVTGQLP 207
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
25-233 6.04e-19

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: 88.54  E-value: 6.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE-------IKQEINMLKKYsHHRNIATYYGAFIKKSppgn 97
Cdd:cd14194     7 YDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRrgvsredIEREVSILKEI-QHPNVITLHEVYENKT---- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 ddQLWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNV-LLTENA---EVKLVDFG 173
Cdd:cd14194    82 --DVILILELVAGGELFDFLAEKE--SLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVpkpRIKIIDFG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  174 VSAQLDRTVGRRNTFiGTPYWMAPEVIacDENPdatYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14194   158 LAHKIDFGNEFKNIF-GTPEFVAPEIV--NYEP---LGLEADMWSIGVITYILLSGASPF 211
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
25-233 6.22e-19

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: 89.69  E-value: 6.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFikksppGNDDQ 100
Cdd:cd05602     9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQkkaiLKKKEEKHIMSERNVLLKNVKHPFLVGLHFSF------QTTDK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd05602    83 LYFVLDYINGGELFYHLQRER--CFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIacDENPdatYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05602   161 PNGTTSTFCGTPEYLAPEVL--HKQP---YDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
30-232 6.63e-19

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: 89.38  E-value: 6.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVK---TGQLAAIKVMD---VTEDEEEEIKQEINMLKKYSHHRNIATYYgAFikksppGNDDQLWL 103
Cdd:cd05582     2 VLGQGSFGKVFLVRKITgpdAGTLYAMKVLKkatLKVRDRVRTKMERDILADVNHPFIVKLHY-AF------QTEGKLYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSV-TDLVKNTkgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd05582    75 ILDFLRGGDLfTRLSKEV---MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHE 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05582   152 KKAYSFCGTVEYMAPEVVN-----RRGHTQSADWWSFGVLMFEMLTGSLP 196
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
25-290 6.85e-19

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: 88.38  E-value: 6.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINM---LKKYSHHRNIATYYGAFikksppGNDDQL 101
Cdd:cd14117     8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRReieIQSHLRHPNILRLYNYF------HDRKRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd14117    82 YLILEYAPRGELYKELQ--KHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 vgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL---CDMHPMRALFLIPRNPPPRLkskkw 258
Cdd:cd14117   160 --RRRTMCGTLDYLPPEMIE-----GRTHDEKVDLWCIGVLCYELLVGMPPFesaSHTETYRRIVKVDLKFPPFL----- 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  259 SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd14117   228 SDGSRDLISKLLRYHPSERLPLKGVMEHPWVK 259
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
31-232 6.87e-19

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: 87.95  E-value: 6.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDE-----EEEIKQEiNMLKKYSHHRNIATYYGAFikksppGNDDQLWLVM 105
Cdd:cd14070    10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKkdsyvTKNLRRE-GRIQQMIRHPNITQLLDIL------ETENSYYLVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaQLDRTVGRR 185
Cdd:cd14070    83 ELCPGGNLMHRIYDKK--RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLS-NCAGILGYS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  186 NTFI---GTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14070   160 DPFStqcGSPAYAAPELLA-----RKKYGPKVDVWSIGVNMYAMLTGTLP 204
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
25-290 7.52e-19

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: 88.63  E-value: 7.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikksppGNDDQL 101
Cdd:cd14086     3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINtkkLSARDHQKLEREARICRLL-KHPNIVRLHDSI------SEEGFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMefcgagsvtDLVKntkGNALKEDCIAyicRE-------------ILRGLAHLHAHKVIHRDIKGQNVLL---TENA 165
Cdd:cd14086    76 YLVF---------DLVT---GGELFEDIVA---REfyseadashciqqILESVNHCHQNGIVHRDLKPENLLLaskSKGA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  166 EVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIacDENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLI 245
Cdd:cd14086   141 AVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVL--RKDP---YGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQI 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578829925  246 PRN----PPPRLKSKKWSKKfiDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd14086   216 KAGaydyPSPEWDTVTPEAK--DLINQMLTVNPAKRITAAEALKHPWIC 262
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
12-284 7.59e-19

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: 88.18  E-value: 7.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   12 DIDLSALrdpagifELVEVVGNGTYGQVYkgRHVKTGQLAAIKVM------DVTEDEEEeIKQEINMLKKYSHhRNIATY 85
Cdd:cd14145     2 EIDFSEL-------VLEEIIGIGGFGKVY--RAIWIGDEVAVKAArhdpdeDISQTIEN-VRQEAKLFAMLKH-PNIIAL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   86 YGAFIKksppgnDDQLWLVMEFCGAGSVTDLVKntkGNALKEDCIAYICREILRGLAHLHAHK---VIHRDIKGQNVLLT 162
Cdd:cd14145    71 RGVCLK------EPNLCLVMEFARGGPLNRVLS---GKRIPPDILVNWAVQIARGMNYLHCEAivpVIHRDLKSSNILIL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  163 ENAE--------VKLVDFGVSAQLDRTVgrRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLC 234
Cdd:cd14145   142 EKVEngdlsnkiLKITDFGLAREWHRTT--KMSAAGTYAWMAPEVIR-----SSMFSKGSDVWSYGVLLWELLTGEVPFR 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  235 DMHPMRALFLIPRNPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLL 284
Cdd:cd14145   215 GIDGLAVAYGVAMNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNIL 264
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
29-233 9.51e-19

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: 87.67  E-value: 9.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTG-QLAAIKVMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKsppgndDQLWLVMEF 107
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGlKLAAKVINKQNSKDKEMVLLEIQVMNQLNH-RNLIQLYEAIETP------NEIVLFMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLL--TENAEVKLVDFGVSAQLDRTVGRR 185
Cdd:cd14190    83 VEGGELFERIVDEDYHLTEVDAMVFV-RQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRYNPREKLK 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  186 NTFiGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPL 233
Cdd:cd14190   162 VNF-GTPEFLSPEVVNYDQVSFPT-----DMWSMGVITYMLLSGLSPF 203
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
24-233 9.82e-19

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: 87.70  E-value: 9.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE-------EIKQEINMLKKYsHHRNIATYYGAFIKKSppg 96
Cdd:cd14196     6 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvsreEIEREVSILRQV-LHPNIITLHDVYENRT--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 nddQLWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNV-LLTENA---EVKLVDF 172
Cdd:cd14196    82 ---DVVLILELVSGGELFDFLAQKE--SLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  173 GVSAQLDRTVGRRNTFiGTPYWMAPEVIacDENPdatYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14196   157 GLAHEIEDGVEFKNIF-GTPEFVAPEIV--NYEP---LGLEADMWSIGVITYILLSGASPF 211
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
29-220 1.12e-18

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: 87.71  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQ-VYKGRHvkTGQLAAIKVM-----DVTEdeeeeikQEINMLKKYSHHRNIATYYGafiKKSppgnDDQ-L 101
Cdd:cd13982     7 KVLGYGSEGTiVFRGTF--DGRPVAVKRLlpeffDFAD-------REVQLLRESDEHPNVIRYFC---TEK----DRQfL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAgSVTDLVKNTKGNALKE----DCIAyICREILRGLAHLHAHKVIHRDIKGQNVLLT-----ENAEVKLVDF 172
Cdd:cd13982    71 YIALELCAA-SLQDLVESPRESKLFLrpglEPVR-LLRQIASGLAHLHSLNIVHRDLKPQNILIStpnahGNVRAMISDF 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  173 GVSAQLDR---TVGRRNTFIGTPYWMAPEVIACDENPDATydyRS-DIWSLG 220
Cdd:cd13982   149 GLCKKLDVgrsSFSRRSGVAGTSGWIAPEMLSGSTKRRQT---RAvDIFSLG 197
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
25-227 1.28e-18

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: 87.48  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRH-VKTGQLAAIKVMDVTEDEEEEIK---QEINMLKKYSH--HRNIATYYGAFikksppGND 98
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSErVPTGKVYAVKKLKPNYAGAKDRLrrlEEVSILRELTLdgHDNIVQLIDSW------EYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTD-LVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd14052    76 GHLYIQTELCENGSLDVfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTfiGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMA 227
Cdd:cd14052   156 WPLIRGIERE--GDREYIAPEILS-----EHMYDKPADIFSLGLILLEAA 198
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
25-232 1.46e-18

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 88.51  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM---DVTEdeeeeiKQEIN--MLKK-------YSHHRNIATYYGAFIKK 92
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALkkgDIIA------RDEVEslMCEKrifetvnSARHPFLVNLFACFQTP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 sppgndDQLWLVMEFCGAGsvtDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 172
Cdd:cd05589    75 ------EHVCFVMEYAAGG---DLMMHIHEDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADF 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  173 GVSAQ----LDRTvgrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05589   146 GLCKEgmgfGDRT----STFCGTPEFLAPEVLT-----DTSYTRAVDWWGLGVLIYEMLVGESP 200
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
25-233 1.58e-18

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 88.94  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE----IKQEINMLKKYSHHRNIATYYGAFIKKSppgnddQ 100
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEdidwVQTEKHVFEQASNHPFLVGLHSCFQTES------R 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd05618    96 LFFVIEYVNGGDL--MFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLR 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05618   174 PGDTTSTFCGTPNYIAPEILRGED-----YGFSVDWWALGVLMFEMMAGRSPF 221
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
31-229 1.67e-18

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 88.42  E-value: 1.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ---EINMLKkYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEF 107
Cdd:cd07879    23 VGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRayrELTLLK-HMQHENVIGLLDVFTSAVSGDEFQDFYLVMPY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CgagsVTDLVKnTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDrtvGRRNT 187
Cdd:cd07879   102 M----QTDLQK-IMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHAD---AEMTG 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578829925  188 FIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEG 229
Cdd:cd07879   174 YVVTRWYRAPEVILNWMH----YNQTVDIWSVGCIMAEMLTG 211
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
25-226 1.71e-18

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: 87.26  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQV----YKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAfikkSPPGND 98
Cdd:cd05080     6 LKKIRDLGEGHFGKVslycYDPTNDGTGEMVAVKALkaDCGPQHRSGWKQEIDILKTL-YHENIVKYKGC----CSEQGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTD-LVKNTKGNALkedcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd05080    81 KSLQLIMEYVPLGSLRDyLPKHSIGLAQ----LLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  178 LD--------RTVGRRNTFigtpyWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd05080   157 VPegheyyrvREDGDSPVF-----WYAPECLK-----EYKFYYASDVWSFGVTLYEL 203
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
25-192 2.10e-18

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 86.74  E-value: 2.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTeDEEEEIKQEINMLKKYSHHRNIAT--YYGAfikksppgNDDQLW 102
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKD-SKHPQLEYEAKVYKLLQGGPGIPRlyWFGQ--------EGDYNV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAgSVTDLVKNTKGN-ALKedCIAYICREILRGLAHLHAHKVIHRDIKGQNVL--LTENA-EVKLVDFGVSAQ- 177
Cdd:cd14016    73 MVMDLLGP-SLEDLFNKCGRKfSLK--TVLMLADQMISRLEYLHSKGYIHRDIKPENFLmgLGKNSnKVYLIDFGLAKKy 149
                         170       180
                  ....*....|....*....|.
gi 578829925  178 LDRTVGR------RNTFIGTP 192
Cdd:cd14016   150 RDPRTGKhipyreGKSLTGTA 170
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
25-315 2.10e-18

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: 87.19  E-value: 2.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEeIKQEINMLKKYSHhRNIATYYGAFikksppGNDDQLWLV 104
Cdd:cd14085     5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKI-VRTEIGVLLRLSH-PNIIKLKEIF------ETPTEISLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNtKGNALKEDCiAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVSAQLDRT 181
Cdd:cd14085    77 LELVTGGELFDRIVE-KGYYSERDA-ADAVKQILEAVAYLHENGIVHRDLKPENLLYAtpaPDAPLKIADFGLSKIVDQQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRnTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKW--- 258
Cdd:cd14085   155 VTMK-TVCGTPGYCAPEILR-----GCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRILNCDYDFVSPWWddv 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  259 SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQvriqlkdHIDRSRKKRGE 315
Cdd:cd14085   229 SLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTGKAANFA-------HMDTAQKKLQE 278
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
21-226 2.11e-18

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: 86.48  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGRHvKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKSPpgnddq 100
Cdd:cd05067     5 PRETLKLVERLGAGQFGEVWMGYY-NGHTKVAIKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLY--AVVTQEP------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd05067    76 IYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIED 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  181 TVGRRNTFIGTPY-WMAPEVIACdenpdATYDYRSDIWSLGITAIEM 226
Cdd:cd05067   156 NEYTAREGAKFPIkWTAPEAINY-----GTFTIKSDVWSFGILLTEI 197
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
25-254 2.11e-18

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: 87.36  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM---DVTEDEEEEIKQEINMLKKYSHHrNIATYYGAFIKKSppgnddQL 101
Cdd:cd07848     3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFkdsEENEEVKETTLRELKMLRTLKQE-NIVELKEAFRRRG------KL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCgAGSVTDLVKNTKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd07848    76 YLVFEYV-EKNMLELLEEMPNGVPPEKVRSYI-YQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  182 VGRRNT-FIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRN----PPPRLK 254
Cdd:cd07848   154 SNANYTeYVATRWYRSPELLL-----GAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVlgplPAEQMK 226
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
31-259 2.29e-18

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: 87.15  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEE----EEIKQEINMlkkysHHRNIATYYGAFIKKSppGNDDQLWLVME 106
Cdd:cd14144     3 VGKGRYGEVWKGKW--RGEKVAVKIFFTTEEASwfreTEIYQTVLM-----RHENILGFIAADIKGT--GSWTQLYLITD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKntkGNALKEDCIAYICREILRGLAHLHAH--------KVIHRDIKGQNVLLTENAEVKLVDFGVSA-- 176
Cdd:cd14144    74 YHENGSLYDFLR---GNTLDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAVkf 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  177 --QLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDY-RSDIWSLGITAIEMA----------EGAPPLCDMHP----- 238
Cdd:cd14144   151 isETNEVDLPPNTRVGTKRYMAPEVLDESLNRNHFDAYkMADMYSFGLVLWEIArrcisggiveEYQLPYYDAVPsdpsy 230
                         250       260
                  ....*....|....*....|...
gi 578829925  239 --MRALFLIPRNPPPrlKSKKWS 259
Cdd:cd14144   231 edMRRVVCVERRRPS--IPNRWS 251
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
24-288 2.29e-18

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: 86.12  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKT-------GQLAAIKVMDVTEDEEEeIKQEINMLKKYSHHRNIATYYGAFIKKsppg 96
Cdd:cd14019     2 KYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPSR-ILNELECLERLGGSNNVSGLITAFRNE---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 ndDQLWLVMEFCGAGSVTDLVKNTKgnalKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLT-ENAEVKLVDFGVS 175
Cdd:cd14019    77 --DQVVAVLPYIEHDDFRDFYRKMS----LTDIRIYL-RNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 -AQLDRTvGRRNTFIGTPYWMAPEVI-ACdenPDATydYRSDIWSLGITAIEMAEGA-PPLCDMHPMRALFLIprnpppr 252
Cdd:cd14019   150 qREEDRP-EQRAPRAGTRGFRAPEVLfKC---PHQT--TAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEI------- 216
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  253 lKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14019   217 -ATIFGSDEAYDLLDKLLELDPSKRITAEEALKHPF 251
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
25-233 2.39e-18

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: 86.54  E-value: 2.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE--IKQEINMLKKYSHhRNIATYYGAFikksppGNDDQLW 102
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEdmIESEILIIKSLSH-PNIVKLFEVY------ETEKEIY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE----VKLVDFGVSAQL 178
Cdd:cd14185    75 LILEYVRGGDLFDAI--IESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDksttLKLADFGLAKYV 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  179 DRTVgrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14185   153 TGPI---FTVCGTPTYVAPEILS-----EKGYGLEVDMWAAGVILYILLCGFPPF 199
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
29-304 2.57e-18

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 87.00  E-value: 2.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEeikQEINMLKKYSHHRNIATYYGAFikksppGNDDQLWLVMEFC 108
Cdd:cd14175     7 ETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPS---EEIEILLRYGQHPNIITLKDVY------DDGKHVYLVTELM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKNTKGNALKEdcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE---NAE-VKLVDFGVSAQLDRTVGR 184
Cdd:cd14175    78 RGGELLDKILRQKFFSERE--ASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDesgNPEsLRICDFGFAKQLRAENGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  185 RNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMhpmralfliPRNPPPRLKSKKWSKKFI- 263
Cdd:cd14175   156 LMTPCYTANFVAPEVLK-----RQGYDEGCDIWSLGILLYTMLAGYTPFANG---------PSDTPEEILTRIGSGKFTl 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  264 -------------DFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVRIQLKD 304
Cdd:cd14175   222 sggnwntvsdaakDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPQSQLNHQD 275
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
25-231 2.82e-18

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: 86.67  E-value: 2.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAF-IKKSppgnddqL 101
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTaiREASLLKDLKH-ANIVTLHDIIhTKKT-------L 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCgagsVTDLVK--NTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQld 179
Cdd:cd07844    74 TLVFEYL----DTDLKQymDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARA-- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  180 RTVGRRnTF---IGTPYWMAPEVIAcdenpdATYDYRS--DIWSLGITAIEMAEGAP 231
Cdd:cd07844   148 KSVPSK-TYsneVVTLWYRPPDVLL------GSTEYSTslDMWGVGCIFYEMATGRP 197
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
31-262 2.92e-18

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 86.75  E-value: 2.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMdvteDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSP-PGNDD---QLWLVME 106
Cdd:cd14171    14 LGTGISGPVRVCVKKSTGERFALKIL----LDRPKARTEVRLHMMCSGHPNIVQIYDVYANSVQfPGESSpraRLLIVME 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE---VKLVDFGVsAQLDRtvG 183
Cdd:cd14171    90 LMEGGELFDRISQHRH--FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGF-AKVDQ--G 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  184 RRNTFIGTPYWMAPEVIACDENPDA------------TYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALfliprnpPP 251
Cdd:cd14171   165 DLMTPQFTPYYVAPQVLEAQRRHRKersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTI-------TK 237
                         250
                  ....*....|.
gi 578829925  252 RLKSKKWSKKF 262
Cdd:cd14171   238 DMKRKIMTGSY 248
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
25-235 3.19e-18

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: 85.81  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEInMLKKYSHHRNIATYYGAFIKKSppgnddQLWLV 104
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREI-INHRSLRHPNIVRFKEVILTPT------HLAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNtkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL--TENAEVKLVDFGVSAQLDRTV 182
Cdd:cd14665    75 MEYAAGGELFERICN--AGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKSSVLHS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  183 GRRNTfIGTPYWMAPEVIACDEnpdatYDYR-SDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd14665   153 QPKST-VGTPAYIAPEVLLKKE-----YDGKiADVWSCGVTLYVMLVGAYPFED 200
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
66-235 3.25e-18

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: 86.54  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   66 IKQEINMLKKYSHhRNIATyygaFIKKSPPGNDDQLWLVMEFCGAGSVTDLVKNtkgNALKEDCIAYICREILRGLAHLH 145
Cdd:cd14200    70 VYQEIAILKKLDH-VNIVK----LIEVLDDPAEDNLYMVFDLLRKGPVMEVPSD---KPFSEDQARLYFRDIVLGIEYLH 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  146 AHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIAcdENPDATYDYRSDIWSLGITAIE 225
Cdd:cd14200   142 YQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLS--DSGQSFSGKALDVWAMGVTLYC 219
                         170
                  ....*....|
gi 578829925  226 MAEGAPPLCD 235
Cdd:cd14200   220 FVYGKCPFID 229
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
25-233 3.75e-18

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 88.53  E-value: 3.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKySHHRNIATYYGAFikksppGNDDQ 100
Cdd:cd05623    74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILNkwemLKRAETACFREERDVLVN-GDSQWITTLHYAF------QDDNN 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL-- 178
Cdd:cd05623   147 LYLVMDYYVGGDLLTLLSKFE-DRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLme 225
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  179 DRTVgRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05623   226 DGTV-QSSVAVGTPDYISPEILQAMEDGKGKYGPECDWWSLGVCMYEMLYGETPF 279
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
30-232 4.13e-18

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 86.99  E-value: 4.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKsppgndDQLWLVM 105
Cdd:cd05575     2 VIGKGSFGKVLLARHKAEGKLYAVKVLQkkaiLKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTK------DKLYFVL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGsvtDLVKNTKgnalKEDCIA-----YICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd05575    76 DYVNGG---ELFFHLQ----RERHFPeprarFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIE 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05575   149 PSDTTSTFCGTPEYLAPEVLRKQP-----YDRTVDWWCLGAVLYEMLYGLPP 195
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
28-231 4.45e-18

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 86.58  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAFikksppGNDDQLWLVM 105
Cdd:cd07872    11 LEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaiREVSLLKDLKH-ANIVTLHDIV------HTDKSLTLVF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFcgagsvtdLVKNTK------GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd07872    84 EY--------LDKDLKqymddcGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07872   156 VPTKTYSNEVVTLWYRPPDVLL----GSSEYSTQIDMWGVGCIFFEMASGRP 203
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
25-232 4.64e-18

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: 85.52  E-value: 4.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVT---EDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKsppgndDQL 101
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSqldEENLKKIYREVQIMKMLNH-PHIIKLYQVMETK------DML 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaQLDRT 181
Cdd:cd14071    75 YLVTEYASNGEIFDYL--AQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS-NFFKP 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  182 VGRRNTFIGTPYWMAPEVIACDEnpdatYD-YRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14071   152 GELLKTWCGSPPYAAPEVFEGKE-----YEgPQLDIWSLGVVLYVLVCGALP 198
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
25-235 5.21e-18

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 86.22  E-value: 5.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEeeiKQEINMLKKYSHHRNIATYYGAFikksppgnDDQ--LW 102
Cdd:cd14178     5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDP---SEEIEILLRYGQHPNIITLKDVY--------DDGkfVY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGNALKEDCiAYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENA----EVKLVDFGVSAQL 178
Cdd:cd14178    74 LVMELMRGGELLDRILRQKCFSEREAS-AVLC-TITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd14178   152 RAENGLLMTPCYTANFVAPEVLK-----RQGYDAACDIWSLGILLYTMLAGFTPFAN 203
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
31-238 5.46e-18

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 86.12  E-value: 5.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKYSHhRNIATyygafIKKSPPGND----DQLWLV 104
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKScrLELSVKNKDRWCHEIQIMKKLNH-PNVVK-----ACDVPEEMNflvnDVPLLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLV-KNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE-NAEV--KLVDFGVSAQLDR 180
Cdd:cd14039    75 MEYCSGGDLRKLLnKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEiNGKIvhKIIDLGYAKDLDQ 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  181 tvGRRNT-FIGTPYWMAPEVIacdENpdATYDYRSDIWSLGITAIEMAEGAPP-LCDMHP 238
Cdd:cd14039   155 --GSLCTsFVGTLQYLAPELF---EN--KSYTVTVDYWSFGTMVFECIAGFRPfLHNLQP 207
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
25-233 5.55e-18

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 87.06  E-value: 5.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKksppgndDQ 100
Cdd:cd05593    17 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKkeviIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTK-------DR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd05593    90 LCFVMEYVNGGEL--FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578829925  181 TVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05593   168 DAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPF 215
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
25-233 6.01e-18

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: 85.44  E-value: 6.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE-------EIKQEINMLKKYsHHRNIATYYGAFIKKSppgn 97
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSrrgvsreEIEREVNILREI-QHPNIITLHDIFENKT---- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 ddQLWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE----NAEVKLVDFG 173
Cdd:cd14195    82 --DVVLILELVSGGELFDFLAEKE--SLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDknvpNPRIKLIDFG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  174 VSAQLDRTVGRRNTFiGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14195   158 IAHKIEAGNEFKNIF-GTPEFVAPEIVNYE-----PLGLEADMWSIGVITYILLSGASPF 211
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
31-251 6.53e-18

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: 85.26  E-value: 6.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTG-QLAAIKV-MDVTEDeeeeikQEINMLKKYSHHRnIATYYGAfIKKSPPGNddqlwLVMEFC 108
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGfQCAVKKVrLEVFRA------EELMACAGLTSPR-VVPLYGA-VREGPWVN-----IFMDLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN-AEVKLVDFGVSAQLD-----RTV 182
Cdd:cd13991    81 EGGSLGQLIKEQ--GCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHAECLDpdglgKSL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  183 GRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPP 251
Cdd:cd13991   159 FTGDYIPGTETHMAPEVVLGK-----PCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPP 222
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
31-231 6.80e-18

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 85.83  E-value: 6.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAFikksppGNDDQLWLVMEFC 108
Cdd:cd07871    13 LGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTaiREVSLLKNLKH-ANIVTLHDII------HTERCLTLVFEYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GagsvTDLVK--NTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRN 186
Cdd:cd07871    86 D----SDLKQylDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578829925  187 TFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07871   162 NEVVTLWYRPPDVLL----GSTEYSTPIDMWGVGCILYEMATGRP 202
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
21-238 7.04e-18

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: 84.87  E-value: 7.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIkkSPpgndDQ 100
Cdd:cd14111     1 PQKPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSL-HHERIMALHEAYI--TP----RY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAG----SVTDLVKNTKgnalkEDCIAYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvSA 176
Cdd:cd14111    74 LVLIAEFCSGKellhSLIDRFRYSE-----DDVVGYLV-QILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFG-SA 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  177 Q-----LDRTVGRRntfIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPLCDMHP 238
Cdd:cd14111   147 QsfnplSLRQLGRR---TGTLEYMAPEMVKGEPVGPPA-----DIWSIGVLTYIMLSGRSPFEDQDP 205
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
29-221 7.91e-18

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: 84.67  E-value: 7.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRhVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAFIKKSPpgnddqLWLVME 106
Cdd:cd05085     2 ELLGKGNFGEVYKGT-LKDKTPVAVKTCKEDLPQELKIKflSEARILKQYDH-PNIVKLIGVCTQRQP------IYIVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRN 186
Cdd:cd05085    74 LVPGGDFLSFLRKKK-DELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSS 152
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 578829925  187 TFIGTPY-WMAPEVIACdenpdATYDYRSDIWSLGI 221
Cdd:cd05085   153 GLKQIPIkWTAPEALNY-----GRYSSESDVWSFGI 183
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
97-289 7.97e-18

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 84.97  E-value: 7.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 NDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN---AEVKLVDFG 173
Cdd:cd14198    79 TTSEIILILEYAAGGEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  174 VSAQLDRTVGRRNtFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR-NPP-P 251
Cdd:cd14198   159 MSRKIGHACELRE-IMGTPEYLAPEILNYDPITTAT-----DMWNIGVIAYMLLTHESPFVGEDNQETFLNISQvNVDyS 232
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 578829925  252 RLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14198   233 EETFSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
29-284 8.07e-18

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: 85.09  E-value: 8.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQL--AAIKVMD--VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFikksppGNDDQLWLV 104
Cdd:cd05047     1 DVIGEGNFGQVLKARIKKDGLRmdAAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGAC------EHRGYLYLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVK--------------NTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV 170
Cdd:cd05047    75 IEYAPHGNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  171 DFGVS----AQLDRTVGRRNTfigtpYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAE-GAPPLCDMHPMRALFLI 245
Cdd:cd05047   155 DFGLSrgqeVYVKKTMGRLPV-----RWMAIESLNY-----SVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKL 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 578829925  246 PRNppPRL-KSKKWSKKFIDFIDTCLIKTYLSRPPTEQLL 284
Cdd:cd05047   225 PQG--YRLeKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 262
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
25-232 8.40e-18

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: 84.85  E-value: 8.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE-------EIKQEINMLKKYSHHrNIATYYGAFIKKSppgn 97
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASrrgvsreDIEREVSILRQVLHP-NIITLHDVFENKT---- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 ddQLWLVMEFCGAGSVTDLVKNtKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLTE----NAEVKLVDFG 173
Cdd:cd14105    82 --DVVLILELVAGGELFDFLAE-KESLSEEEATEFL-KQILDGVNYLHTKNIAHFDLKPENIMLLDknvpIPRIKLIDFG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  174 VSAQLDRTVGRRNTFiGTPYWMAPEVIACDE-NPDAtydyrsDIWSLGITAIEMAEGAPP 232
Cdd:cd14105   158 LAHKIEDGNEFKNIF-GTPEFVAPEIVNYEPlGLEA------DMWSIGVITYILLSGASP 210
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
25-232 8.66e-18

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 85.16  E-value: 8.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLA----AIKVM--DVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKsppgnd 98
Cdd:cd05057     9 LEKGKVLGSGAFGTVYKGVWIPEGEKVkipvAIKVLreETGPKANEEILDEAYVMASVDH-PHLVRLLGICLSS------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd05057    82 -QVQLITQLMPLGCLLDYVRNHRDNIGSQLLLNW-CVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  179 DRTVGRRNTFIG-TPY-WMAPEVIACDEnpdatYDYRSDIWSLGITAIE-MAEGAPP 232
Cdd:cd05057   160 DVDEKEYHAEGGkVPIkWMALESIQYRI-----YTHKSDVWSYGVTVWElMTFGAKP 211
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
32-173 1.10e-17

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: 80.95  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHVKTGQLAAIKVMD-VTEDEEEEIKQEINMLKKYS-HHRNIATYYGAFIkksppgNDDQLWLVMEFCG 109
Cdd:cd13968     2 GEGASAKVFWAEGECTTIGVAVKIGDdVNNEEGEDLESEMDILRRLKgLELNIPKVLVTED------VDGPNILLMELVK 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  110 AGSVTDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG 173
Cdd:cd13968    76 GGTLIAYTQEEE---LDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
29-227 1.11e-17

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 85.09  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKtgQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHrNIATYYGAfiKKSPPGNDDQLWLVMEFC 108
Cdd:cd14141     1 EIKARGRFGCVWKAQLLN--EYVAVKIFPIQDKLSWQNEYEIYSLPGMKHE-NILQFIGA--EKRGTNLDVDLWLITAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKntkGNALKEDCIAYICREILRGLAHLH--------AHK--VIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd14141    76 EKGSLTDYLK---ANVVSWNELCHIAQTMARGLAYLHedipglkdGHKpaIAHRDIKSKNVLLKNNLTACIADFGLALKF 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  179 D--RTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMA 227
Cdd:cd14141   153 EagKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELA 203
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
32-226 1.20e-17

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: 83.87  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHVKTGQLAaIKVMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSPpgnddqLWLVMEFCGAG 111
Cdd:cd05034     4 GAGQFGEVWMGVWNGTTKVA-VKTLKPGTMSPEAFLQEAQIMKKL-RHDKLVQLYAVCSDEEP------IYIVTELMSKG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  112 SVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGT 191
Cdd:cd05034    76 SLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAREGAKF 155
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 578829925  192 PY-WMAPEVIACDenpdaTYDYRSDIWSLGITAIEM 226
Cdd:cd05034   156 PIkWTAPEAALYG-----RFTIKSDVWSFGILLYEI 186
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
25-231 1.25e-17

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 84.89  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKV----MDVTEDEEEEIKqEINMLKKYSHHRNIATYYGafIKKSPPGNDDQ 100
Cdd:cd07837     3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKKtrleMEEEGVPSTALR-EVSLLQMLSQSIYIVRLLD--VEHVEENGKPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAG--SVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV-KLVDFGVSAQ 177
Cdd:cd07837    80 LYLVFEYLDTDlkKFIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGLGRA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07837   160 FTIPIKSYTHEIVTLWYRAPEVLLGSTH----YSTPVDMWSVGCIFAEMSRKQP 209
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
26-221 1.35e-17

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: 83.94  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGrhVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSPpgnddqLWLVM 105
Cdd:cd05039     9 KLGELIGKGEFGDVMLG--DYRGQKVAVKCLKDDSTAAQAFLAEASVMTTLRH-PNLVQLLGVVLEGNG------LYIVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKnTKGNAL--KEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS--AQLDRT 181
Cdd:cd05039    80 EYMAKGSLVDYLR-SRGRAVitRKDQLGF-ALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAkeASSNQD 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578829925  182 VGRrntfigTPY-WMAPEVIACDEnpdatYDYRSDIWSLGI 221
Cdd:cd05039   158 GGK------LPIkWTAPEALREKK-----FSTKSDVWSFGI 187
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
31-288 1.52e-17

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 83.86  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIA---TYygafikKSPPgnddQLWLVMEF 107
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYITlhdTY------ESPT----SYILVLEL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVSAQLdrTVGR 184
Cdd:cd14115    71 MDDGRLLDYLMNH--DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQI--SGHR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  185 R-NTFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR---NPPPRLKSKKwSK 260
Cdd:cd14115   147 HvHHLLGNPEFAAPEVIQGTPVSLAT-----DIWSIGVLTYVMLSGVSPFLDESKEETCINVCRvdfSFPDEYFGDV-SQ 220
                         250       260
                  ....*....|....*....|....*...
gi 578829925  261 KFIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14115   221 AARDFINVILQEDPRRRPTAATCLQHPW 248
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
31-231 1.58e-17

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: 84.67  E-value: 1.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAFikksppGNDDQLWLVMEFc 108
Cdd:cd07873    10 LGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTaiREVSLLKDLKH-ANIVTLHDII------HTEKSLTLVFEY- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 gagsvtdLVKNTK------GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd07873    82 -------LDKDLKqylddcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPT 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578829925  183 GRRNTFIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07873   155 KTYSNEVVTLWYRPPDILLGSTD----YSTQIDMWGVGCIFYEMSTGRP 199
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
25-296 1.91e-17

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: 84.14  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKySHHRNIATYYGAFikKSPpgndDQLWLV 104
Cdd:cd14104     2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNI-ARHRNILRLHESF--ESH----EELVMI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDRTV 182
Cdd:cd14104    75 FEFISGVDIFERITTARFELNEREIVSYV-RQVCEALEFLHSKNIGHFDIRPENIIYCtrRGSYIKIIEFGQSRQLKPGD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIgTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAPPLCDMHPMRALFLIpRNPPPRLKS---KKWS 259
Cdd:cd14104   154 KFRLQYT-SAEFYAPEVHQHESVSTAT-----DMWSLGCLVYVLLSGINPFEAETNQQTIENI-RNAEYAFDDeafKNIS 226
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578829925  260 KKFIDFIDTCLIKTYLSRPPTEQLLKFPFIRdQPTER 296
Cdd:cd14104   227 IEALDFVDRLLVKERKSRMTAQEALNHPWLK-QGMET 262
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
29-232 1.99e-17

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 85.10  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDeeeeiKQEI-------NMLKKYSHHRNIATYYgAFIKKsppgndD 99
Cdd:cd05571     1 KVLGKGTFGKVILCREKATGELYAIKILkkEVIIA-----KDEVahtltenRVLQNTRHPFLTSLKY-SFQTN------D 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSV-TDLVKNTKgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQl 178
Cdd:cd05571    69 RLCFVMEYVNGGELfFHLSRERV---FSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKE- 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  179 DRTVGRR-NTFIGTPYWMAPEVIacDENpdatyDY-RS-DIWSLGITAIEMAEGAPP 232
Cdd:cd05571   145 EISYGATtKTFCGTPEYLAPEVL--EDN-----DYgRAvDWWGLGVVMYEMMCGRLP 194
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
25-232 1.99e-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: 83.93  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHvkTGQLAAIKVM------DVTEDEEEeIKQEINMLKKYSHhRNIATYYGAFIKksppgnD 98
Cdd:cd14147     5 LRLEEVIGIGGFGKVYRGSW--RGELVAVKAArqdpdeDISVTAES-VRQEARLFAMLAH-PNIIALKAVCLE------E 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSvtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHK---VIHRDIKGQNVLLTENAE--------V 167
Cdd:cd14147    75 PNLCLVMEYAAGGP---LSRALAGRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIEnddmehktL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  168 KLVDFGVSAQLDRTVgrRNTFIGTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14147   152 KITDFGLAREWHKTT--QMSAAGTYAWMAPEVIKA-----STFSKGSDVWSFGVLLWELLTGEVP 209
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
31-226 2.01e-17

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 83.84  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIK-VMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKksppgnDDQLWLVMEFCG 109
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKeLIRCDEETQKTFLTEVKVMRSLDH-PNVLKFIGVLYK------DKRLNLLTEFIE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  110 AGSVTDLVKNTKGNALKEDciAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL----------- 178
Cdd:cd14222    74 GGTLKDFLRADDPFPWQQK--VSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIveekkkpppdk 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  179 ----DRTVGR-----RNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd14222   152 pttkKRTLRKndrkkRYTVVGNPYWMAPEMLN-----GKSYDEKVDIFSFGIVLCEI 203
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
30-293 2.08e-17

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: 84.74  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEikqEINMLKKY-----SHHRNIATYYGAFIKKSppgnddQLW 102
Cdd:cd05592     2 VLGKGSFGKVMLAELKGTNQYFAIKALkkDVVLEDDDV---ECTMIERRvlalaSQHPFLTHLFCTFQTES------HLF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGsvtDLVKNTKGNA-LKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ---L 178
Cdd:cd05592    73 FVMEYLNGG---DLMFHIQQSGrFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKEniyG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVgrrNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPL--CDMHpmrALFLIPRNPPPrlksk 256
Cdd:cd05592   150 ENKA---STFCGTPDYIAPEILKGQK-----YNQSVDWWSFGVLLYEMLIGQSPFhgEDED---ELFWSICNDTP----- 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 578829925  257 kWSKKFIDFIDTCLIKTYLSRPPTEQL----LKFPFIRDQP 293
Cdd:cd05592   214 -HYPRWLTKEAASCLSLLLERNPEKRLgvpeCPAGDIRDHP 253
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
25-226 2.29e-17

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: 83.64  E-value: 2.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHvKTGQLAAIKVMDV-TEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKSPPgnddqLWL 103
Cdd:cd05148     8 FTLERKLGSGYFGEVWEGLW-KNRVRVAIKILKSdDLLKQQDFQKEVQALKRLRHKHLISLF--AVCSVGEP-----VYI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV- 182
Cdd:cd05148    80 ITELMEKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVy 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578829925  183 GRRNTFIgtPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd05148   160 LSSDKKI--PYkWTAPEAAS-----HGTFSTKSDVWSFGILLYEM 197
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
29-236 2.49e-17

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: 83.06  E-value: 2.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAFIKKSPpgnddqLWLVME 106
Cdd:cd05084     2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAKflQEARILKQYSH-PNIVRLIGVCTQKQP------IYIVME 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKnTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV---- 182
Cdd:cd05084    75 LVQGGDFLTFLR-TEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVyaat 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  183 -GRRNTFIGtpyWMAPEVIACdenpdATYDYRSDIWSLGITAIE-MAEGAPPLCDM 236
Cdd:cd05084   154 gGMKQIPVK---WTAPEALNY-----GRYSSESDVWSFGILLWEtFSLGAVPYANL 201
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
25-233 2.54e-17

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: 84.67  E-value: 2.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEikqEINMLKKyshhRNIAtyygafIKKSPP------- 95
Cdd:cd05616     2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILkkDVVIQDDDV---ECTMVEK----RVLA------LSGKPPfltqlhs 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 --GNDDQLWLVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG 173
Cdd:cd05616    69 cfQTMDRLYFVMEYVNGGDLMYHIQQV--GRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFG 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  174 VSAQ--LDRTVGRrnTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05616   147 MCKEniWDGVTTK--TFCGTPDYIAPEIIAYQ-----PYGKSVDWWAFGVLLYEMLAGQAPF 201
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
31-232 2.54e-17

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 84.47  E-value: 2.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKV---------MDVTedeeeeiKQEINMLKKYShHRNIATYYGafIKKSPPGNDDQl 101
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVfnnlsfmrpLDVQ-------MREFEVLKKLN-HKNIVKLFA--IEEELTTRHKV- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 wLVMEFCGAGSV-TDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVL--LTENAEV--KLVDFGVSa 176
Cdd:cd13988    70 -LVMELCPCGSLyTVLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSvyKLTDFGAA- 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  177 qldRTVGRRNTFI---GTPYWMAP---EVIACDENPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd13988   148 ---RELEDDEQFVslyGTEEYLHPdmyERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLP 206
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
21-274 2.56e-17

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: 83.55  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGRHVKTGQLAaIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKSPPgnddq 100
Cdd:cd05072     5 PRESIKLVKKLGAGQFGEVWMGYYNNSTKVA-VKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLY--AVVTKEEP----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL-D 179
Cdd:cd05072    77 IYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIeD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAEGA----PPLCDMHPMRAL---FLIPR--NPP 250
Cdd:cd05072   157 NEYTAREGAKFPIKWTAPEAINF-----GSFTIKSDVWSFGILLYEIVTYGkipyPGMSNSDVMSALqrgYRMPRmeNCP 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  251 PRL--------KSKKWSKKFIDFIDTCLIKTY 274
Cdd:cd05072   232 DELydimktcwKEKAEERPTFDYLQSVLDDFY 263
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
25-235 2.58e-17

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: 83.50  E-value: 2.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYShHRNIATYYGAFikkspPGNDDQ 100
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRflprELQIVERLD-HKNIIHVYEML-----ESADGK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLtENAEVKLVDFGVSAQLdr 180
Cdd:cd14163    76 IYLVMELAEDGDVFDCV--LHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQL-- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  181 TVGRR---NTFIGTPYWMAPEVIAcdenpDATYDYRS-DIWSLGITAIEMAEGAPPLCD 235
Cdd:cd14163   151 PKGGRelsQTFCGSTAYAAPEVLQ-----GVPHDSRKgDIWSMGVVLYVMLCAQLPFDD 204
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
24-223 2.74e-17

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: 83.40  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRnIATYYGAFIKKSppgnddQLWL 103
Cdd:cd14107     3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLSHRR-LTCLLDQFETRK------TLIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTD-LVKntKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDR 180
Cdd:cd14107    76 ILELCSSEELLDrLFL--KGVVTEAEVKLYI-QQVLEGIGYLHGMNILHLDIKPDNILMVspTREDIKICDFGFAQEITP 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578829925  181 TVGRRNTFiGTPYWMAPEVIACDENPDATydyrsDIWSLGITA 223
Cdd:cd14107   153 SEHQFSKY-GSPEFVAPEIVHQEPVSAAT-----DIWALGVIA 189
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
31-232 2.79e-17

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: 83.73  E-value: 2.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYsHHRNIATYYGAFIKKsppgndDQLWLVME 106
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETmalnEKIILEKV-SSPFIVSLAYAFETK------DKLCLVLT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL---DRTVG 183
Cdd:cd05577    74 LMNGGDLKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFkggKKIKG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578829925  184 RrntfIGTPYWMAPEVIACDEnpdaTYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05577   154 R----VGTHGYMAPEVLQKEV----AYDFSVDWFALGCMLYEMIAGRSP 194
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
25-231 2.81e-17

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 84.10  E-value: 2.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE---EEIKQEINMLKKYsHHRNIATYYGAFikksppGNDDQL 101
Cdd:PLN00009    4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEgvpSTAIREISLLKEM-QHGNIVRLQDVV------HSEKRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGagsvTDLVK---NTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT-ENAEVKLVDFGVSAQ 177
Cdd:PLN00009   77 YLVFEYLD----LDLKKhmdSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLARA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIACDEnpdaTYDYRSDIWSLGITAIEMAEGAP 231
Cdd:PLN00009  153 FGIPVRTFTHEVVTLWYRAPEILLGSR----HYSTPVDIWSVGCIFAEMVNQKP 202
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
31-233 3.43e-17

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: 83.70  E-value: 3.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGR----HVKTGQLAAIkVMDVTEDEEEEIKQEINMLKKYSHHrNIATYYGAfikkSPPGndDQLWLVME 106
Cdd:cd14158    23 LGEGGFGVVFKGYindkNVAVKKLAAM-VDISTEDLTKQFEQEIQVMAKCQHE-NLVELLGY----SCDG--PQLCLVYT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVkntkgnALKEDCIA-------YICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV---SA 176
Cdd:cd14158    95 YMPNGSLLDRL------ACLNDTPPlswhmrcKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLaraSE 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  177 QLDRTVGRRnTFIGTPYWMAPEVIACDENPdatydyRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14158   169 KFSQTIMTE-RIVGTTAYMAPEALRGEITP------KSDIFSFGVVLLEIITGLPPV 218
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
29-233 3.72e-17

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: 84.25  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFikksppGNDDQLWLV 104
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQkktiLKKKEQNHIMAERNVLLKNLKHPFLVGLHYSF------QTSEKLYFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGR 184
Cdd:cd05603    75 LDYVNGGEL--FFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEET 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578829925  185 RNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05603   153 TSTFCGTPEYLAPEVLR--KEP---YDRTVDWWCLGAVLYEMLYGLPPF 196
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
25-231 4.05e-17

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


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 84.22  E-value: 4.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINML--------KKYSHHrnIATYYGAFIKKSppg 96
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILtllntkydPEDKHH--IVRLLDHFMHHG--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 nddQLWLVMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN--AEVKLVDFGV 174
Cdd:cd14212    76 ---HLCIVFELLGV-NLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGS 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  175 SAQLDRTVgrrNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd14212   152 ACFENYTL---YTYIQSRFYRSPEVLL--GLP---YSTAIDMWSLGCIAAELFLGLP 200
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
21-232 4.24e-17

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: 83.23  E-value: 4.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEV-VGNGTYGQVYKGRHVKTG-QLAAIKVMD--VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikKSPPG 96
Cdd:cd14031     7 PGGRFLKFDIeLGRGAFKTVYKGLDTETWvEVAWCELQDrkLTKAEQQRFKEEAEMLKGL-QHPNIVRFYDSW--ESVLK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 NDDQLWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLT-ENAEVKLVDFG 173
Cdd:cd14031    84 GKKCIVLVTELMTSGTLKTYLKRFK--VMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLG 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  174 VSAQLDRTVGRrnTFIGTPYWMAPEVIacdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14031   162 LATLMRTSFAK--SVIGTPEFMAPEMY------EEHYDESVDVYAFGMCMLEMATSEYP 212
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
67-236 4.92e-17

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


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 85.83  E-value: 4.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   67 KQEINMLKKYSHHRNIATYYGAFIKksppgnDDQLWLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHA 146
Cdd:COG5752    85 RQEAVRLDELGKHPQIPELLAYFEQ------DQRLYLVQEFIEGQTLAQELE--KKGVFSESQIWQLLKDLLPVLQFIHS 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  147 HKVIHRDIKGQNVLL-TENAEVKLVDFGVSAQL-DRTVGRRNTFIGTPYWMAPEVIACDENPdatydyRSDIWSLGITAI 224
Cdd:COG5752   157 RNVIHRDIKPANIIRrRSDGKLVLIDFGVAKLLtITALLQTGTIIGTPEYMAPEQLRGKVFP------ASDLYSLGVTCI 230
                         170
                  ....*....|..
gi 578829925  225 EMAEGAPPLcDM 236
Cdd:COG5752   231 YLLTGVSPF-DL 241
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
19-308 5.94e-17

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 85.09  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   19 RDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdvteDEEEEIKQEINMLKKYSHHRNIA----TYYGAFIKKsp 94
Cdd:PTZ00036   62 RSPNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV----LQDPQYKNRELLIMKNLNHINIIflkdYYYTECFKK-- 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   95 pgNDDQLWL--VMEFCgAGSVTDLVKNTKGN--ALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE-VKL 169
Cdd:PTZ00036  136 --NEKNIFLnvVMEFI-PQTVHKYMKHYARNnhALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  170 VDFGVSAQLdrTVGRRN-TFIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR- 247
Cdd:PTZ00036  213 CDFGSAKNL--LAGQRSvSYICSRFYRAPELMLGATN----YTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQv 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  248 ------------NPP------PRLKSKKWSKKF--------IDFIDTCLIKTYLSRPPTEQLLKFPFIRDQpteRQVRIQ 301
Cdd:PTZ00036  287 lgtptedqlkemNPNyadikfPDVKPKDLKKVFpkgtpddaINFISQFLKYEPLKRLNPIEALADPFFDDL---RDPCIK 363

                  ....*..
gi 578829925  302 LKDHIDR 308
Cdd:PTZ00036  364 LPKYIDK 370
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
30-232 6.04e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 82.34  E-value: 6.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGrhVKTGQLAAIKVM------DVTEDEEEeIKQEINMLKKYsHHRNIATYYGAFIKksPPgnddQLWL 103
Cdd:cd14148     1 IIGVGGFGKVYKG--LWRGEEVAVKAArqdpdeDIAVTAEN-VRQEARLFWML-QHPNIIALRGVCLN--PP----HLCL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSvtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHK---VIHRDIKGQNVLLTENAE--------VKLVDF 172
Cdd:cd14148    71 VMEYARGGA---LNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPIEnddlsgktLKITDF 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  173 GVSAQLDRTVgrRNTFIGTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14148   148 GLAREWHKTT--KMSAAGTYAWMAPEVIRL-----SLFSKSSDVWSFGVLLWELLTGEVP 200
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
25-229 6.31e-17

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


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 83.77  E-value: 6.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHR-----NIATYYGAFIkksppgNDD 99
Cdd:cd14134    14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAAKIEIDVLETLAEKDpngksHCVQLRDWFD------YRG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT----------------- 162
Cdd:cd14134    88 HMCIVFELLGP-SLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVdsdyvkvynpkkkrqir 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  163 --ENAEVKLVDFGvSAQLDRTvgRRNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEG 229
Cdd:cd14134   167 vpKSTDIKLIDFG-SATFDDE--YHSSIVSTRHYRAPEVIL--GLG---WSYPCDVWSIGCILVELYTG 227
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
25-235 6.57e-17

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 82.87  E-value: 6.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVK-TGQLAAIKVM--------DVTEDEEEEIKQEINMLKKYSHhRNIATYYgAFIKkspp 95
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAVPLRnTGKPVAIKVVrkadlssdNLKGSSRANILKEVQIMKRLSH-PNIVKLL-DFQE---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 gNDDQLWLVMEFCGAGSVTD-LVKNTkgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL------------- 161
Cdd:cd14096    77 -SDEYYYIVLELADGGEIFHqIVRLT---YFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  162 ------TENAE--------------VKLVDFGVSAQLDRTVGRrnTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGI 221
Cdd:cd14096   153 kadddeTKVDEgefipgvggggigiVKLADFGLSKQVWDSNTK--TPCGTVGYTAPEVVKDER-----YSKKVDMWALGC 225
                         250
                  ....*....|....
gi 578829925  222 TAIEMAEGAPPLCD 235
Cdd:cd14096   226 VLYTLLCGFPPFYD 239
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
133-232 6.99e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 85.62  E-value: 6.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  133 ICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG----VSAQldrTVGRRNTFIGTPYWMAPEVIAcdenpDA 208
Cdd:NF033483  112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaraLSST---TMTQTNSVLGTVHYLSPEQAR-----GG 183
                          90       100
                  ....*....|....*....|....
gi 578829925  209 TYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:NF033483  184 TVDARSDIYSLGIVLYEMLTGRPP 207
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
29-233 7.07e-17

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 83.42  E-value: 7.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEE--EEIKQEINMLKKYSHHRNIATYYGAFikKSPpgndDQLWLV 104
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGRLYAVKVLkkDVILQDDdvECTMTEKRILSLARNHPFLTQLYCCF--QTP----DRLFFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGR 184
Cdd:cd05590    75 MEFVNGGDLMFHIQ--KSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKT 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578829925  185 RNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05590   153 TSTFCGTPDYIAPEILQ-----EMLYGPSVDWWAMGVLLYEMLCGHAPF 196
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
25-220 7.15e-17

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: 82.93  E-value: 7.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE---EIKQEINMLKKYsHHRNIATYYGAFIKKSPP----GN 97
Cdd:cd07864     9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpiTAIREIKILRQL-NHRSVVNLKEIVTDKQDAldfkKD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 DDQLWLVMEFCGAgsvtDLVK--NTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVs 175
Cdd:cd07864    88 KGAFYLVFEYMDH----DLMGllESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGL- 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  176 AQLDRTVGRR---NTFIgTPYWMAPEVIACDENpdatYDYRSDIWSLG 220
Cdd:cd07864   163 ARLYNSEESRpytNKVI-TLWYRPPELLLGEER----YGPAIDVWSCG 205
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
25-284 7.20e-17

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: 82.56  E-value: 7.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK---VMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSPPgnddQL 101
Cdd:cd14049     8 FEEIARLGKGGYGKVYKVRNKLDGQYYAIKkilIKKVTKRDCMKVLREVKVLAGL-QHPNIVGYHTAWMEHVQL----ML 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAgSVTDLV--KNTKGNALKEDCIAY----------ICREILRGLAHLHAHKVIHRDIKGQNVLLTENA-EVK 168
Cdd:cd14049    83 YIQMQLCEL-SLWDWIveRNKRPCEEEFKSAPYtpvdvdvttkILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDiHVR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  169 LVDFGV-----------SAQLDRTVGRRNTF-IGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEgaPPLCDM 236
Cdd:cd14049   162 IGDFGLacpdilqdgndSTTMSRLNGLTHTSgVGTCLYAAPEQLEGSH-----YDFKSDMYSIGVILLELFQ--PFGTEM 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  237 HPMRALFLIPRNPPPRLKSKKWsKKFIDFIDTCLIKTYLSRPPTEQLL 284
Cdd:cd14049   235 ERAEVLTQLRNGQIPKSLCKRW-PVQAKYIKLLTSTEPSERPSASQLL 281
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
27-232 7.28e-17

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: 82.92  E-value: 7.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGRHVKTGQLA-----AIKVM--DVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPPgndd 99
Cdd:cd05054    11 LGKPLGRGAFGKVIQASAFGIDKSAtcrtvAVKMLkeGATASEHKALMTELKILIHIGHHLNVVNLLGACTKPGGP---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 qLWLVMEFCGAGSVTDLVKNTKGNALK-------------------------EDCIAYiCREILRGLAHLHAHKVIHRDI 154
Cdd:cd05054    87 -LMVIVEFCKFGNLSNYLRSKREEFVPyrdkgardveeeedddelykepltlEDLICY-SFQVARGMEFLASRKCIHRDL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  155 KGQNVLLTENAEVKLVDFGvsaqLDRTVGR-----RNTFIGTPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEM-A 227
Cdd:cd05054   165 AARNILLSENNVVKICDFG----LARDIYKdpdyvRKGDARLPLkWMAPESIF-----DKVYTTQSDVWSFGVLLWEIfS 235

                  ....*
gi 578829925  228 EGAPP 232
Cdd:cd05054   236 LGASP 240
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
30-232 7.81e-17

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: 82.01  E-value: 7.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGrhVKTGQLAAIKVM------DVTEDEEEeIKQEINMLKKYsHHRNIATYYGAFIKKSppgnddQLWL 103
Cdd:cd14146     1 IIGVGGFGKVYRA--TWKGQEVAVKAArqdpdeDIKATAES-VRQEAKLFSML-RHPNIIKLEGVCLEEP------NLCL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKGNA-------LKEDCIAYICREILRGLAHLHAHKV---IHRDIKGQNVLLTENAE------- 166
Cdd:cd14146    71 VMEFARGGTLNRALAAANAAPgprrarrIPPHILVNWAVQIARGMLYLHEEAVvpiLHRDLKSSNILLLEKIEhddicnk 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  167 -VKLVDFGVSAQLDRTVgrRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14146   151 tLKITDFGLAREWHRTT--KMSAAGTYAWMAPEVIK-----SSLFSKGSDIWSYGVLLWELLTGEVP 210
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
25-233 8.08e-17

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: 83.43  E-value: 8.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEikqEINMLKKYS-----HHRNIATYYGAFIKKsppgn 97
Cdd:cd05619     7 FVLHKMLGKGSFGKVFLAELKGTNQFFAIKALkkDVVLMDDDV---ECTMVEKRVlslawEHPFLTHLFCTFQTK----- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 dDQLWLVMEFCGAGSVTDLVKNTKGNALKEDciAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd05619    79 -ENLFFVMEYLNGGDLMFHIQSCHKFDLPRA--TFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05619   156 NMLGDAKTSTFCGTPDYIAPEILLGQK-----YNTSVDWWSFGVLLYEMLIGQSPF 206
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
28-231 9.24e-17

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: 82.32  E-value: 9.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKsppgndDQLWLVM 105
Cdd:cd07870     5 LEKLGEGSYATVYKGISRINGQLVALKVisMKTEEGVPFTAIREASLLKGLKH-ANIVLLHDIIHTK------ETLTFVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR 185
Cdd:cd07870    78 EYMHTDLAQYMIQHPGG--LHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTY 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  186 NTFIGTPYWMAPEVIAcdenpdATYDYRS--DIWSLGITAIEMAEGAP 231
Cdd:cd07870   156 SSEVVTLWYRPPDVLL------GATDYSSalDIWGAGCIFIEMLQGQP 197
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
26-227 9.34e-17

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: 82.01  E-value: 9.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKG--RHVKTGQL---AAIKVMDVTEDEEEEIK--QEINMLKKYSHHrNIATYYGAFIKKSPPgnd 98
Cdd:cd05032     9 TLIRELGQGSFGMVYEGlaKGVVKGEPetrVAIKTVNENASMRERIEflNEASVMKEFNCH-HVVRLLGVVSTGQPT--- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dqlWLVMEFCGAGSVTDLVKNTKGNAlkEDCIAYI----------CREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVK 168
Cdd:cd05032    85 ---LVVMELMAKGDLKSYLRSRRPEA--ENNPGLGpptlqkfiqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  169 LVDFGVSAQLDRTVGRRNTFIGT-PY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMA 227
Cdd:cd05032   160 IGDFGMTRDIYETDYYRKGGKGLlPVrWMAPESLK-----DGVFTTKSDVWSFGVVLWEMA 215
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
25-233 9.64e-17

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 81.62  E-value: 9.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTE--DEEEEIKQEINMLKKYSHHRNIAtyygaFIKKSPpgNDDQLW 102
Cdd:cd14184     3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKccGKEHLIENEVSILRRVKHPNIIM-----LIEEMD--TPAELY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE----VKLVDFGVSAQL 178
Cdd:cd14184    76 LVMELVKGGDLFDAI--TSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDgtksLKLGDFGLATVV 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  179 DrtvGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14184   154 E---GPLYTVCGTPTYVAPEIIA-----ETGYGLKVDIWAAGVITYILLCGFPPF 200
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
4-255 9.73e-17

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 83.54  E-value: 9.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925    4 PAPARSLDDIDLSALRDPAGI----FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdvtedeeeeiKQEINMLKKYSHH 79
Cdd:cd05594     2 PSDNSGAEEMEVSLTKPKHKVtmndFEYLKLLGKGTFGKVILVKEKATGRYYAMKIL----------KKEVIVAKDEVAH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   80 -----RNIATYYGAFIK--KSPPGNDDQLWLVMEFCGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHK-VIH 151
Cdd:cd05594    72 tltenRVLQNSRHPFLTalKYSFQTHDRLCFVMEYANGGEL--FFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  152 RDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd05594   150 RDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRL 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578829925  232 PLCDMHPMRALFLI-------PRNPPPRLKS 255
Cdd:cd05594   225 PFYNQDHEKLFELIlmeeirfPRTLSPEAKS 255
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
16-233 1.04e-16

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 82.75  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   16 SALRDpagiFELVEVVGNGTYGQVYKGRHVKTGQLAAIK-VMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAFIKK 92
Cdd:cd07866     5 SKLRD----YEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHNEKDGFPITalREIKILKKLKH-PNVVPLIDMAVER 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 SPPGNDDQLWLVMEF-------CGagsvtdLVKNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA 165
Cdd:cd07866    80 PDKSKRKRGSVYMVTpymdhdlSG------LLENPSVK-LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQG 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  166 EVKLVDFGVSAQLD---------RTVGRRN--TFIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd07866   153 ILKIADFGLARPYDgpppnpkggGGGGTRKytNLVVTRWYRPPELLLGERR----YTTAVDIWGIGCVFAEMFTRRPIL 227
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
24-289 1.12e-16

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 81.15  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIK------VMDVTEDEEEEIKQEINMLKKyshhrnIATYYGAFIK-----K 92
Cdd:cd14102     1 VYQVGSVLGSGGFGTVYAGSRIADGLPVAVKhvvkerVTEWGTLNGVMVPLEIVLLKK------VGSGFRGVIKlldwyE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   93 SPpgndDQLWLVMEfcgagsVTDLVKN-----TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL-TENAE 166
Cdd:cd14102    75 RP----DGFLIVME------RPEPVKDlfdfiTEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  167 VKLVDFGVSAQLDRTVgrRNTFIGTPYWMAPEVIACDEnpdatYDYRS-DIWSLGITAIEMAEGAPPL-CDMHPMRALFL 244
Cdd:cd14102   145 LKLIDFGSGALLKDTV--YTDFDGTRVYSPPEWIRYHR-----YHGRSaTVWSLGVLLYDMVCGDIPFeQDEEILRGRLY 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578829925  245 IPRNPPPRLKSkkwskkfidFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14102   218 FRRRVSPECQQ---------LIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
25-235 1.17e-16

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: 81.35  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEInMLKKYSHHRNIATYYGAFIKKSppgnddQLWLV 104
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREI-INHRSLRHPNIIRFKEVVLTPT------HLAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL--TENAEVKLVDFGVSAQldrTV 182
Cdd:cd14662    75 MEYAAGGELFERICNA--GRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKS---SV 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  183 --GRRNTFIGTPYWMAPEVIACDEnpdatYDYR-SDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd14662   150 lhSQPKSTVGTPAYIAPEVLSRKE-----YDGKvADVWSCGVTLYVMLVGAYPFED 200
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
30-232 1.51e-16

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: 82.44  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVM--DVtedeeeeIKQ----EINMLKKyshhRNIAtyygafIKKSPP-------- 95
Cdd:cd05587     3 VLGKGSFGKVMLAERKGTDELYAIKILkkDV-------IIQdddvECTMVEK----RVLA------LSGKPPfltqlhsc 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 -GNDDQLWLVMEFCGAGsvtDLVKN-TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG 173
Cdd:cd05587    66 fQTMDRLYFVMEYVNGG---DLMYHiQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFG 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  174 VSAqlDRTVGRRNT--FIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05587   143 MCK--EGIFGGKTTrtFCGTPDYIAPEIIA--YQP---YGKSVDWWAYGVLLYEMLAGQPP 196
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
25-306 1.56e-16

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 82.76  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEeikQEINMLKKYSHHRNIATYYGAFikksppgnDD--QLW 102
Cdd:cd14176    21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT---EEIEILLRYGQHPNIITLKDVY--------DDgkYVY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGNALKEdcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA----EVKLVDFGVSAQL 178
Cdd:cd14176    90 VVTELMKGGELLDKILRQKFFSERE--ASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMhpmralfliPRNPPPRLKSKKW 258
Cdd:cd14176   168 RAENGLLMTPCYTANFVAPEVLE-----RQGYDAACDIWSLGVLLYTMLTGYTPFANG---------PDDTPEEILARIG 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  259 SKKF---------IDFIDTCLIKTYLSRPPTE-----QLLKFPFI--RDQPTERQVRIQLKDHI 306
Cdd:cd14176   234 SGKFslsggywnsVSDTAKDLVSKMLHVDPHQrltaaLVLRHPWIvhWDQLPQYQLNRQDAPHL 297
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
36-252 1.60e-16

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: 81.28  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   36 YGQVYKGRHVktgqlaAIKVMDVTEDEEEEIKQEINMLkKYSHHRNIATYYGAFIkksppgNDDQLWLVMEFCGAGSVTD 115
Cdd:cd13992    19 KVGVYGGRTV------AIKHITFSRTEKRTILQELNQL-KELVHDNLNKFIGICI------NPPNIAVVTEYCTRGSLQD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  116 LVKNTKgnaLKEDCIAYIC--REILRGLAHLHAHKVI-HRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTP 192
Cdd:cd13992    86 VLLNRE---IKMDWMFKSSfiKDIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQH 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  193 Y---WMAPEVIACDENPDATyDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR--NPPPR 252
Cdd:cd13992   163 KkllWTAPELLRGSLLEVRG-TQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISggNKPFR 226
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
24-289 1.64e-16

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: 81.48  E-value: 1.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFikKSPpgndDQL 101
Cdd:cd14169     4 VYELKEKLGEGAFSEVVLAQERGSQRLVALKCIpkKALRGKEAMVENEIAVLRRINH-ENIVSLEDIY--ESP----THL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNtKGNALKEDCiAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVSAQL 178
Cdd:cd14169    77 YLAMELVTGGELFDRIIE-RGSYTEKDA-SQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKIE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRtvGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRnPPPRLKSKKW 258
Cdd:cd14169   155 AQ--GMLSTACGTPGYVAPELLE-----QKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILK-AEYEFDSPYW 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  259 ---SKKFIDFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14169   227 ddiSESAKDFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
25-231 1.77e-16

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: 81.62  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTG----QLAAIKVMDVTEDEEEEIKQEINMLKKYS--HHRNIATYYGAfIKKSPPGND 98
Cdd:cd07862     3 YECVAEIGEGAYGKVFKARDLKNGgrfvALKRVRVQTGEEGMPLSTIREVAVLRHLEtfEHPNVVRLFDV-CTVSRTDRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTKGNALKEdCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV---- 174
Cdd:cd07862    82 TKLTLVFEHVDQDLTTYLDKVPEPGVPTE-TIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLariy 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  175 SAQLDRTVgrrntFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07862   161 SFQMALTS-----VVVTLWYRAPEVLL-----QSSYATPVDLWSVGCIFAEMFRRKP 207
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
31-233 2.00e-16

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: 81.55  E-value: 2.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKV--MDVTEDEEEEIKQEINMLKKYSHHRNIATyygafiKKSPPG------NDDQLw 102
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQcrQELSPKNRERWCLEIQIMKRLNHPNVVAA------RDVPEGlqklapNDLPL- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVT---DLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV---KLVDFGVSA 176
Cdd:cd14038    75 LAMEYCQGGDLRkylNQFENCCG--LREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAK 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  177 QLDRTvGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14038   153 ELDQG-SLCTSFVGTLQYLAPELLE-----QQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
25-231 2.81e-16

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: 81.68  E-value: 2.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK-----QEINMLKKYSHHRNIATYYGAFIKKspPGNDD 99
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITNVFSKKILakralRELKLLRHFRGHKNITCLYDMDIVF--PGNFN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAgsvtDLVKNTK-GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV---- 174
Cdd:cd07857    80 ELYLYEELMEA----DLHQIIRsGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLargf 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  175 SAQLDRTVGRRNTFIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd07857   156 SENPGENAGFMTEYVATRWYRAPEIMLSFQS----YTKAIDVWSVGCILAELLGRKP 208
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
24-235 2.94e-16

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 80.83  E-value: 2.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEeeiKQEINMLKKYSHHRNIATYYGAFikksppgnDDQ--L 101
Cdd:cd14177     5 VYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDP---SEEIEILMRYGQHPNIITLKDVY--------DDGryV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALKE-DCIAYIcreILRGLAHLHAHKVIHRDIKGQNVLLTENA----EVKLVDFGVSA 176
Cdd:cd14177    74 YLVTELMKGGELLDRILRQKFFSEREaSAVLYT---ITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFAK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  177 QLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd14177   151 QLRGENGLLLTPCYTANFVAPEVLM-----RQGYDAACDIWSLGVLLYTMLAGYTPFAN 204
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
31-220 3.32e-16

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 81.65  E-value: 3.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIK----VMDVTEDEEEEIKqEINMLKKYSHHRNIAtyygafIKK--SPPGND--DQLW 102
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIKkianAFDNRIDAKRTLR-EIKLLRHLDHENVIA------IKDimPPPHREafNDVY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGagsvTDLVKNTKGN-ALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd07858    86 IVYELMD----TDLHQIIRSSqTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEK 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578829925  182 VGRRNTFIGTPYWMAPEVI-ACDEnpdatYDYRSDIWSLG 220
Cdd:cd07858   162 GDFMTEYVVTRWYRAPELLlNCSE-----YTTAIDVWSVG 196
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
25-231 3.55e-16

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 81.34  E-value: 3.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHR----NIATYYGAFIKKSppgnddQ 100
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENadefNFVRAYECFQHKN------H 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA----EVKLVDFGVSA 176
Cdd:cd14211    75 TCLVFEMLEQ-NLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFGSAS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  177 QLDRTVgrRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd14211   154 HVSKAV--CSTYLQSRYYRAPEIIL-----GLPFCEAIDMWSLGCVIAELFLGWP 201
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
29-233 3.66e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 80.03  E-value: 3.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMdvteDEEEEIKQEINMLKKYSHHRNIATYYGAFikKSPPGNDDQLWLVMEFC 108
Cdd:cd14172    10 QVLGLGVNGKVLECFHRRTGQKCALKLL----YDSPKARREVEHHWRASGGPHIVHILDVY--ENMHHGKRCLLIIMECM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGVSAQLDRTvGRR 185
Cdd:cd14172    84 EGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFAKETTVQ-NAL 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  186 NTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14172   163 QTPCYTPYYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCGFPPF 205
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
31-226 4.08e-16

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: 79.58  E-value: 4.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAaIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKSPpgnddqLWLVMEFCGA 110
Cdd:cd14203     3 LGQGCFGEVWMGTWNGTTKVA-IKTLKPGTMSPEAFLEEAQIMKKLRHDKLVQLY--AVVSEEP------IYIVTEFMSK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL-DRTVGRRNTFI 189
Cdd:cd14203    74 GSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIeDNEYTARQGAK 153
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 578829925  190 GTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEM 226
Cdd:cd14203   154 FPIKWTAPEAALY-----GRFTIKSDVWSFGILLTEL 185
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
79-290 4.12e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 82.76  E-value: 4.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   79 HRNIATYYGAFikKSppgnDDQLWLVMEFcgaGSVTDLVKNTKGN-----ALKEDCIAYICREILRGLAHLHAHKVIHRD 153
Cdd:PTZ00267  124 HFGIVKHFDDF--KS----DDKLLLIMEY---GSGGDLNKQIKQRlkehlPFQEYEVGLLFYQIVLALDEVHSRKMMHRD 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  154 IKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR--NTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:PTZ00267  195 LKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDvaSSFCGTPYYLAPELWE-----RKRYSKKADMWSLGVILYELLTLHR 269
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  232 PL---CDMHPMRALFLIPRNPPPRLKSKKWSKkfidFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:PTZ00267  270 PFkgpSQREIMQQVLYGKYDPFPCPVSSGMKA----LLDPLLSKNPALRPTTQQLLHTEFLK 327
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
29-232 4.13e-16

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 81.00  E-value: 4.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVtedeeeeIKQ----EINMLKKY-----SHHRNIATYYGAFIKKsppgn 97
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKVLkkDV-------ILQdddvDCTMTEKRilalaAKHPFLTALHSCFQTK----- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 dDQLWLVMEFCGAGSVtdLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd05591    69 -DRLFFVMEYVNGGDL--MFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKE 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  178 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05591   146 GILNGKTTTTFCGTPDYIAPEILQ-----ELEYGPSVDWWALGVLMYEMMAGQPP 195
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
31-232 4.45e-16

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 79.74  E-value: 4.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTG-QLAAIKVMD--VTEDEEEEIKQEINMLKKYsHHRNIATYYGaFIKKSPPGNDdQLWLVMEF 107
Cdd:cd14032     9 LGRGSFKTVYKGLDTETWvEVAWCELQDrkLTKVERQRFKEEAEMLKGL-QHPNIVRFYD-FWESCAKGKR-CIVLVTEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLT-ENAEVKLVDFGVsAQLDRTVGR 184
Cdd:cd14032    86 MTSGTLKTYLKRFK--VMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGL-ATLKRASFA 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  185 RnTFIGTPYWMAPEVIacdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14032   163 K-SVIGTPEFMAPEMY------EEHYDESVDVYAFGMCMLEMATSEYP 203
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
29-251 4.45e-16

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: 80.48  E-value: 4.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEEEIKQEInmlkkYS----HHRNIATYYGAFIKKSPPGNDDQLwLV 104
Cdd:cd14054     1 QLIGQGRYGTVWKGSL--DERPVAVKVFPARHRQNFQNEKDI-----YElplmEHSNILRFIGADERPTADGRMEYL-LV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTD-LVKNTkgNALKEDCIayICREILRGLAHLH-------AHK--VIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd14054    73 LEYAPKGSLCSyLRENT--LDWMSSCR--MALSLTRGLAYLHtdlrrgdQYKpaIAHRDLNSRNVLVKADGSCVICDFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  175 SAQL--DRTVGRR-----NTFI---GTPYWMAPEVI--ACDENPDATYDYRSDIWSLGITAIEMAegapplcdmhpMRAL 242
Cdd:cd14054   149 AMVLrgSSLVRGRpgaaeNASIsevGTLRYMAPEVLegAVNLRDCESALKQVDVYALGLVLWEIA-----------MRCS 217

                  ....*....
gi 578829925  243 FLIPRNPPP 251
Cdd:cd14054   218 DLYPGESVP 226
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
21-286 5.77e-16

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: 80.22  E-value: 5.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGR-----HVKTGQLAAIKVMDVT--EDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKS 93
Cdd:cd05055    33 PRNNLSFGKTLGAGAFGKVVEATayglsKSDAVMKVAVKMLKPTahSSEREALMSELKIMSHLGNHENIVNLLGACTIGG 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   94 PpgnddqLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG 173
Cdd:cd05055   113 P------ILVITEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  174 VSAQL---DRTVGRRNTFIGTPyWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM-AEGAPPLCDMhPMRALFLIPRNP 249
Cdd:cd05055   187 LARDImndSNYVVKGNARLPVK-WMAPESIF-----NCVYTFESDVWSYGILLWEIfSLGSNPYPGM-PVDSKFYKLIKE 259
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578829925  250 PPRLKSKKWSKKFI-DFIDTCLIKTYLSRPPTEQLLKF 286
Cdd:cd05055   260 GYRMAQPEHAPAEIyDIMKTCWDADPLKRPTFKQIVQL 297
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
30-310 6.04e-16

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 80.54  E-value: 6.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMD---VTEDEEEE-IKQEINMLKKYSHHRNIATYYGAFIKKSppgnddQLWLVM 105
Cdd:cd05588     2 VIGRGSYAKVLMVELKKTKRIYAMKVIKkelVNDDEDIDwVQTEKHVFETASNHPFLVGLHSCFQTES------RLFFVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGsvtDLVKNT-KGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGR 184
Cdd:cd05588    76 EFVNGG---DLMFHMqRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  185 RNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPL--------CDMHPMRALFLIPRNPP---PRL 253
Cdd:cd05588   153 TSTFCGTPNYIAPEILRGED-----YGFSVDWWALGVLMFEMLAGRSPFdivgssdnPDQNTEDYLFQVILEKPiriPRS 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  254 KSKKWSKkfidfidtcLIKTYLSRPPTEQL-----------LKFPFIR----DQPTERQVRIQLKDHIDRSR 310
Cdd:cd05588   228 LSVKAAS---------VLKGFLNKNPAERLgchpqtgfadiQSHPFFRtidwEQLEQKQVTPPYKPRIESER 290
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
29-233 7.29e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 79.69  E-value: 7.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTE-DEEEEIKQEINMLKKYSHHRNIATYYGAFikksppGNDDQLWLVME- 106
Cdd:cd14173     8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPgHSRSRVFREVEMLYQCQGHRNVLELIEFF------EEEDKFYLVFEk 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKNTKGNALKEdciAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN---AEVKLVDF--GVSAQLDR- 180
Cdd:cd14173    82 MRGGSILSHIHRRRHFNELEA---SVVVQDIASALDFLHNKGIAHRDLKPENILCEHPnqvSPVKICDFdlGSGIKLNSd 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  181 ----TVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14173   159 cspiSTPELLTPCGSAEYMAPEVVEAFNEEASIYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
22-249 7.29e-16

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: 80.12  E-value: 7.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   22 AGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAFIKKsppgndD 99
Cdd:cd07869     4 ADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTaiREASLLKGLKH-ANIVLLHDIIHTK------E 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKNTKGnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd07869    77 TLTLVFEYVHTDLCQYMDKHPGG--LHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGA---PPLCDMH-PMRALFLIPRNP 249
Cdd:cd07869   155 VPSHTYSNEVVTLWYRPPDVLL----GSTEYSTCLDMWGVGCIFVEMIQGVaafPGMKDIQdQLERIFLVLGTP 224
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
31-226 8.82e-16

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: 80.06  E-value: 8.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHV-------KTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPpgnddqL 101
Cdd:cd05101    32 LGEGCFGQVVMAEAVgidkdkpKEAVTVAVKMLkdDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGP------L 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKG---------NALKEDCIAY-----ICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 167
Cdd:cd05101   106 YVIVEYASKGNLREYLRARRPpgmeysydiNRVPEEQMTFkdlvsCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVM 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  168 KLVDFGVSAQLDRTVGRRNTFIGT-PY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd05101   186 KIADFGLARDINNIDYYKKTTNGRlPVkWMAPEALF-----DRVYTHQSDVWSFGVLMWEI 241
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
20-252 1.04e-15

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 78.57  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFeLVEVVGNGTYGQVYKGRHVKTGQ---LAAIKVMDVTEDEeeeiKQEINMLKKYS-----HHRNIATYYGAFIK 91
Cdd:cd05033     2 DASYVT-IEKVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLKSGYSD----KQRLDFLTEASimgqfDHPNVIRLEGVVTK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   92 KSPpgnddqLWLVMEFCGAGSVTDLVKNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVD 171
Cdd:cd05033    77 SRP------VMIVTEYMENGSLDKFLRENDGK-FTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  172 FGVSAQLDRTVGRRNTFIG-TPY-WMAPEVIAcdenpdatydYR-----SDIWSLGITAIE-MAEGAPPLCDM---HPMR 240
Cdd:cd05033   150 FGLSRRLEDSEATYTTKGGkIPIrWTAPEAIA----------YRkftsaSDVWSFGIVMWEvMSYGERPYWDMsnqDVIK 219
                         250
                  ....*....|..
gi 578829925  241 ALFLIPRNPPPR 252
Cdd:cd05033   220 AVEDGYRLPPPM 231
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
25-226 1.12e-15

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: 78.48  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEEEIKQEINMLKKysHHRNIATYYGAFIKKSppgndDQLWLV 104
Cdd:cd05082     8 LKLLQTIGKGEFGDVMLGDY--RGNKVAVKCIKNDATAQAFLAEASVMTQL--RHSNLVQLLGVIVEEK-----GGLYIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTvgr 184
Cdd:cd05082    79 TEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASST--- 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578829925  185 RNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd05082   156 QDTGKLPVKWTAPEALR-----EKKFSTKSDVWSFGILLWEI 192
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
25-226 1.21e-15

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: 78.76  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIK--QEINMLKKYSHhRNIATYYGAFIKKSPPGNDDQ-- 100
Cdd:cd14048     8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKvlREVRALAKLDH-PGIVRYFNAWLERPPEGWQEKmd 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 ---LWLVMEFCGAGSVTDLVKNTKGNALKEDCIA-YICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA 176
Cdd:cd14048    87 evyLYIQMQLCRKENLKDWMNRRCTMESRELFVClNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVT 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  177 QLDR-----TVG-------RRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd14048   167 AMDQgepeqTVLtpmpayaKHTGQVGTRLYMSPEQIH-----GNQYSEKVDIFALGLILFEL 223
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
31-226 1.33e-15

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: 78.57  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAaIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKSPpgnddqLWLVMEFCGA 110
Cdd:cd05069    20 LGQGCFGEVWMGTWNGTTKVA-IKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLY--AVVSEEP------IYIVTEFMGK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL-DRTVGRRNTFI 189
Cdd:cd05069    91 GSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIeDNEYTARQGAK 170
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 578829925  190 GTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEM 226
Cdd:cd05069   171 FPIKWTAPEAALY-----GRFTIKSDVWSFGILLTEL 202
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
23-237 1.49e-15

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: 78.29  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   23 GIFELVEVVGNGTYGQVYKGRHV-----KTGQLAAIKVMDVTEDEEE----EIKQEINMLKKYSHhRNIaTYYGAFIKks 93
Cdd:cd14076     1 GPYILGRTLGEGEFGKVKLGWPLpkanhRSGVQVAIKLIRRDTQQENcqtsKIMREINILKGLTH-PNI-VRLLDVLK-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   94 ppgNDDQLWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG 173
Cdd:cd14076    77 ---TKKYIGIVLEFVSGGELFDYILARR--RLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFG 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  174 VSAQLDRTVGR-RNTFIGTPYWMAPEVIACDENPDATydyRSDIWSLGITAIEMAEGAPPLCDMH 237
Cdd:cd14076   152 FANTFDHFNGDlMSTSCGSPCYAAPELVVSDSMYAGR---KADIWSCGVILYAMLAGYLPFDDDP 213
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
29-233 1.87e-15

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 78.53  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTE-DEEEEIKQEINMLKKYSHHRNIATYYGAFikksppGNDDQLWLVMEF 107
Cdd:cd14174     8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAgHSRSRVFREVETLYQCQGNKNILELIEFF------EDDTRFYLVFEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLlTENAE----VKLVDF--GVSAQLDR- 180
Cdd:cd14174    82 LRGGSILAHIQKRK--HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENIL-CESPDkvspVKICDFdlGSGVKLNSa 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  181 ----TVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14174   159 ctpiTTPELTTPCGSAEYMAPEVVEVFTDEATFYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
31-232 1.95e-15

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: 77.74  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAA---IKVMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikKSPPGNDDQLWLVMEF 107
Cdd:cd14033     9 IGRGSFKTVYRGLDTETTVEVAwceLQTRKLSKGERQRFSEEVEMLKGL-QHPNIVRFYDSW--KSTVRGHKCIILVTEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKGNALKedCIAYICREILRGLAHLHAH--KVIHRDIKGQNVLLT-ENAEVKLVDFGVsAQLDRTVGR 184
Cdd:cd14033    86 MTSGTLKTYLKRFREMKLK--LLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFITgPTGSVKIGDLGL-ATLKRASFA 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  185 RnTFIGTPYWMAPEVIacdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14033   163 K-SVIGTPEFMAPEMY------EEKYDEAVDVYAFGMCILEMATSEYP 203
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
25-283 2.02e-15

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: 78.14  E-value: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeEEEIKQ---------EINMLKKYSHHRNIATYYGAFIKkspp 95
Cdd:cd05630     2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLE-----KKRIKKrkgeamalnEKQILEKVNSRFVVSLAYAYETK---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 gndDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd05630    73 ---DALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQL--DRTVGRRntfIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMralflIPRNPPPRL 253
Cdd:cd05630   150 VHVpeGQTIKGR---VGTVGYMAPEVVK-----NERYTFSPDWWALGCLLYEMIAGQSPFQQRKKK-----IKREEVERL 216
                         250       260       270
                  ....*....|....*....|....*....|...
gi 578829925  254 ---KSKKWSKKFIDFIDTcLIKTYLSRPPTEQL 283
Cdd:cd05630   217 vkeVPEEYSEKFSPQARS-LCSMLLCKDPAERL 248
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
26-286 2.05e-15

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 78.13  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGR-HvktGQLAaIKVMDVTEDEEEEIK---QEInMLKKYSHHRNIATYYGAFIkkSPPgnddQL 101
Cdd:cd14153     3 EIGELIGKGRFGQVYHGRwH---GEVA-IRLIDIERDNEEQLKafkREV-MAYRQTRHENVVLFMGACM--SPP----HL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLtENAEVKLVDFG---VSAQL 178
Cdd:cd14153    72 AIITSLCKGRTLYSVVRDAK-VVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGlftISGVL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DrtVGRRNTFIGTPY-W---MAPEVIAcDENPDATYDY-----RSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNP 249
Cdd:cd14153   150 Q--AGRREDKLRIQSgWlchLAPEIIR-QLSPETEEDKlpfskHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSGM 226
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578829925  250 PPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKF 286
Cdd:cd14153   227 KPNLSQIGMGKEISDILLFCWAYEQEERPTFSKLMEM 263
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
31-232 2.10e-15

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: 77.92  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRhVKTGQLAAIK--VMDVTEDEEEEIKQEINMLKKySHHRNIATYYGAFikksppGNDDQLWLVMEFC 108
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKrlKGEGTQGGDHGFQAEIQTLGM-IRHRNIVRLRGYC------SNPTTNLLVYEYM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKNTKGNALKEDCIAY--ICREILRGLAHLHAH---KVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVG 183
Cdd:cd14664    73 PNGSLGELLHSRPESQPPLDWETRqrIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  184 RRNTFI-GTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14664   153 HVMSSVaGSYGYIAPEYAYT-----GKVSEKSDVYSYGVVLLELITGKRP 197
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
25-233 2.23e-15

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: 79.27  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEikqEINMLKKyshhRNIAtyygafIKKSPP------- 95
Cdd:cd05615    12 FNFLMVLGKGSFGKVMLAERKGSDELYAIKILkkDVVIQDDDV---ECTMVEK----RVLA------LQDKPPfltqlhs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 --GNDDQLWLVMEFCGAGSVTDLVKNTkgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG 173
Cdd:cd05615    79 cfQTVDRLYFVMEYVNGGDLMYHIQQV--GKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFG 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  174 VSAQ--LDRTVGRrnTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05615   157 MCKEhmVEGVTTR--TFCGTPDYIAPEIIAYQ-----PYGRSVDWWAYGVLLYEMLAGQPPF 211
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
26-221 2.47e-15

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: 77.85  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGRHVKTGQLA---AIKV--MDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFikksppgNDDQ 100
Cdd:cd05056     9 TLGRCIGEGQFGDVYQGVYMSPENEKiavAVKTckNCTSPSVREKFLQEAYIMRQFDH-PHIVKLIGVI-------TENP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd05056    81 VWIVMELAPLGELRSYLQVNKYSLDLASLILY-AYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMED 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  181 TVGRRNTFIGTPY-WMAPEVIacdenpdatyDYR-----SDIWSLGI 221
Cdd:cd05056   160 ESYYKASKGKLPIkWMAPESI----------NFRrftsaSDVWMFGV 196
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
25-238 2.61e-15

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 79.33  E-value: 2.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSppgnddq 100
Cdd:cd05627     4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRkadmLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRN------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD- 179
Cdd:cd05627    77 LYLIMEFLPGGDMMTLL--MKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKk 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 --RTVGRRN--------------------------------TFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIE 225
Cdd:cd05627   155 ahRTEFYRNlthnppsdfsfqnmnskrkaetwkknrrqlaySTVGTPDYIAPEVFM-----QTGYNKLCDWWSLGVIMYE 229
                         250
                  ....*....|...
gi 578829925  226 MAEGAPPLCDMHP 238
Cdd:cd05627   230 MLIGYPPFCSETP 242
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
29-226 3.34e-15

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: 77.76  E-value: 3.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKtgQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHrNIATYYGAfiKKSPPGNDDQLWLVMEFC 108
Cdd:cd14140     1 EIKARGRFGCVWKAQLMN--EYVAVKIFPIQDKQSWQSEREIFSTPGMKHE-NLLQFIAA--EKRGSNLEMELWLITAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKntkGNALKEDCIAYICREILRGLAHLH---------AHK--VIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd14140    76 DKGSLTDYLK---GNIVSWNELCHIAETMARGLSYLHedvprckgeGHKpaIAHRDFKSKNVLLKNDLTAVLADFGLAVR 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  178 LD--RTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEM 226
Cdd:cd14140   153 FEpgKPPGDTHGQVGTRRYMAPEVLEGAINFQRDSFLRIDMYAMGLVLWEL 203
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
30-235 3.41e-15

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: 77.64  E-value: 3.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYsHHRNIATYYGAFIKKSppgnddQLWLVM 105
Cdd:cd05607     9 VLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKmallEKEILEKV-NSPFIVSLAYAFETKT------HLCLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD--RTVG 183
Cdd:cd05607    82 SLMNGGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKegKPIT 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  184 RRntfIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd05607   162 QR---AGTNGYMAPEILK-----EESYSYPVDWFAMGCSIYEMVAGRTPFRD 205
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
31-236 3.91e-15

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 77.00  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRH-VKTGQLAAIKVMDVTEDEEEEIKQEInmLKKYS-----HHRNIATYYGafIKKSPPgnddqLWLV 104
Cdd:cd05060     3 LGHGNFGSVRKGVYlMKSGKEVEVAVKTLKQEHEKAGKKEF--LREASvmaqlDHPCIVRLIG--VCKGEP-----LMLV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTD-LVKNTKGNALKedcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaqldRTVG 183
Cdd:cd05060    74 MELAPLGPLLKyLKKRREIPVSD---LKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMS----RALG 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  184 RRNTFigtpY-----------WMAPEVIACdenpdATYDYRSDIWSLGITAIEM-AEGAPPLCDM 236
Cdd:cd05060   147 AGSDY----YrattagrwplkWYAPECINY-----GKFSSKSDVWSYGVTLWEAfSYGAKPYGEM 202
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
31-232 4.46e-15

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: 77.40  E-value: 4.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTG-QLAAIKVMD--VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikKSPPGNDDQLWLVMEF 107
Cdd:cd14030    33 IGRGSFKTVYKGLDTETTvEVAWCELQDrkLSKSERQRFKEEAGMLKGL-QHPNIVRFYDSW--ESTVKGKKCIVLVTEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLT-ENAEVKLVDFGVsAQLDRTVGR 184
Cdd:cd14030   110 MTSGTLKTYLKRFK--VMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGL-ATLKRASFA 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  185 RnTFIGTPYWMAPEVIacdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14030   187 K-SVIGTPEFMAPEMY------EEKYDESVDVYAFGMCMLEMATSEYP 227
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
31-243 4.71e-15

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 77.36  E-value: 4.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHV-----KTGQLA--AIKVM--DVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPpgnddqL 101
Cdd:cd05098    21 LGEGCFGQVVLAEAIgldkdKPNRVTkvAVKMLksDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGP------L 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALK----EDCI-------------AYicrEILRGLAHLHAHKVIHRDIKGQNVLLTEN 164
Cdd:cd05098    95 YVIVEYASKGNLREYLQARRPPGMEycynPSHNpeeqlsskdlvscAY---QVARGMEYLASKKCIHRDLAARNVLVTED 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  165 AEVKLVDFGVSAQLDRTVGRRNTFIGT-PY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEM-AEGAPPLCDMhPMRA 241
Cdd:cd05098   172 NVMKIADFGLARDIHHIDYYKKTTNGRlPVkWMAPEALF-----DRIYTHQSDVWSFGVLLWEIfTLGGSPYPGV-PVEE 245

                  ..
gi 578829925  242 LF 243
Cdd:cd05098   246 LF 247
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
25-238 5.22e-15

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 78.54  E-value: 5.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKQEINMLKKYSHHRNIATYYgAFIKKSppgnddQ 100
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRkadmLEKEQVGHIRAERDILVEADSLWVVKMFY-SFQDKL------N 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD- 179
Cdd:cd05628    76 LYLIMEFLPGGDMMTLL--MKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKk 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 --RTVGRRN---------TF-----------------------IGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIE 225
Cdd:cd05628   154 ahRTEFYRNlnhslpsdfTFqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFM-----QTGYNKLCDWWSLGVIMYE 228
                         250
                  ....*....|...
gi 578829925  226 MAEGAPPLCDMHP 238
Cdd:cd05628   229 MLIGYPPFCSETP 241
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
29-236 5.33e-15

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: 77.35  E-value: 5.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQL--AAIKVMD--VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFikksppGNDDQLWLV 104
Cdd:cd05089     8 DVIGEGNFGQVIKAMIKKDGLKmnAAIKMLKefASENDHRDFAGELEVLCKLGHHPNIINLLGAC------ENRGYLYIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTK--------------GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV 170
Cdd:cd05089    82 IEYAPYGNLLDFLRKSRvletdpafakehgtASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  171 DFGVS----AQLDRTVGRRNTfigtpYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAE-GAPPLCDM 236
Cdd:cd05089   162 DFGLSrgeeVYVKKTMGRLPV-----RWMAIESLNY-----SVYTTKSDVWSFGVLLWEIVSlGGTPYCGM 222
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
27-232 5.58e-15

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 76.33  E-value: 5.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGR---HVKTgqlaAIKVMDVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSPpgnddqLWL 103
Cdd:cd05059     8 FLKELGSGQFGVVHLGKwrgKIDV----AIKMIKEGSMSEDDFIEEAKVMMKLSH-PKLVQLYGVCTKQRP------IFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKGnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaqldRTV- 182
Cdd:cd05059    77 VTEYMANGCLLNYLRERRG-KFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLA----RYVl 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  183 -GRRNTFIGTPY---WMAPEVIAcdenpDATYDYRSDIWSLGITAIEM-AEGAPP 232
Cdd:cd05059   152 dDEYTSSVGTKFpvkWSPPEVFM-----YSKFSSKSDVWSFGVLMWEVfSEGKMP 201
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
18-233 5.59e-15

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 77.60  E-value: 5.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   18 LRDPAgifelvevVGNGTYGQVYKGRHVKTGQLAAIKVmdVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFikksppgn 97
Cdd:cd14180     9 LEEPA--------LGEGSFSVCRKCRHRQSGQEYAVKI--ISRRMEANTQREVAALRLCQSHPNIVALHEVL-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 DDQL--WLVMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL---TENAEVKLVDF 172
Cdd:cd14180    71 HDQYhtYLVMELLRGGELLDRIK--KKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDF 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  173 GVSAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14180   149 GFARLRPQGSRPLQTPCFTLQYAAPELFS-----NQGYDESCDLWSLGVILYTMLSGQVPF 204
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
28-238 7.05e-15

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: 76.53  E-value: 7.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHVKTGQL----AAIKVMDVTEDEEEEIKQEINMLKKYS-HHRNIATYYGAFikkspPGNddQLW 102
Cdd:cd05111    12 LKVLGSGVFGTVHKGIWIPEGDSikipVAIKVIQDRSGRQSFQAVTDHMLAIGSlDHAYIVRLLGIC-----PGA--SLQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVsAQLDRTV 182
Cdd:cd05111    85 LVTQLLPLGSLLDHVRQHRGS-LGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGV-ADLLYPD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTF--IGTPY-WMAPEVIACDEnpdatYDYRSDIWSLGITAIE-MAEGAPPLCDMHP 238
Cdd:cd05111   163 DKKYFYseAKTPIkWMALESIHFGK-----YTHQSDVWSYGVTVWEmMTFGAEPYAGMRL 217
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
26-233 7.38e-15

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 76.55  E-value: 7.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGR-HvktGQLAaIKVMDVTEDEEEEIK---QEInMLKKYSHHRNIATYYGAFIkkSPPgnddQL 101
Cdd:cd14152     3 ELGELIGQGRWGKVHRGRwH---GEVA-IRLLEIDGNNQDHLKlfkKEV-MNYRQTRHENVVLFMGACM--HPP----HL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLtENAEVKLVD---FGVSAQL 178
Cdd:cd14152    72 AIITSFCKGRTLYSFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDfglFGISGVV 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  179 DRtvGRRNTFIGTP----YWMAPEVI-----ACDENpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14152   150 QE--GRRENELKLPhdwlCYLAPEIVremtpGKDED-CLPFSKAADVYAFGTIWYELQARDWPL 210
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
12-234 7.48e-15

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: 76.60  E-value: 7.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   12 DIDLSALRdpagifeLVEVVGNGTYGQVYKGRHVKTG---QLAAIKVMDVTEDEEEEIKQEIN---MLKKYSHHRNIATY 85
Cdd:cd05091     2 EINLSAVR-------FMEELGEDRFGKVYKGHLFGTApgeQTQAVAIKTLKDKAEGPLREEFRheaMLRSRLQHPNIVCL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   86 YGAFIKKSP--------PGNDDQLWLVME--FCGAGSVTDlvKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIK 155
Cdd:cd05091    75 LGVVTKEQPmsmifsycSHGDLHEFLVMRspHSDVGSTDD--DKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  156 GQNVLLTENAEVKLVDFGV-----SAQLDRTVGRRNTFIgtpYWMAPEVIACdenpdATYDYRSDIWSLGITAIEM-AEG 229
Cdd:cd05091   153 TRNVLVFDKLNVKISDLGLfrevyAADYYKLMGNSLLPI---RWMSPEAIMY-----GKFSIDSDIWSYGVVLWEVfSYG 224

                  ....*
gi 578829925  230 APPLC 234
Cdd:cd05091   225 LQPYC 229
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
31-227 9.41e-15

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: 76.26  E-value: 9.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAaIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKSPpgnddqLWLVMEFCGA 110
Cdd:cd05071    17 LGQGCFGEVWMGTWNGTTRVA-IKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLY--AVVSEEP------IYIVTEYMSK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL-DRTVGRRNTFI 189
Cdd:cd05071    88 GSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIeDNEYTARQGAK 167
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 578829925  190 GTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMA 227
Cdd:cd05071   168 FPIKWTAPEAALY-----GRFTIKSDVWSFGILLTELT 200
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
21-226 9.70e-15

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: 75.83  E-value: 9.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGRHVKTGQLAaIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKSPpgnddq 100
Cdd:cd05073     9 PRESLKLEKKLGAGQFGEVWMATYNKHTKVA-VKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLH--AVVTKEP------ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL-D 179
Cdd:cd05073    80 IYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIeD 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  180 RTVGRRNTFIGTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEM 226
Cdd:cd05073   160 NEYTAREGAKFPIKWTAPEAINF-----GSFTIKSDVWSFGILLMEI 201
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
29-233 9.83e-15

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: 76.91  E-value: 9.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEikqEINMLKKY-----SHHRNIATYYGAFIKKsppgndDQL 101
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALkkDVVLIDDDV---ECTMVEKRvlalaWENPFLTHLYCTFQTK------EHL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALKEdcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 181
Cdd:cd05620    72 FFVMEFLNGGDLMFHIQDKGRFDLYR--ATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  182 VGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05620   150 DNRASTFCGTPDYIAPEILQ-----GLKYTFSVDWWSFGVLLYEMLIGQSPF 196
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
24-289 9.86e-15

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 75.78  E-value: 9.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE-------EEIKQEINMLKKyshhrnIATYYGAFIK----- 91
Cdd:cd14100     1 QYQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEwgelpngTRVPMEIVLLKK------VGSGFRGVIRlldwf 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   92 KSPpgndDQLWLVMEfcGAGSVTDLVKN-TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN-AEVKL 169
Cdd:cd14100    75 ERP----DSFVLVLE--RPEPVQDLFDFiTERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNtGELKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  170 VDFGVSAQLDRTVgrRNTFIGTPYWMAPEVIACDEnpdatYDYRS-DIWSLGITAIEMAEGAPPL-CDMHPMRALFLIPR 247
Cdd:cd14100   149 IDFGSGALLKDTV--YTDFDGTRVYSPPEWIRFHR-----YHGRSaAVWSLGILLYDMVCGDIPFeHDEEIIRGQVFFRQ 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578829925  248 NPPPRLKSkkwskkfidFIDTCLIKTYLSRPPTEQLLKFPFI 289
Cdd:cd14100   222 RVSSECQH---------LIKWCLALRPSDRPSFEDIQNHPWM 254
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
29-236 1.02e-14

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: 76.57  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTG--QLAAIKVMD--VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSppgnddQLWLV 104
Cdd:cd05088    13 DVIGEGNFGQVLKARIKKDGlrMDAAIKRMKeyASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRG------YLYLA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVK--------------NTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLV 170
Cdd:cd05088    87 IEYAPHGNLLDFLRksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  171 DFGVS----AQLDRTVGRRNTfigtpYWMAPEVIACdenpdATYDYRSDIWSLGITAIEMAE-GAPPLCDM 236
Cdd:cd05088   167 DFGLSrgqeVYVKKTMGRLPV-----RWMAIESLNY-----SVYTTNSDVWSYGVLLWEIVSlGGTPYCGM 227
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
21-233 1.11e-14

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 75.80  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEV---VGNGTYGQVYKGRHVKTGQLAAIKVMDVTE--DEEEEIKQEINMLKKYSHhRNIATyygaFIKKSPP 95
Cdd:cd14183     1 PASISERYKVgrtIGDGNFAVVKECVERSTGREYALKIINKSKcrGKEHMIQNEVSILRRVKH-PNIVL----LIEEMDM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 GNddQLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE----VKLVD 171
Cdd:cd14183    76 PT--ELYLVMELVKGGDLFDAI--TSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDgsksLKLGD 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  172 FGVSAQLDrtvGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14183   152 FGLATVVD---GPLYTVCGTPTYVAPEIIA-----ETGYGLKVDIWAAGVITYILLCGFPPF 205
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
25-233 1.71e-14

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: 76.16  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeEEEIKQ---------EINMLKKYSHHRNIATYYGAFIKkspp 95
Cdd:cd05632     4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLE-----KKRIKKrkgesmalnEKQILEKVNSQFVVNLAYAYETK---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 gndDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd05632    75 ---DALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  176 AQL---DRTVGRrntfIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05632   152 VKIpegESIRGR----VGTVGYMAPEVLN-----NQRYTLSPDYWGLGCLIYEMIEGQSPF 203
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
27-245 1.72e-14

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 75.77  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV-------TEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSPPgndd 99
Cdd:cd05045     4 LGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVkmlkenaSSSELRDLLSEFNLLKQVNH-PHVIKLYGACSQDGPL---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 qlWLVMEFCGAGSVTDLVKNTK----------GN------------ALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQ 157
Cdd:cd05045    79 --LLIVEYAKYGSLRSFLRESRkvgpsylgsdGNrnssyldnpderALTMGDLISFAWQISRGMQYLAEMKLVHRDLAAR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  158 NVLLTENAEVKLVDFGVS-------AQLDRTVGRrntfigTPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAE- 228
Cdd:cd05045   157 NVLVAEGRKMKISDFGLSrdvyeedSYVKRSKGR------IPVkWMAIESLF-----DHIYTTQSDVWSFGVLLWEIVTl 225
                         250
                  ....*....|....*..
gi 578829925  229 GAPPLCDMHPMRALFLI 245
Cdd:cd05045   226 GGNPYPGIAPERLFNLL 242
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
31-227 1.77e-14

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: 75.46  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEEEIKQEI--NMLKKyshHRNIATYYGAFIKKSppGNDDQLWLVMEFC 108
Cdd:cd14220     3 IGKGRYGEVWMGKW--RGEKVAVKVFFTTEEASWFRETEIyqTVLMR---HENILGFIAADIKGT--GSWTQLYLITDYH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKntkgnalkedCIAYICREILR-------GLAHLHAH--------KVIHRDIKGQNVLLTENAEVKLVDFG 173
Cdd:cd14220    76 ENGSLYDFLK----------CTTLDTRALLKlaysaacGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLG 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  174 VSAQLDRTVGR----RNTFIGTPYWMAPEVIACDENPDATYDY-RSDIWSLGITAIEMA 227
Cdd:cd14220   146 LAVKFNSDTNEvdvpLNTRVGTKRYMAPEVLDESLNKNHFQAYiMADIYSFGLIIWEMA 204
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
31-244 1.85e-14

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 75.35  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQV----YKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAfikkSPPGNDDQLWLV 104
Cdd:cd05079    12 LGEGHFGKVelcrYDPEGDNTGEQVAVKSLkpESGGNHIADLKKEIEILRNL-YHENIVKYKGI----CTEDGGNGIKLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTKGNALKEDCIAYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV--SAQLDRTV 182
Cdd:cd05079    87 MEFLPSGSLKEYLPRNKNKINLKQQLKYAV-QICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLtkAIETDKEY 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  183 GRRNTFIGTP-YWMAPE-VIACdenpdaTYDYRSDIWSLGITAIEMAEgappLCDMH--PMrALFL 244
Cdd:cd05079   166 YTVKDDLDSPvFWYAPEcLIQS------KFYIASDVWSFGVTLYELLT----YCDSEssPM-TLFL 220
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
25-289 2.11e-14

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 76.28  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVmdvtedeeeeIKQeinmlKKYSHHRNIA--TYYGAFIKKSPPGNDD--- 99
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKI----------IRN-----KKRFHHQALVevKILDALRRKDRDNSHNvih 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 ---------QLWLVMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE--NAEVK 168
Cdd:cd14225   110 mkeyfyfrnHLCITFELLGM-NLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQrgQSSIK 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  169 LVDFGVSAQLDRTVgrrNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL----------CDMHP 238
Cdd:cd14225   189 VIDFGSSCYEHQRV---YTYIQSRFYRSPEVIL-----GLPYSMAIDMWSLGCILAELYTGYPLFpgeneveqlaCIMEV 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  239 M-------------RALFLIPRNPPPRLKSKKWSKK-----------------FIDFIDTCLIKTYLSRPPTEQLLKFPF 288
Cdd:cd14225   261 LglpppelienaqrRRLFFDSKGNPRCITNSKGKKRrpnskdlasalktsdplFLDFIRRCLEWDPSKRMTPDEALQHEW 340

                  .
gi 578829925  289 I 289
Cdd:cd14225   341 I 341
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
29-227 2.48e-14

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: 75.17  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHvkTGQLAAIKVM----DVTEDEEEEIKQEInMLKkyshHRNIATYYGAFIKKSppGNDDQLWLV 104
Cdd:cd14143     1 ESIGKGRFGEVWRGRW--RGEDVAVKIFssreERSWFREAEIYQTV-MLR----HENILGFIAADNKDN--GTWTQLWLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTkgnALKEDCIAYICREILRGLAHLHAHKV--------IHRDIKGQNVLLTENAEVKLVDFGVSA 176
Cdd:cd14143    72 SDYHEHGSLFDYLNRY---TVTVEGMIKLALSIASGLAHLHMEIVgtqgkpaiAHRDLKSKNILVKKNGTCCIADLGLAV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  177 QLDRTVGR----RNTFIGTPYWMAPEVIAcDENPDATYDY--RSDIWSLGITAIEMA 227
Cdd:cd14143   149 RHDSATDTidiaPNHRVGTKRYMAPEVLD-DTINMKHFESfkRADIYALGLVFWEIA 204
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
24-173 2.67e-14

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 75.40  E-value: 2.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGR--HVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYsHHRNIATYYGAFIKKsppgN 97
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKrkNGKDGKEYAIKKFKGDKEQYTGISQsacrEIALLREL-KHENVVSLVEVFLEH----A 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 DDQLWLVMEFCGAgsvtDLV------KNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT----ENAEV 167
Cdd:cd07842    76 DKSVYLLFDYAEH----DLWqiikfhRQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMgegpERGVV 151

                  ....*.
gi 578829925  168 KLVDFG 173
Cdd:cd07842   152 KIGDLG 157
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
69-264 2.93e-14

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 75.31  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   69 EINMLKKYSHH-------RNIATYYGAFIKKSPPGNddQLWLVMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGL 141
Cdd:cd14136    56 EIKLLKCVREAdpkdpgrEHVVQLLDDFKHTGPNGT--HVCMVFEVLGP-NLLKLIKRYNYRGIPLPLVKKIARQVLQGL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  142 AHLHAH-KVIHRDIKGQNVLLTE-NAEVKLVDFGVSAQLDRtvgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSL 219
Cdd:cd14136   133 DYLHTKcGIIHTDIKPENVLLCIsKIEVKIADLGNACWTDK---HFTEDIQTRQYRSPEVIL-----GAGYGTPADIWST 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  220 GITAIEMAEGApPLCDMHPMR---------ALF--LIPRNPPPRLKSKKWSKKFID 264
Cdd:cd14136   205 ACMAFELATGD-YLFDPHSGEdysrdedhlALIieLLGRIPRSIILSGKYSREFFN 259
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
27-226 3.22e-14

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: 74.67  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGRHV----KTGQLAAIKVMD-VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKksppGNDDQL 101
Cdd:cd14205     8 FLQQLGKGNFGSVEMCRYDplqdNTGEVVAVKKLQhSTEEHLRDFEREIEILKSL-QHDNIVKYKGVCYS----AGRRNL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALKEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--D 179
Cdd:cd14205    83 RLIMEYLPYGSLRDYLQKHKERIDHIKLLQY-TSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLpqD 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578829925  180 RTVGRRNTFIGTP-YWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd14205   162 KEYYKVKEPGESPiFWYAPESLT-----ESKFSVASDVWSFGVVLYEL 204
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
28-226 3.33e-14

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 74.54  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHV----KTGQLAAIK-VMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSPPGnddqLW 102
Cdd:cd05081     9 ISQLGKGNFGSVELCRYDplgdNTGALVAVKqLQHSGPDQQRDFQREIQILKAL-HSDFIVKYRGVSYGPGRRS----LR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKgNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL---- 178
Cdd:cd05081    84 LVMEYLPSGCLRDFLQRHR-ARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLpldk 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578829925  179 DRTVGRRNTfiGTP-YWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd05081   163 DYYVVREPG--QSPiFWYAPESLS-----DNIFSRQSDVWSFGVVLYEL 204
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
25-247 3.38e-14

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: 74.33  E-value: 3.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAaIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKSPpgnddqLWLV 104
Cdd:cd05070    11 LQLIKRLGNGQFGEVWMGTWNGNTKVA-IKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLY--AVVSEEP------IYIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL-DRTVG 183
Cdd:cd05070    82 TEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIeDNEYT 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  184 RRNTFIGTPYWMAPEVIACdenpdATYDYRSDIWSLGITAIEM-AEGAPPLCDMHPMRALFLIPR 247
Cdd:cd05070   162 ARQGAKFPIKWTAPEAALY-----GRFTIKSDVWSFGILLTELvTKGRVPYPGMNNREVLEQVER 221
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
25-232 3.46e-14

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 75.42  E-value: 3.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKG-----RHVKTGQLAAIKVMD--VTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPPgn 97
Cdd:cd14207     9 LKLGKSLGRGAFGKVVQAsafgiKKSPTCRVVAVKMLKegATASEYKALMTELKILIHIGHHLNVVNLLGACTKSGGP-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 ddqLWLVMEFCGAGSVTDLVKN-------TKGNALK-------------------------------------------- 126
Cdd:cd14207    87 ---LMVIVEYCKYGNLSNYLKSkrdffvtNKDTSLQeelikekkeaeptggkkkrlesvtssesfassgfqedkslsdve 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  127 ----------------EDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT---VGRRNT 187
Cdd:cd14207   164 eeeedsgdfykrpltmEDLISY-SFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNpdyVRKGDA 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578829925  188 FIGTPyWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM-AEGAPP 232
Cdd:cd14207   243 RLPLK-WMAPESIF-----DKIYSTKSDVWSYGVLLWEIfSLGASP 282
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
31-231 3.57e-14

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 75.57  E-value: 3.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVT--EDEEEEIKQEINM----------LK--KYSHHRNIATYYGAFIKKsppg 96
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIeiSNDVTKDRQLVGMcgihfttlreLKimNEIKHENIMGLVDVYVEG---- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 ndDQLWLVMEFCGAgsvtDLVKNTKGNA-LKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:PTZ00024   93 --DFINLVMDIMAS----DLKKVVDRKIrLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLA 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQL-----------DRTVGRRNTF---IGTPYWMAPEVIACDEnpdaTYDYRSDIWSLGITAIEMAEGAP 231
Cdd:PTZ00024  167 RRYgyppysdtlskDETMQRREEMtskVVTLWYRAPELLMGAE----KYHFAVDMWSVGCIFAELLTGKP 232
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
31-226 4.00e-14

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 75.00  E-value: 4.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGR----------HVKTgqlAAIKVM--DVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPpgnd 98
Cdd:cd05099    20 LGEGCFGQVVRAEaygidksrpdQTVT---VAVKMLkdNATDKDLADLISEMELMKLIGKHKNIINLLGVCTQEGP---- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dqLWLVMEFCGAGSVTDLVKNTK---------GNALKEDCIAY-----ICREILRGLAHLHAHKVIHRDIKGQNVLLTEN 164
Cdd:cd05099    93 --LYVIVEYAAKGNLREFLRARRppgpdytfdITKVPEEQLSFkdlvsCAYQVARGMEYLESRRCIHRDLAARNVLVTED 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  165 AEVKLVDFGVSAQLDRTVGRRNTFIG-TPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd05099   171 NVMKIADFGLARGVHDIDYYKKTSNGrLPVkWMAPEALF-----DRVYTHQSDVWSFGILMWEI 229
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
25-291 4.20e-14

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: 75.30  E-value: 4.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdvtedeeeeikQEINMLKKYSHHRNIATYYGAFIKKSP--------PG 96
Cdd:cd05610     6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVV-----------KKADMINKNMVHQVQAERDALALSKSPfivhlyysLQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 NDDQLWLVMEFCGAGSVTDLVkNTKGNALKEDCIAYICrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS- 175
Cdd:cd05610    75 SANNVYLVMEYLIGGDVKSLL-HIYGYFDEEMAVKYIS-EVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSk 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQLDRTVG---------------------------------------------RRNT-------FIGTPYWMAPEVIAcd 203
Cdd:cd05610   153 VTLNRELNmmdilttpsmakpkndysrtpgqvlslisslgfntptpyrtpksvRRGAarvegerILGTPDYLAPELLL-- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  204 enpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRAL-FLIPRNPPPRLKSKKWSKKFIDFIDTCLIKTYLSRPPTEQ 282
Cdd:cd05610   231 ---GKPHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFqNILNRDIPWPEGEEELSVNAQNAIEILLTMDPTKRAGLKE 307

                  ....*....
gi 578829925  283 LLKFPFIRD 291
Cdd:cd05610   308 LKQHPLFHG 316
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
103-235 4.60e-14

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 73.86  E-value: 4.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE---VKLVDFGVSAQLD 179
Cdd:cd14113    80 LVLEMADQGRLLDYV--VRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLN 157
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  180 RTVgRRNTFIGTPYWMAPEVIAcdENPdatYDYRSDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd14113   158 TTY-YIHQLLGSPEFAAPEIIL--GNP---VSLTSDLWSIGVLTYVLLSGVSPFLD 207
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
25-233 5.38e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 74.26  E-value: 5.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeEEEIKQ---------EINMLKKYSHHRNIATYYGAFIKkspp 95
Cdd:cd05631     2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLE-----KKRIKKrkgeamalnEKRILEKVNSRFVVSLAYAYETK---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 gndDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd05631    73 ---DALCLVLTIMNGGDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  176 AQL---DRTVGRrntfIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd05631   150 VQIpegETVRGR----VGTVGYMAPEVIN-----NEKYTFSPDWWGLGCLIYEMIQGQSPF 201
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
29-251 6.16e-14

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


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 73.47  E-value: 6.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQ---LAAIKVMDV--TEDEEEEIKQEINMLKKYSHHrNIATYYGAFIKKSPpgnddqLWL 103
Cdd:cd05063    11 KVIGAGEFGEVFRGILKMPGRkevAVAIKTLKPgyTEKQRQDFLSEASIMGQFSHH-NIIRLEGVVTKFKP------AMI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKGNALKEDCIAYIcREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL-DRTV 182
Cdd:cd05063    84 ITEYMENGALDKYLRDHDGEFSSYQLVGML-RGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLeDDPE 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  183 GRRNTFIGT-PY-WMAPEVIACDENPDAtydyrSDIWSLGITAIE-MAEGAPPLCDM---HPMRALFLIPRNPPP 251
Cdd:cd05063   163 GTYTTSGGKiPIrWTAPEAIAYRKFTSA-----SDVWSFGIVMWEvMSFGERPYWDMsnhEVMKAINDGFRLPAP 232
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
27-281 6.94e-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: 6.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEEEIKQEINMLKkySHHRNIATYYGAFIKKSppgnddqLWLVME 106
Cdd:cd05083    10 LGEIIGEGEFGAVLQGEY--MGQKVAVKNIKCDVTAQAFLEETAVMTK--LQHKNLVRLLGVILHNG-------LYIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKnTKGNALKEDC-IAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRR 185
Cdd:cd05083    79 LMSKGNLVNFLR-SRGRALVPVIqLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMGVDNS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  186 NTFIGtpyWMAPEVIAcdenpDATYDYRSDIWSLGITAIEmaegapplcdmhpmraLFLIPRNPPPRLKSKKwskkfidf 265
Cdd:cd05083   158 RLPVK---WTAPEALK-----NKKFSSKSDVWSYGVLLWE----------------VFSYGRAPYPKMSVKE-------- 205
                         250
                  ....*....|....*.
gi 578829925  266 IDTCLIKTYLSRPPTE 281
Cdd:cd05083   206 VKEAVEKGYRMEPPEG 221
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
25-232 7.62e-14

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: 74.28  E-value: 7.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM---DVTEDEEEE-IKQEINMLKKYSHHRNIATYYgAFikksppGNDDQ 100
Cdd:cd05598     3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLrkkDVLKRNQVAhVKAERDILAEADNEWVVKLYY-SF------QDKEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 180
Cdd:cd05598    76 LYFVMDYIPGGDLMSLL--IKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRW 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  181 TVGRR----NTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05598   154 THDSKyylaHSLVGTPNYIAPEVLL-----RTGYTQLCDWWSVGVILYEMLVGQPP 204
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
30-235 8.59e-14

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: 73.76  E-value: 8.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMdvtedEEEEIKQEINMLKKYSHHRNIATYYGAFIK------KSPpgndDQLWL 103
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRIYALKTI-----RKAHIVSRSEVTHTLAERTVLAQVDCPFIVplkfsfQSP----EKLYL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKntKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVG 183
Cdd:cd05585    72 VLAFINGGELFHHLQ--REGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDD 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  184 RRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd05585   150 KTNTFCGTPEYLAPELLL-----GHGYTKAVDWWTLGVLLYEMLTGLPPFYD 196
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
21-255 8.97e-14

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: 73.18  E-value: 8.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGRHVKTG-----QLAAIKVM--DVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKS 93
Cdd:cd05048     3 PLSAVRFLEELGEGAFGKVYKGELLGPSseesaISVAIKTLkeNASPKTQQDFRREAELMSDL-QHPNIVCLLGVCTKEQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   94 P--------PGNDDQLWLVME--FCGAGSVTDLvkNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE 163
Cdd:cd05048    82 PqcmlfeymAHGDLHEFLVRHspHSDVGVSSDD--DGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  164 NAEVKLVDFGV-----SAQLDRTVGRRNTFIgtpYWMAPEVIACdenpdATYDYRSDIWSLGITAIEM-AEGAPPLC--- 234
Cdd:cd05048   160 GLTVKISDFGLsrdiySSDYYRVQSKSLLPV---RWMPPEAILY-----GKFTTESDVWSFGVVLWEIfSYGLQPYYgys 231
                         250       260
                  ....*....|....*....|....*.
gi 578829925  235 -----DMHPMRALFLIPRNPPPRLKS 255
Cdd:cd05048   232 nqeviEMIRSRQLLPCPEDCPARVYS 257
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
25-288 1.06e-13

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 72.63  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRnIATYYGAFIKKSppgnddQLWLV 104
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHKS-IVRFHDAFEKRR------VVIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKNTkgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE--VKLVDFGVSAQLDRTV 182
Cdd:cd14108    77 TELCHEELLERITKRP---TVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQELTPNE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFiGTPYWMAPEVIacDENPDATYdyrSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIpRNPPPRLKS---KKWS 259
Cdd:cd14108   154 PQYCKY-GTPEFVAPEIV--NQSPVSKV---TDIWPVGVIAYLCLTGISPFVGENDRTTLMNI-RNYNVAFEEsmfKDLC 226
                         250       260
                  ....*....|....*....|....*....
gi 578829925  260 KKFIDFIDTCLIKTYLsRPPTEQLLKFPF 288
Cdd:cd14108   227 REAKGFIIKVLVSDRL-RPDAEETLEHPW 254
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
12-255 1.10e-13

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 73.12  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   12 DIDLSALRdpagifeLVEVVGNGTYGQVYKGRHVKTG----QLAAIKVM-DVTEDEE-EEIKQEINMLKKYsHHRNIATY 85
Cdd:cd05090     1 ELPLSAVR-------FMEELGECAFGKIYKGHLYLPGmdhaQLVAIKTLkDYNNPQQwNEFQQEASLMTEL-HHPNIVCL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   86 YGAFIKKSP--------PGNDDQLWLVMEF----CGAGSVTDlvkNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRD 153
Cdd:cd05090    73 LGVVTQEQPvcmlfefmNQGDLHEFLIMRSphsdVGCSSDED---GTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  154 IKGQNVLLTENAEVKLVDFGVSAQL---DRTVGRRNTFIGTpYWMAPEVIACdenpdATYDYRSDIWSLGITAIEM-AEG 229
Cdd:cd05090   150 LAARNILVGEQLHVKISDLGLSREIyssDYYRVQNKSLLPI-RWMPPEAIMY-----GKFSSDSDIWSFGVVLWEIfSFG 223
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  230 APP--------LCDMHPMRALFLIPRNPPPRLKS 255
Cdd:cd05090   224 LQPyygfsnqeVIEMVRKRQLLPCSEDCPPRMYS 257
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
99-232 1.10e-13

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: 73.16  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd05605    73 DALCLVLTIMNGGDLKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEI 152
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  179 ---DRTVGRrntfIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05605   153 pegETIRGR----VGTVGYMAPEVVK-----NERYTFSPDWWGLGCLIYEMIEGQAP 200
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
31-243 1.15e-13

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 73.90  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQ-------LAAIKVM--DVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPpgnddqL 101
Cdd:cd05100    20 LGEGCFGQVVMAEAIGIDKdkpnkpvTVAVKMLkdDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGP------L 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTDLVKNTKGNALK---EDC-----------IAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 167
Cdd:cd05100    94 YVLVEYASKGNLREYLRARRPPGMDysfDTCklpeeqltfkdLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVM 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  168 KLVDFGVSAQLDRTVGRRNTFIGT-PY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALF 243
Cdd:cd05100   174 KIADFGLARDVHNIDYYKKTTNGRlPVkWMAPEALF-----DRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 246
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
25-239 1.20e-13

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 73.86  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHvKTGQLAAIKVMDVTEDEEEEIKQEINMLKK-----YSHHRNIATYYGAFikksppGNDD 99
Cdd:PTZ00426   32 FNFIRTLGTGSFGRVILATY-KNEDFPPVAIKRFEKSKIIKQKQVDHVFSErkilnYINHPFCVNLYGSF------KDES 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:PTZ00426  105 YLYLVLEFVIGGEFFTFLRRNK--RFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RtvgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPM 239
Cdd:PTZ00426  183 T---RTYTLCGTPEYIAPEILL-----NVGHGKAADWWTLGIFIYEILVGCPPFYANEPL 234
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
30-229 1.57e-13

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 73.60  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLK--KYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEF 107
Cdd:cd07850     7 PIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVlmKLVNHKNIIGLLNVFTPQKSLEEFQDVYLVMEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  108 CGAgSVTDLVKNTkgnaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvsaqLDRTVGrrNT 187
Cdd:cd07850    87 MDA-NLCQVIQMD----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFG----LARTAG--TS 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  188 FIGTP-----YWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEG 229
Cdd:cd07850   156 FMMTPyvvtrYYRAPEVIL-----GMGYKENVDIWSVGCIMGEMIRG 197
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
25-231 1.91e-13

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 73.14  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHR----NIATYYGAFIKKSppgnddQ 100
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENadefNFVRAYECFQHRN------H 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCgAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA----EVKLVDFGVSA 176
Cdd:cd14229    76 TCLVFEML-EQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFGSAS 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  177 QLDRTVGrrNTFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAP 231
Cdd:cd14229   155 HVSKTVC--STYLQSRYYRAPEIILGLPFCEAI-----DMWSLGCVIAELFLGWP 202
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
133-226 2.60e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 72.99  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  133 ICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvSAQLDRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDY 212
Cdd:PHA03209  162 IEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLG-AAQFPVVAPAFLGLAGTVETNAPEVLARDK-----YNS 235
                          90
                  ....*....|....
gi 578829925  213 RSDIWSLGITAIEM 226
Cdd:PHA03209  236 KADIWSAGIVLFEM 249
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
19-227 2.73e-13

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: 72.39  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   19 RDPAGIFELVEVVGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEEEIKQEINMlKKYSHHRNIATYYGAFIKKSppGND 98
Cdd:cd14219     1 RTIAKQIQMVKQIGKGRYGEVWMGKW--RGEKVAVKVFFTTEEASWFRETEIYQ-TVLMRHENILGFIAADIKGT--GSW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYicrEILRGLAHLHAH--------KVIHRDIKGQNVLLTENAEVKLV 170
Cdd:cd14219    76 TQLYLITDYHENGSLYDYLKSTTLDTKAMLKLAY---SSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNGTCCIA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578829925  171 DFGVSAQLDRTVGR----RNTFIGTPYWMAPEVIACDENPDATYDY-RSDIWSLGITAIEMA 227
Cdd:cd14219   153 DLGLAVKFISDTNEvdipPNTRVGTKRYMPPEVLDESLNRNHFQSYiMADMYSFGLILWEVA 214
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
25-232 3.23e-13

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: 71.04  E-value: 3.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ----EINMLKKYSHHRNIATYygAFIKKSppgnDDQ 100
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKflprELSILRRVNHPNIVQMF--ECIEVA----NGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEfcgaGSVTDLVKNTKGNALKEDCIAY-ICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE-VKLVDFGVSAQL 178
Cdd:cd14164    76 LYIVME----AAATDLLQKIQEVHHIPKDLARdMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRkIKIADFGFARFV 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  179 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRS-DIWSLGITAIEMAEGAPP 232
Cdd:cd14164   152 EDYPELSTTFCGSRAYTPPEVIL-----GTPYDPKKyDVWSLGVVLYVMVTGTMP 201
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
31-227 3.33e-13

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: 71.30  E-value: 3.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSPpgnddqLWLVMEFCGA 110
Cdd:cd05052    14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEI-KHPNLVQLLGVCTREPP------FYIITEFMPY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLdrtvgRRNTFI- 189
Cdd:cd05052    87 GNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLM-----TGDTYTa 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578829925  190 --GTPY---WMAPEVIACDenpdaTYDYRSDIWSLGITAIEMA 227
Cdd:cd05052   162 haGAKFpikWTAPESLAYN-----KFSIKSDVWAFGVLLWEIA 199
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
32-254 3.78e-13

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: 71.49  E-value: 3.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRHvkTGQLAAIKVMDV----------------------TEDEEEEIKQEINMLKKYsHHRNIATYYGAF 89
Cdd:cd14000     3 GDGGFGSVYRASY--KGEPVAVKIFNKhtssnfanvpadtmlrhlratdAMKNFRLLRQELTVLSHL-HHPSIVYLLGIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   90 IKKsppgnddqLWLVMEFCGAGSVTDLVKNTK--GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL-----T 162
Cdd:cd14000    80 IHP--------LMLVLELAPLGSLDHLLQQDSrsFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  163 ENAEVKLVDFGVSAQLDRTVGRrnTFIGTPYWMAPEVIACDEnpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRAL 242
Cdd:cd14000   152 SAIIIKIADYGISRQCCRMGAK--GSEGTPGFRAPEIARGNV----IYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNE 225
                         250
                  ....*....|..
gi 578829925  243 FLIPRNPPPRLK 254
Cdd:cd14000   226 FDIHGGLRPPLK 237
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
29-237 4.41e-13

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 71.60  E-value: 4.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMdvteDEEEEIKQEINMLKKYSHHRNIATYYGAFikKSPPGNDDQLWLVMEFC 108
Cdd:cd14170     8 QVLGLGINGKVLQIFNKRTQEKFALKML----QDCPKARREVELHWRASQCPHIVRIVDVY--ENLYAGRKCLLIVMECL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  109 GAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE---NAEVKLVDFGVsAQLDRTVGRR 185
Cdd:cd14170    82 DGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGF-AKETTSHNSL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  186 NTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAPPLCDMH 237
Cdd:cd14170   161 TTPCYTPYYVAPEVLGPEK-----YDKSCDMWSLGVIMYILLCGYPPFYSNH 207
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
26-226 5.38e-13

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: 70.90  E-value: 5.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQVYKGRHVKTGQlAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYygAFIKKSPPgnddqLWLVM 105
Cdd:cd05068    11 KLLRKLGSGQFGEVWEGLWNNTTP-VAVKTLKPGTMDPEDFLREAQIMKKLRHPKLIQLY--AVCTLEEP-----IYIIT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNtKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvsaqLDRTVGRR 185
Cdd:cd05068    83 ELMKHGSLLEYLQG-KGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFG----LARVIKVE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  186 NTF---IGTPY---WMAPEVIACDEnpdatYDYRSDIWSLGITAIEM 226
Cdd:cd05068   158 DEYearEGAKFpikWTAPEAANYNR-----FSIKSDVWSFGILLTEI 199
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
21-232 5.56e-13

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 71.94  E-value: 5.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGR-----HVKTGQLAAIKVMDV--TEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKS 93
Cdd:cd05103     5 PRDRLKLGKPLGRGAFGQVIEADafgidKTATCRTVAVKMLKEgaTHSEHRALMSELKILIHIGHHLNVVNLLGACTKPG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   94 PPgnddqLWLVMEFCGAGSVTDLVKNTKG--------------------------------------------------- 122
Cdd:cd05103    85 GP-----LMVIVEFCKFGNLSAYLRSKRSefvpyktkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveeksls 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  123 -----NALKED-CIAYICREIL--------RGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--DRTVGRRN 186
Cdd:cd05103   160 dveeeEAGQEDlYKDFLTLEDLicysfqvaKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIykDPDYVRKG 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  187 TFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM-AEGAPP 232
Cdd:cd05103   240 DARLPLKWMAPETIF-----DRVYTIQSDVWSFGVLLWEIfSLGASP 281
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
21-232 5.63e-13

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: 70.64  E-value: 5.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKG--RHVKTGQLAAIKVMDVTEDEEEEIKqEINMLKKySHHRNIATYYGAFiKKSPpgnd 98
Cdd:cd14112     1 PTGRFSFGSEIFRGRFSVIVKAvdSTTETDAHCAVKIFEVSDEASEAVR-EFESLRT-LQHENVQRLIAAF-KPSN---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dQLWLVMEFCGAGSVTDLVKNTKGNalkEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSA 176
Cdd:cd14112    74 -FAYLVMEKLQEDVFTRFSSNDYYS---EEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQ 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  177 QLDRTVGRRNTfiGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd14112   150 KVSKLGKVPVD--GDTDWASPEFH----NPETPITVQSDIWGLGVLTFCLLSGFHP 199
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
27-255 6.37e-13

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: 70.77  E-value: 6.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKG--RHVKTGQL---AAIKVMDVTEDEEEEIK--QEINMLKKYSHHrNIATYYGAFIKKSPPgndd 99
Cdd:cd05061    10 LLRELGQGSFGMVYEGnaRDIIKGEAetrVAVKTVNESASLRERIEflNEASVMKGFTCH-HVVRLLGVVSKGQPT---- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 qlWLVMEFCGAGSVTDLVKNTKGNA----------LKEdcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 169
Cdd:cd05061    85 --LVVMELMAHGDLKSYLRSLRPEAennpgrppptLQE--MIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  170 VDFGVSAQLDRTVGRRNTFIG-TPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAP-PLCDMHPMRALFLI- 245
Cdd:cd05061   161 GDFGMTRDIYETDYYRKGGKGlLPVrWMAPESLK-----DGVFTTSSDMWSFGVVLWEITSLAEqPYQGLSNEQVLKFVm 235
                         250
                  ....*....|....*..
gi 578829925  246 -------PRNPPPRLKS 255
Cdd:cd05061   236 dggyldqPDNCPERVTD 252
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
30-232 6.42e-13

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: 70.54  E-value: 6.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMDvteDEEEEIKQ-------EINMLKKYSHHRN---IATYYGAFikKSPpgndD 99
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGKMYAMKCLD---KKRIKMKQgetlalnERIMLSLVSTGGDcpfIVCMTYAF--QTP----D 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGsvtDLVKN-TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd05606    72 KLCFILDLMNGG---DLHYHlSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDF 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  179 DRTvgRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd05606   149 SKK--KPHASVGTHGYMAPEVLQ----KGVAYDSSADWFSLGCMLYKLLKGHSP 196
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
31-258 8.08e-13

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 70.40  E-value: 8.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRhVKTGqLAAIKVMDVTEDEEEEIKQEINMLKKYS-----HHRNIATYYGAFIKKSPpgnddqLWLVM 105
Cdd:cd05087     5 IGHGWFGKVFLGE-VNSG-LSSTQVVVKELKASASVQDQMQFLEEAQpyralQHTNLLQCLAQCAEVTP------YLLVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKG-NALKED--CIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA---QLD 179
Cdd:cd05087    77 EFCPLGDLKGYLRSCRAaESMAPDplTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHckyKED 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  180 RTVGRRNTFIgtPY-WMAPEVIacDEN------PDATydYRSDIWSLGITAIEMAE-GAPPLCDMHPMRALFLIPRN--- 248
Cdd:cd05087   157 YFVTADQLWV--PLrWIAPELV--DEVhgnllvVDQT--KQSNVWSLGVTIWELFElGNQPYRHYSDRQVLTYTVREqql 230
                         250
                  ....*....|....*
gi 578829925  249 --PPPRLK---SKKW 258
Cdd:cd05087   231 klPKPQLKlslAERW 245
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
25-227 8.79e-13

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 72.52  E-value: 8.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKtgqlaaikvmdvtedeEEEIKQEINMLKKYSHH----------------RNIATYYGA 88
Cdd:PLN03225  134 FVLGKKLGEGAFGVVYKASLVN----------------KQSKKEGKYVLKKATEYgaveiwmnervrracpNSCADFVYG 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   89 FIKKSPPGNDDQLWLVMEFCGAGSVTDLVKNT------------------KGNALKEDCIAYICREILRGLAHLHAHKVI 150
Cdd:PLN03225  198 FLEPVSSKKEDEYWLVWRYEGESTLADLMQSKefpynvepyllgkvqdlpKGLERENKIIQTIMRQILFALDGLHSTGIV 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  151 HRDIKGQNVLLTENA-EVKLVDFGVSAQLdrTVG---RRNTFIGTPYWMAPE-VIACDENPDA----------------T 209
Cdd:PLN03225  278 HRDVKPQNIIFSEGSgSFKIIDLGAAADL--RVGinyIPKEFLLDPRYAAPEqYIMSTQTPSApsapvatalspvlwqlN 355
                         250
                  ....*....|....*...
gi 578829925  210 YDYRSDIWSLGITAIEMA 227
Cdd:PLN03225  356 LPDRFDIYSAGLIFLQMA 373
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
31-269 9.24e-13

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: 69.87  E-value: 9.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHvkTGQLAAIKVMDVTEDEEeeiKQEINML-KKYS-----HHRNIATYYGAFIkksppgnDD--QLW 102
Cdd:cd14064     1 IGSGSFGKVYKGRC--RNKIVAIKRYRANTYCS---KSDVDMFcREVSilcrlNHPCVIQFVGACL-------DDpsQFA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGNA-LKEDCIayICREILRGLAHLH--AHKVIHRDIKGQNVLLTENAEVKLVDFGVS---A 176
Cdd:cd14064    69 IVTQYVSGGSLFSLLHEQKRVIdLQSKLI--IAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESrflQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  177 QLDRTVGRRNTfiGTPYWMAPEVIAcdenPDATYDYRSDIWSLGI-------------------TAIEMA--EGAPPLCD 235
Cdd:cd14064   147 SLDEDNMTKQP--GNLRWMAPEVFT----QCTRYSIKADVFSYALclwelltgeipfahlkpaaAAADMAyhHIRPPIGY 220
                         250       260       270
                  ....*....|....*....|....*....|....
gi 578829925  236 MHPMRALFLIPRNPPPRLKSKKWSKKFIDFIDTC 269
Cdd:cd14064   221 SIPKPISSLLMRGWNAEPESRPSFVEIVALLEPC 254
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
33-272 1.04e-12

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 69.89  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   33 NGTYGQVYKGRHVKTGQLAAIKVmdvtedeeeeIKQEI-NMLKKYSH-----HRN-IATYYGAFIKKsppgndDQLWlVM 105
Cdd:PHA03390   26 DGKFGKVSVLKHKPTQKLFVQKI----------IKAKNfNAIEPMVHqlmkdNPNfIKLYYSVTTLK------GHVL-IM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTEN-AEVKLVDFGvsaqLDRTVGR 184
Cdd:PHA03390   89 DYIKDGDLFDLLKKEG--KLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAkDRIYLCDYG----LCKIIGT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  185 RNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPP----------LCDMHPMRalflipRNPPPRLK 254
Cdd:PHA03390  163 PSCYDGTLDYFSPEKIKGH-----NYDVSFDWWAVGVLTYELLTGKHPfkededeeldLESLLKRQ------QKKLPFIK 231
                         250
                  ....*....|....*...
gi 578829925  255 SKkwSKKFIDFIdTCLIK 272
Cdd:PHA03390  232 NV--SKNANDFV-QSMLK 246
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
25-255 1.35e-12

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: 70.86  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEINMLKKYSHHRN-------IATYYGAFI--KKSPP 95
Cdd:cd05633     7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLD---------KKRIKMKQGETLALNerimlslVSTGDCPFIvcMTYAF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 GNDDQLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd05633    78 HTPDKLCFILDLMNGGDLHYHL--SQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQLDRTvgRRNTFIGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPPL-----CDMHPMRALFL-----I 245
Cdd:cd05633   156 CDFSKK--KPHASVGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLtvnveL 229
                         250
                  ....*....|
gi 578829925  246 PRNPPPRLKS 255
Cdd:cd05633   230 PDSFSPELKS 239
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
25-255 1.64e-12

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: 70.08  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDvtedeeeeiKQEINMLKKYSHHRN-------IATYYGAFI--KKSPP 95
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLD---------KKRIKMKQGETLALNerimlslVSTGDCPFIvcMSYAF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 GNDDQLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd14223    73 HTPDKLSFILDLMNGGDLHYHL--SQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 AQLDRTvgRRNTFIGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPPL-----CDMHPMRALFL-----I 245
Cdd:cd14223   151 CDFSKK--KPHASVGTHGYMAPEVL----QKGVAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLtmaveL 224
                         250
                  ....*....|
gi 578829925  246 PRNPPPRLKS 255
Cdd:cd14223   225 PDSFSPELRS 234
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
25-228 1.71e-12

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: 70.28  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEE-------------------------IKQEINMLKKYSHH 79
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENVElalrefwalssiqrqhpnviqleecVLQRDGLAQRMSHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   80 RNIATYYGAFIKKSPPGN---DDQ----LWLVMEFCGAGSVTDLVKNTKGNALKEDCIAyicREILRGLAHLHAHKVIHR 152
Cdd:cd13977    82 SSKSDLYLLLVETSLKGErcfDPRsacyLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFM---LQLSSALAFLHRNQIVHR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  153 DIKGQNVLLTENAE---VKLVDFGVSaQLDRTVGRR------------NTFIGTPYWMAPEVIacdenpDATYDYRSDIW 217
Cdd:cd13977   159 DLKPDNILISHKRGepiLKVADFGLS-KVCSGSGLNpeepanvnkhflSSACGSDFYMAPEVW------EGHYTAKADIF 231
                         250
                  ....*....|.
gi 578829925  218 SLGITAIEMAE 228
Cdd:cd13977   232 ALGIIIWAMVE 242
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
31-229 1.88e-12

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: 69.58  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQL--AAIKVMDVTEDEEEE-----IKQEINMLKKYSHHRNIATYYGAFIKKSPPGNDDQLwL 103
Cdd:cd14020     8 LGQGSSASVYRVSSGRGADQptSALKEFQLDHQGSQEsgdygFAKERAALEQLQGHRNIVTLYGVFTNHYSANVPSRC-L 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV-KLVDFGVSAQldrtV 182
Cdd:cd14020    87 LLELLDV-SVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDECfKLIDFGLSFK----E 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  183 GRRNT-FIGTPYWMAPEviACDENPDATYDYRS--------DIWSLGITAIEMAEG 229
Cdd:cd14020   162 GNQDVkYIQTDGYRAPE--AELQNCLAQAGLQSetectsavDLWSLGIVLLEMFSG 215
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
25-235 1.90e-12

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: 68.90  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK--VMDVTEDEEEEIKQEINMLKKYSHHrNIATYYGAFIKKSppgnddQLW 102
Cdd:cd14088     3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkfLKRDGRKVRKAAKNEINILKMVKHP-NILQLVDVFETRK------EYF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNtKGNALKEDcIAYICREILRGLAHLHAHKVIHRDIKGQNVLL---TENAEVKLVDFGVsAQLD 179
Cdd:cd14088    76 IFLELATGREVFDWILD-QGYYSERD-TSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYynrLKNSKIVISDFHL-AKLE 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  180 RTVGRRNTfiGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCD 235
Cdd:cd14088   153 NGLIKEPC--GTPEYLAPEVVG-----RQRYGRPVDCWAIGVIMYILLSGNPPFYD 201
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
31-188 2.04e-12

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 69.69  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHV---KTGQLAAIKVMDVTEDEEEEIKQEI-NMLKKYSHHRNIATYYGAFIkksppgNDDQLWLVME 106
Cdd:cd13981     8 LGEGGYASVYLAKDDdeqSDGSLVALKVEKPPSIWEFYICDQLhSRLKNSRLRESISGAHSAHL------FQDESILVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLV---KNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---------------ENAEVK 168
Cdd:cd13981    82 YSSQGTLLDVVnkmKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRleicadwpgegengwLSKGLK 161
                         170       180
                  ....*....|....*....|
gi 578829925  169 LVDFGVSaqLDRTVGRRNTF 188
Cdd:cd13981   162 LIDFGRS--IDMSLFPKNQS 179
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
28-232 2.28e-12

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: 69.28  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYY-----GAFIKKSppgnddqLW 102
Cdd:cd05109    12 VKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYvcrllGICLTST-------VQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGNALKEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd05109    85 LVTQLMPYGCLLDYVRENKDRIGSQDLLNW-CVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDE 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578829925  183 GRRNTFIG-TPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIE-MAEGAPP 232
Cdd:cd05109   164 TEYHADGGkVPIkWMALESIL-----HRRFTHQSDVWSYGVTVWElMTFGAKP 211
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
30-226 2.75e-12

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: 68.64  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGR-----HVKTGQLAAIKVMDVTEDEE--EEIKQEINMLKKYSHhRNIATYYGAFIKKSPpgnddqLW 102
Cdd:cd05046    12 TLGRGEFGEVFLAKakgieEEGGETLVLVKALQKTKDENlqSEFRRELDMFRKLSH-KNVVRLLGLCREAEP------HY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGNALKED--------CIAyICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKlvdfgV 174
Cdd:cd05046    85 MILEYTDLGDLKQFLRATKSKDEKLKppplstkqKVA-LCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVK-----V 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  175 SA-QLDRTVGR------RNTFIgtPY-WMAPEVIACDEnpdatYDYRSDIWSLGITAIEM 226
Cdd:cd05046   159 SLlSLSKDVYNseyyklRNALI--PLrWLAPEAVQEDD-----FSTKSDVWSFGVLMWEV 211
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
29-251 3.04e-12

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: 68.36  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTG---QLAAIKVMDV--TEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSPpgnddqLWL 103
Cdd:cd05065    10 EVIGAGEFGEVCRGRLKLPGkreIFVAIKTLKSgyTEKQRRDFLSEASIMGQFDH-PNIIHLEGVVTKSRP------VMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKGNALKEDCIAyICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--DRT 181
Cdd:cd05065    83 ITEFMENGALDSFLRQNDGQFTVIQLVG-MLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLedDTS 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578829925  182 VGRRNTFIGTPY---WMAPEVIACDENPDAtydyrSDIWSLGITAIE-MAEGAPPLCDMHPMRALFLIP---RNPPP 251
Cdd:cd05065   162 DPTYTSSLGGKIpirWTAPEAIAYRKFTSA-----SDVWSYGIVMWEvMSYGERPYWDMSNQDVINAIEqdyRLPPP 233
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
537-793 3.07e-12

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 71.74  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  537 GRGMNPADKPAWAREVEERTRMNKQQNSPLAKSKPGSTGPEPPIPQASPGPPGPLSqTPPMQRPVEPQEGPHKSLVAHRV 616
Cdd:PHA03307   58 GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSS-PDPPPPTPPPASPPPSPAPDLSE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  617 PLKPYAAPVPRSQslqdqptrnlAAFPASHDPDPAIPAPTATPsaRGAVIRQNSDPTSEGPGPSPNPPAWVRPDNEAPPK 696
Cdd:PHA03307  137 MLRPVGSPGPPPA----------ASPPAAGASPAAVASDAASS--RQAALPLSSPEETARAPSSPPAEPPPSTPPAAASP 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  697 VPQRTSSIA-------TALNTSGAGGSRPAQAVRASNPDLRRSDPGwERSDSVLPaSHGHLPQAGSLERNRVGVSSKPDS 769
Cdd:PHA03307  205 RPPRRSSPIsasasspAPAPGRSAADDAGASSSDSSSSESSGCGWG-PENECPLP-RPAPITLPTRIWEASGWNGPSSRP 282
                         250       260
                  ....*....|....*....|....
gi 578829925  770 SPVLSPGNKAKPDDhRSRPGRPAD 793
Cdd:PHA03307  283 GPASSSSSPRERSP-SPSPSSPGS 305
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
25-318 3.86e-12

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 69.04  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK--------VMDVTEdeeeeIKQEINMLKkYSHHRNIATYYGAFIKKSPPG 96
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKkindvfehVSDATR-----ILREIKLLR-LLRHPDIVEIKHIMLPPSRRE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   97 NDDqLWLVMEFCGagsvTDLVKNTKGNA-LKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVS 175
Cdd:cd07859    76 FKD-IYVVFELME----SDLHQVIKANDdLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  176 -AQLDRTVGRR--NTFIGTPYWMAPEVIACDEnpdATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR---NP 249
Cdd:cd07859   151 rVAFNDTPTAIfwTDYVATRWYRAPELCGSFF---SKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDllgTP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  250 PP----RLKSKK---------------WSKKF--IDFIDTCLIKTYLS-----RPPTEQLLKFPFIR-----DQPTERQV 298
Cdd:cd07859   228 SPetisRVRNEKarrylssmrkkqpvpFSQKFpnADPLALRLLERLLAfdpkdRPTAEEALADPYFKglakvEREPSAQP 307
                         330       340
                  ....*....|....*....|
gi 578829925  299 RIQLKDHIDRSRKKRGEKEE 318
Cdd:cd07859   308 ITKLEFEFERRRLTKEDVRE 327
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
25-231 3.90e-12

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 69.35  E-value: 3.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHR----NIATYYGAFIKKsppgndDQ 100
Cdd:cd14228    17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENadeyNFVRSYECFQHK------NH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCgAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA----EVKLVDFGVSA 176
Cdd:cd14228    91 TCLVFEML-EQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFGSAS 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  177 QLDRTVGrrNTFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAP 231
Cdd:cd14228   170 HVSKAVC--STYLQSRYYRAPEIILGLPFCEAI-----DMWSLGCVIAELFLGWP 217
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
31-283 4.25e-12

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: 68.00  E-value: 4.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRhVKTGQLAAiKVMDVTEDEEEEIKQEINMLKKYS-----HHRNIATYYGAFIKKSPpgnddqLWLVM 105
Cdd:cd05042     3 IGNGWFGKVLLGE-IYSGTSVA-QVVVKELKASANPKEQDTFLKEGQpyrilQHPNILQCLGQCVEAIP------YLLVM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  106 EFCGAGSVTDLVKNTKGNALKEDCIAYICR---EILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQldrtv 182
Cdd:cd05042    75 EFCDLGDLKAYLRSEREHERGDSDTRTLQRmacEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHS----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  183 GRRNTFIGTP-------YWMAPEVIACDENPDATYDY--RSDIWSLGITAIEMAE-GAPPLCDMHPMRALFLIPRN---- 248
Cdd:cd05042   150 RYKEDYIETDdklwfplRWTAPELVTEFHDRLLVVDQtkYSNIWSLGVTLWELFEnGAQPYSNLSDLDVLAQVVREqdtk 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578829925  249 -PPPRLKsKKWSKKFIDFIDTCLIKTYlSRPPTEQL 283
Cdd:cd05042   230 lPKPQLE-LPYSDRWYEVLQFCWLSPE-QRPAAEDV 263
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
25-231 4.54e-12

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 68.88  E-value: 4.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYY-----GAFIKKsppgndD 99
Cdd:cd14226    15 YEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTENKYYivrlkRHFMFR------N 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCgAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAH--KVIHRDIKGQNVLL--TENAEVKLVDFGVS 175
Cdd:cd14226    89 HLCLVFELL-SYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLcnPKRSAIKIIDFGSS 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  176 AQLDRTVGRrntFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd14226   168 CQLGQRIYQ---YIQSRFYRSPEVLLGLP-----YDLAIDMWSLGCILVEMHTGEP 215
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
136-284 4.97e-12

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: 69.65  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  136 EILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT---VGRRNTFIGTPyWMAPEVIAcdenpDATYDY 212
Cdd:cd05107   247 QVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDsnyISKGSTFLPLK-WMAPESIF-----NNLYTT 320
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  213 RSDIWSLGITAIEM-AEGAPPLCDMhPMRALFLIPRNPPPRL-KSKKWSKKFIDFIDTCLIKTYLSRPPTEQLL 284
Cdd:cd05107   321 LSDVWSFGILLWEIfTLGGTPYPEL-PMNEQFYNAIKRGYRMaKPAHASDEIYEIMQKCWEEKFEIRPDFSQLV 393
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
72-230 5.20e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 68.90  E-value: 5.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   72 MLKKYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEFCGAGSVTDLVKNtkgnaLKEDCIAYICREILRGLAHLHAHKVIH 151
Cdd:cd07876    72 VLLKCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELMDANLCQVIHME-----LDHERMSYLLYQMLCGIKHLHSAGIIH 146
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  152 RDIKGQNVLLTENAEVKLVDFGVsAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGA 230
Cdd:cd07876   147 RDLKPSNIVVKSDCTLKILDFGL-ARTACTNFMMTPYVVTRYYRAPEVIL-----GMGYKENVDIWSVGCIMGELVKGS 219
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
29-226 5.30e-12

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: 67.75  E-value: 5.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYK-------GRHV-------KTGQLAAIKVMDvtedeeeEIKQEINMLKKYSHhRNIATYYGAFIkksp 94
Cdd:cd05040     1 EKLGDGSFGVVRRgewttpsGKVIqvavkclKSDVLSQPNAMD-------DFLKEVNAMHSLDH-PNLIRLYGVVL---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   95 pgnDDQLWLVMEFCGAGSVTDLVKNTKGNALkedcIAYICR---EILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVD 171
Cdd:cd05040    69 ---SSPLMMVTELAPLGSLLDRLRKDQGHFL----ISTLCDyavQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGD 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  172 FGVSAQLDRTvgrRNTFIGTPY------WMAPEVIACdenpdATYDYRSDIWSLGITAIEM 226
Cdd:cd05040   142 FGLMRALPQN---EDHYVMQEHrkvpfaWCAPESLKT-----RKFSHASDVWMFGVTLWEM 194
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
25-232 6.44e-12

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: 68.13  E-value: 6.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM--DVTEDEEEEIKQEI---NMLKKYSHHRNIATYYGAFIKKSppgndd 99
Cdd:cd05108     9 FKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAikELREATSPKANKEIldeAYVMASVDNPHVCRLLGICLTST------ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 qLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 179
Cdd:cd05108    83 -VQLITQLMPFGCLLDYVREHKDNIGSQYLLNW-CVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  180 RTVGRRNTFIG-TPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIE-MAEGAPP 232
Cdd:cd05108   161 AEEKEYHAEGGkVPIkWMALESIL-----HRIYTHQSDVWSYGVTVWElMTFGSKP 211
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
25-231 6.44e-12

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 68.58  E-value: 6.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHR----NIATYYGAFIKKsppgndDQ 100
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESaddyNFVRAYECFQHK------NH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 LWLVMEFCgAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA----EVKLVDFGVSA 176
Cdd:cd14227    91 TCLVFEML-EQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSrqpyRVKVIDFGSAS 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  177 QLDRTVGrrNTFIGTPYWMAPEVIACDENPDATydyrsDIWSLGITAIEMAEGAP 231
Cdd:cd14227   170 HVSKAVC--STYLQSRYYRAPEIILGLPFCEAI-----DMWSLGCVIAELFLGWP 217
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
27-232 8.07e-12

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: 67.34  E-value: 8.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ--------EINMLKKYSHHRnIATYYGAF-IKKsppgn 97
Cdd:cd13990     4 LLNLLGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKQnyikhalrEYEIHKSLDHPR-IVKLYDVFeIDT----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   98 dDQLWLVMEFCgAGSVTDLVKNTKGNALKEDCIAYICrEILRGLAHLHAHK--VIHRDIKGQNVLLTENA---EVKLVDF 172
Cdd:cd13990    78 -DSFCTVLEYC-DGNDLDFYLKQHKSIPEREARSIIM-QVVSALKYLNEIKppIIHYDLKPGNILLHSGNvsgEIKITDF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  173 GVSAQLDRTVGRRNTFI------GTPYWMAPEVIACDENPdATYDYRSDIWSLGITAIEMAEGAPP 232
Cdd:cd13990   155 GLSKIMDDESYNSDGMEltsqgaGTYWYLPPECFVVGKTP-PKISSKVDVWSVGVIFYQMLYGRKP 219
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
133-229 8.52e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 68.87  E-value: 8.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  133 ICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA-QLDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYD 211
Cdd:PHA03212  187 IERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACfPVDINANKYYGWAGTIATNAPELLARD-----PYG 261
                          90
                  ....*....|....*...
gi 578829925  212 YRSDIWSLGITAIEMAEG 229
Cdd:PHA03212  262 PAVDIWSAGIVLFEMATC 279
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
127-232 8.94e-12

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 68.08  E-value: 8.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  127 EDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--DRTVGRRNTFIGTPYWMAPEVIAcde 204
Cdd:cd05102   172 EDLICY-SFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIykDPDYVRKGSARLPLKWMAPESIF--- 247
                          90       100
                  ....*....|....*....|....*....
gi 578829925  205 npDATYDYRSDIWSLGITAIEM-AEGAPP 232
Cdd:cd05102   248 --DKVYTTQSDVWSFGVLLWEIfSLGASP 274
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
25-234 9.29e-12

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 68.34  E-value: 9.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMdvtedeeeeIKQEinMLKK--YSHHRN------------IATYYGAFi 90
Cdd:cd05629     3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTL---------LKSE--MFKKdqLAHVKAerdvlaesdspwVVSLYYSF- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   91 kksppgNDDQ-LWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 169
Cdd:cd05629    71 ------QDAQyLYLIMEFLPGGDLMTML--IKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  170 VDFGVSA---------------------------------QLDRTVGRRNTF--------------IGTPYWMAPEVIAc 202
Cdd:cd05629   143 SDFGLSTgfhkqhdsayyqkllqgksnknridnrnsvavdSINLTMSSKDQIatwkknrrlmaystVGTPDYIAPEIFL- 221
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  203 denpDATYDYRSDIWSLGITAIEMAEGAPPLC 234
Cdd:cd05629   222 ----QQGYGQECDWWSLGAIMFECLIGWPPFC 249
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
31-245 1.34e-11

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 67.50  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEeeIKQ---EINMLKKYSHHrNIATYYGAFIKKSPPGNDD-------- 99
Cdd:cd07854    13 LGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQS--VKHalrEIKIIRRLDHD-NIVKVYEVLGPSGSDLTEDvgslteln 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGagsvTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL-TENAEVKLVDFGVSAQL 178
Cdd:cd07854    90 SVYIVQEYME----TDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDFGLARIV 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 DRTV---GRRNTFIGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLI 245
Cdd:cd07854   166 DPHYshkGYLSEGLVTKWYRSPRLLLSPNN----YTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLI 231
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
32-221 1.55e-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: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGrhVKTGQLAAIKVMDvTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSPpgnddqlwLVMEFCGAG 111
Cdd:cd14068     3 GDGGFGSVYRA--VYRGEDVAVKIFN-KHTSFRLLRQELVVLSHL-HHPSLVALLAAGTAPRM--------LVMELAPKG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  112 SVTDLVKNTKGnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVL---LTENAEV--KLVDFGVsAQLDRTVGRRn 186
Cdd:cd14068    71 SLDALLQQDNA-SLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLlftLYPNCAIiaKIADYGI-AQYCCRMGIK- 147
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 578829925  187 TFIGTPYWMAPEViacdENPDATYDYRSDIWSLGI 221
Cdd:cd14068   148 TSEGTPGFRAPEV----ARGNVIYNQQADVYSFGL 178
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
103-283 1.73e-11

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: 66.51  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVK-NTKGNALKED-------CIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGV 174
Cdd:cd14206    74 LIMEFCQLGDLKRYLRaQRKADGMTPDlptrdlrTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGL 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  175 SAQldrtvGRRNTFIGTP-------YWMAPE--------VIACDENPDatydyrSDIWSLGITAIEMAE-GAPPLCDMHP 238
Cdd:cd14206   154 SHN-----NYKEDYYLTPdrlwiplRWVAPElldelhgnLIVVDQSKE------SNVWSLGVTIWELFEfGAQPYRHLSD 222
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  239 MRALFLIPRN-----PPPRLKsKKWSKKFIDFIDTCLIKTYlSRPPTEQL 283
Cdd:cd14206   223 EEVLTFVVREqqmklAKPRLK-LPYADYWYEIMQSCWLPPS-QRPSVEEL 270
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
72-226 1.73e-11

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 67.42  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   72 MLKKYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEFCGAgSVTDLVKNTkgnaLKEDCIAYICREILRGLAHLHAHKVIH 151
Cdd:cd07874    68 VLMKCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELMDA-NLCQVIQME----LDHERMSYLLYQMLCGIKHLHSAGIIH 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  152 RDIKGQNVLLTENAEVKLVDFGvsaqLDRTVGrrNTFIGTP-----YWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd07874   143 RDLKPSNIVVKSDCTLKILDFG----LARTAG--TSFMMTPyvvtrYYRAPEVIL-----GMGYKENVDIWSVGCIMGEM 211
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
24-258 2.68e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 66.96  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM---DV-TEDEEEEIKQEINMLKKYSHHRNIATYYgAFIKKsppgndD 99
Cdd:cd05626     2 MFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLrkkDVlNRNQVAHVKAERDILAEADNEWVVKLYY-SFQDK------D 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL- 178
Cdd:cd05626    75 NLYFVMDYIPGGDMMSLL--IRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  179 ----------------------------------DR--TVGRR----------NTFIGTPYWMAPEVIAcdenpDATYDY 212
Cdd:cd05626   153 wthnskyyqkgshirqdsmepsdlwddvsncrcgDRlkTLEQRatkqhqrclaHSLVGTPNYIAPEVLL-----RKGYTQ 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578829925  213 RSDIWSLGITAIEMAEGAPPlcdmhpmralFLIPRNPPPRLKSKKW 258
Cdd:cd05626   228 LCDWWSVGVILFEMLVGQPP----------FLAPTPTETQLKVINW 263
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
20-221 3.24e-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: 65.29  E-value: 3.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   20 DPAGIFELVEVvGNGTYGQVYKGRHvkTGQL-AAIKVMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKSPpgnd 98
Cdd:cd05113     2 DPKDLTFLKEL-GTGQFGVVKYGKW--RGQYdVAIKMIKEGSMSEDEFIEEAKVMMNL-SHEKLVQLYGVCTKQRP---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dqLWLVMEFCGAGSVTDLVKNTkGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ- 177
Cdd:cd05113    74 --IFIITEYMANGCLLNYLREM-RKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYv 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578829925  178 LDrtvGRRNTFIGTPY---WMAPEVIACdenpdATYDYRSDIWSLGI 221
Cdd:cd05113   151 LD---DEYTSSVGSKFpvrWSPPEVLMY-----SKFSSKSDVWAFGV 189
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
25-229 4.00e-11

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 65.71  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTG-QLAAIKVMDVTEDEEEEIKQEINMLKKYSHH-----RNIATYYGAFIKKSppgnd 98
Cdd:cd14135     2 YRVYGYLGKGVFSNVVRARDLARGnQEVAIKIIRNNELMHKAGLKELEILKKLNDAdpddkKHCIRLLRHFEHKN----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 dQLWLVMEfCGAGSVTDLVKN-TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV-KLVDFGvSA 176
Cdd:cd14135    77 -HLCLVFE-SLSMNLREVLKKyGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTlKLCDFG-SA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578829925  177 QLDRTVGRrntfigTPY-----WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEG 229
Cdd:cd14135   154 SDIGENEI------TPYlvsrfYRAPEIIL-----GLPYDYPIDMWSVGCTLYELYTG 200
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
130-227 4.18e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 66.41  E-value: 4.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  130 IAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTF--IGTPYWMAPEVIACDenpd 207
Cdd:PHA03207  187 AITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDTPQCYgwSGTLETNSPELLALD---- 262
                          90       100
                  ....*....|....*....|
gi 578829925  208 aTYDYRSDIWSLGITAIEMA 227
Cdd:PHA03207  263 -PYCAKTDIWSAGLVLFEMS 281
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
27-226 4.45e-11

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: 65.18  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKG--RHVKTGQ---LAAIKVMD--VTEDEEEEIKQEINMLKKYsHHRNIATYYGAFikksppGNDD 99
Cdd:cd05049     9 LKRELGEGAFGKVFLGecYNLEPEQdkmLVAVKTLKdaSSPDARKDFEREAELLTNL-QHENIVKFYGVC------TEGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVK-------------NTKGNALKEDCIAyICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE 166
Cdd:cd05049    82 PLLMVFEYMEHGDLNKFLRshgpdaaflasedSAPGELTLSQLLH-IAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  167 VKLVDFGVSAQL---D--RTVGRRNTFIgtpYWMAPEVIACdenpdATYDYRSDIWSLGITAIEM 226
Cdd:cd05049   161 VKIGDFGMSRDIystDyyRVGGHTMLPI---RWMPPESILY-----RKFTTESDVWSFGVVLWEI 217
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
25-238 4.48e-11

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 65.17  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKG--RHVKTGQLAAIkVMDVTEDEEEEikqEINML-----KKYS-HHRNIATYYGAFIKKS-PP 95
Cdd:cd05043     8 VTLSDLLQEGTFGRIFHGilRDEKGKEEEVL-VKTVKDHASEI---QVTMLlqessLLYGlSHQNLLPILHVCIEDGeKP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   96 ---------GNddqLWLVMEFCgagsvtDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE 166
Cdd:cd05043    84 mvlypymnwGN---LKLFLQQC------RLSEANNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  167 VKLVDFGVSaqldrtvgrRNTFIGTPY-----------WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAE-GAPPLC 234
Cdd:cd05043   155 VKITDNALS---------RDLFPMDYHclgdnenrpikWMSLESLV-----NKEYSSASDVWSFGVLLWELMTlGQTPYV 220

                  ....
gi 578829925  235 DMHP 238
Cdd:cd05043   221 EIDP 224
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
28-242 5.21e-11

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


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 65.47  E-value: 5.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRHVKTGQLA----AIKVMDVTEDEEEEIK-QEINMLKKYSHHRNIATYYGAFIKKSppgnddqLW 102
Cdd:cd05110    12 VKVLGSGAFGTVYKGIWVPEGETVkipvAIKILNETTGPKANVEfMDEALIMASMDHPHLVRLLGVCLSPT-------IQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  103 LVMEFCGAGSVTDLVKNTKGNALKEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 182
Cdd:cd05110    85 LVTQLMPHGCLLDYVHEHKDNIGSQLLLNW-CVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDE 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578829925  183 GRRNTFIGTP--YWMAPEVIACDEnpdatYDYRSDIWSLGITAIE-MAEGAPPLcDMHPMRAL 242
Cdd:cd05110   164 KEYNADGGKMpiKWMALECIHYRK-----FTHQSDVWSYGVTIWElMTFGGKPY-DGIPTREI 220
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
29-238 6.09e-11

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: 64.42  E-value: 6.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQL---AAIKVMDV---TEDEEEEIKQEINMlkKYSHHRNIATYYGAFIKK--SPpgnddq 100
Cdd:cd05058     1 EVIGKGHFGCVYHGTLIDSDGQkihCAVKSLNRitdIEEVEQFLKEGIIM--KDFSHPNVLSLLGICLPSegSP------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  101 lWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ-LD 179
Cdd:cd05058    73 -LVVLPYMKHGDLRNFIRSETHNPTVKDLIGF-GLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDiYD 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578829925  180 RTVG--RRNTFIGTPY-WMAPEVIACDenpdaTYDYRSDIWSLGITAIE-MAEGAPPLCDMHP 238
Cdd:cd05058   151 KEYYsvHNHTGAKLPVkWMALESLQTQ-----KFTTKSDVWSFGVLLWElMTRGAPPYPDVDS 208
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
34-233 6.24e-11

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 64.55  E-value: 6.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   34 GTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYsHHRNIATYYGAFIkkSPpgndDQLWLVMEFCgagSV 113
Cdd:cd14110    14 GRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRL-SHPRIAQLHSAYL--SP----RHLVLIEELC---SG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  114 TDLVKN-TKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvSAQL--DRTVGRRNTFIG 190
Cdd:cd14110    84 PELLYNlAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLG-NAQPfnQGKVLMTDKKGD 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578829925  191 TPYWMAPEVIacdENPDATydYRSDIWSLGITAIEMAEGAPPL 233
Cdd:cd14110   163 YVETMAPELL---EGQGAG--PQTDIWAIGVTAFIMLSADYPV 200
PHA03247 PHA03247
large tegument protein UL36; Provisional
542-791 7.37e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 67.27  E-value: 7.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  542 PADKPA--WAREVEERTRMNKQQNSPLAKSKPGSTGPEPPIPQASPGPPGPLSQTPPMQRPvEPQEGPHKSLVAHRVPLK 619
Cdd:PHA03247 2573 PAPRPSepAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP-AANEPDPHPPPTVPPPER 2651
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  620 PYAAPVPRSQSLQDQPTRNLAAFPASHDPDPaiPAPTATPSARGAVIrQNSDPTSEGPGPSPNPPAWVrPDNEAPPkVPQ 699
Cdd:PHA03247 2652 PRDDPAPGRVSRPRRARRLGRAAQASSPPQR--PRRRAARPTVGSLT-SLADPPPPPPTPEPAPHALV-SATPLPP-GPA 2726
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  700 RTSSIATALNTSGAGGSRPAQAVRASNPDLRRS--------DPGWERSDSVLPASHGHLPQAGSLERNRVGVSSKPDSSP 771
Cdd:PHA03247 2727 AARQASPALPAAPAPPAVPAGPATPGGPARPARppttagppAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD 2806
                         250       260
                  ....*....|....*....|...
gi 578829925  772 ---VLSPGNKAKPDDHRSRPGRP 791
Cdd:PHA03247 2807 ppaAVLAPAAALPPAASPAGPLP 2829
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
31-233 8.92e-11

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: 64.11  E-value: 8.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   31 VGNGTYGQVYKGRHVKTGQLAaIKVMDVTEDEEEEIKQEINMLKKYSHHRnIATYYGAFIKKSPpgnddqLWLVMEFCGA 110
Cdd:cd05114    12 LGSGLFGVVRLGKWRAQYKVA-IKAIREGAMSEEDFIEEAKVMMKLTHPK-LVQLYGVCTQQKP------IYIVTEFMEN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKGNaLKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL--DRTVgrrnTF 188
Cdd:cd05114    84 GCLLNYLRQRRGK-LSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVldDQYT----SS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578829925  189 IGTPY---WMAPEVIACDEnpdatYDYRSDIWSLGITAIEM-AEGAPPL 233
Cdd:cd05114   159 SGAKFpvkWSPPEVFNYSK-----FSSKSDVWSFGVLMWEVfTEGKMPF 202
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
28-230 9.23e-11

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 64.12  E-value: 9.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   28 VEVVGNGTYGQVYKGRhVKTGQLAAIKVMDVTEDEEEEIKQE--INMLKKYS--HHRNIATYYGAFIKKSPpgnddqLWL 103
Cdd:cd05086     2 IQEIGNGWFGKVLLGE-IYTGTSVARVVVKELKASANPKEQDdfLQQGEPYYilQHPNILQCVGQCVEAIP------YLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  104 VMEFCGAGSVTDLVKNTKGNALKEDCIAYICR---EILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA---Q 177
Cdd:cd05086    75 VFEFCDLGDLKTYLANQQEKLRGDSQIMLLQRmacEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFsryK 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  178 LDRTVGRRNTFIGTpYWMAPEVIACDENPDATYDYR--SDIWSLGITAIEMAEGA 230
Cdd:cd05086   155 EDYIETDDKKYAPL-RWTAPELVTSFQDGLLAAEQTkySNIWSLGVTLWELFENA 208
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
72-229 9.71e-11

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 65.07  E-value: 9.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   72 MLKKYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEFCGAgSVTDLVKNTkgnaLKEDCIAYICREILRGLAHLHAHKVIH 151
Cdd:cd07875    75 VLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDA-NLCQVIQME----LDHERMSYLLYQMLCGIKHLHSAGIIH 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  152 RDIKGQNVLLTENAEVKLVDFGvsaqLDRTVGrrNTFIGTP-----YWMAPEVIAcdenpDATYDYRSDIWSLGITAIEM 226
Cdd:cd07875   150 RDLKPSNIVVKSDCTLKILDFG----LARTAG--TSFMMTPyvvtrYYRAPEVIL-----GMGYKENVDIWSVGCIMGEM 218

                  ...
gi 578829925  227 AEG 229
Cdd:cd07875   219 IKG 221
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
29-219 1.07e-10

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: 63.67  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   29 EVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYS--HHRNIATYYGafIKKSPPGnddqlwLVME 106
Cdd:cd14025     2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEmaKFRHILPVYG--ICSEPVG------LVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  107 FCGAGSVTDLVKNtkgNALKEDCIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLTENAEVKLVDFGVS---AQLDRT 181
Cdd:cd14025    74 YMETGSLEKLLAS---EPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAkwnGLSHSH 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578829925  182 VGRRNTFIGTPYWMAPEVI-ACDENPDATYDYRS---DIWSL 219
Cdd:cd14025   151 DLSRDGLRGTIAYLPPERFkEKNRCPDTKHDVYSfaiVIWGI 192
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
25-231 1.66e-10

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 63.58  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLkkYSH-----HRNIATYYGAFikksppGNDD 99
Cdd:cd14051     2 FHEVEKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQNALNEV--YAHavlgkHPHVVRYYSAW------AEDD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLV-KNTK-GNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL---VDFGV 174
Cdd:cd14051    74 HMIIQNEYCNGGSLADAIsENEKaGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSseeEEEDF 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  175 SAQLDRTVGRRNTF-IG---------TPY-------WMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAP 231
Cdd:cd14051   154 EGEEDNPESNEVTYkIGdlghvtsisNPQveegdcrFLANEIL----QENYSHLPKADIFALALTVYEAAGGGP 223
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
111-283 1.88e-10

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 62.75  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  111 GSVTDLVKNTKgnALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDRTVGRRNTF 188
Cdd:cd14022    69 GDMHSFVRTCK--KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKdeERTRVKLESLEDAYILRGHDDSLSDK 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  189 IGTPYWMAPEVIacdeNPDATYDYRS-DIWSLGITAIEMAEGAPPLCDMHP-------MRALFLIPRNPPPRLKskkwsk 260
Cdd:cd14022   147 HGCPAYVSPEIL----NTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPsslfskiRRGQFNIPETLSPKAK------ 216
                         170       180
                  ....*....|....*....|...
gi 578829925  261 kfidfidtCLIKTYLSRPPTEQL 283
Cdd:cd14022   217 --------CLIRSILRREPSERL 231
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
24-239 2.05e-10

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 64.30  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVM---DVT-EDEEEEIKQEINMLKKYSHHRNIATYYgAFIKKsppgndD 99
Cdd:cd05625     2 MFVKIKTLGIGAFGEVCLARKVDTKALYATKTLrkkDVLlRNQVAHVKAERDILAEADNEWVVRLYY-SFQDK------D 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA--- 176
Cdd:cd05625    75 NLYFVMDYIPGGDMMSLL--IRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  177 --------------------------------------QLDRTVGRR------NTFIGTPYWMAPEVIAcdenpDATYDY 212
Cdd:cd05625   153 wthdskyyqsgdhlrqdsmdfsnewgdpencrcgdrlkPLERRAARQhqrclaHSLVGTPNYIAPEVLL-----RTGYTQ 227
                         250       260
                  ....*....|....*....|....*..
gi 578829925  213 RSDIWSLGITAIEMAEGAPPLCDMHPM 239
Cdd:cd05625   228 LCDWWSVGVILFEMLVGQPPFLAQTPL 254
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
25-263 2.35e-10

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 64.00  E-value: 2.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHH-----RNIATYYGAFIKKsppgndD 99
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKQdkdntMNVIHMLESFTFR------N 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 QLWLVMEFCGAgSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE--VKLVDFGVSAQ 177
Cdd:cd14224   141 HICMTFELLSM-NLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSSCY 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRtvgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAP--PLCDMHPMRALFL-IPRNPPPR-L 253
Cdd:cd14224   220 EHQ---RIYTYIQSRFYRAPEVIL-----GARYGMPIDMWSFGCILAELLTGYPlfPGEDEGDQLACMIeLLGMPPQKlL 291
                         250
                  ....*....|
gi 578829925  254 KSKKWSKKFI 263
Cdd:cd14224   292 ETSKRAKNFI 301
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
83-227 2.59e-10

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


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 63.23  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   83 ATYYGAFI-KKSPPGNDDQLWLVMEFCGAGSVTDLVKN------------------TKGNALKEDCIAYICREILRGLAH 143
Cdd:cd14013    56 AEFVGAFLdTTSKKFTKPSLWLVWKYEGDATLADLMQGkefpynlepiifgrvlipPRGPKRENVIIKSIMRQILVALRK 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  144 LHAHKVIHRDIKGQNVLLTE-NAEVKLVDFGVSAqlDRTVGRR---NTFIGTPYWMAPE-VIACDENPDA---------- 208
Cdd:cd14013   136 LHSTGIVHRDVKPQNIIVSEgDGQFKIIDLGAAA--DLRIGINyipKEFLLDPRYAPPEqYIMSTQTPSAppapvaaals 213
                         170       180
                  ....*....|....*....|....*
gi 578829925  209 ----TYDY--RSDIWSLGITAIEMA 227
Cdd:cd14013   214 pvlwQMNLpdRFDMYSAGVILLQMA 238
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
32-242 2.66e-10

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: 62.50  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   32 GNGTYGQVYKGRH--VKTGQL----AAIKVMDVTEDEEEEIKQE-INMLKKYSHhRNIATYYGAFIKksppgndDQLWLV 104
Cdd:cd05037     8 GQGTFTNIYDGILreVGDGRVqeveVLLKVLDSDHRDISESFFEtASLMSQISH-KHLVKLYGVCVA-------DENIMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  105 MEFCGAGSVTDLVKnTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAE------VKLVDFGVSaql 178
Cdd:cd05037    80 QEYVRYGPLDKYLR-RMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSDPGVP--- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578829925  179 dRTVGRRNTFIGTPYWMAPEviaCDENPDATYDYRSDIWSLGITAIEMAEGAP-PLCDMHPMRAL 242
Cdd:cd05037   156 -ITVLSREERVDRIPWIAPE---CLRNLQANLTIAADKWSFGTTLWEICSGGEePLSALSSQEKL 216
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
27-227 3.66e-10

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: 62.33  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   27 LVEVVGNGTYGQVYKGRHVKTGQL--AAIKVMDV---TEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKSPPGNDDQL 101
Cdd:cd05075     4 LGKTLGEGEFGSVMEGQLNQDDSVlkVAVKTMKIaicTRSEMEDFLSEAVCMKEFDH-PNVMRLIGVCLQNTESEGYPSP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  102 WLVMEFCGAGSVTD-LVKNTKGNA---LKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd05075    83 VVILPFMKHGDLHSfLLYSRLGDCpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578829925  178 L-DRTVGRRNTFIGTPY-WMAPEVIAcdenpDATYDYRSDIWSLGITAIEMA 227
Cdd:cd05075   163 IyNGDYYRQGRISKMPVkWIAIESLA-----DRVYTTKSDVWSFGVTMWEIA 209
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
25-287 4.90e-10

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 61.96  E-value: 4.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   25 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVmdvTEDEEEEIKQEINMLKK-YSH-----HRNIATYYGAFikksppGND 98
Cdd:cd14138     7 FHELEKIGSGEFGSVFKCVKRLDGCIYAIKR---SKKPLAGSVDEQNALREvYAHavlgqHSHVVRYYSAW------AED 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTKGNA--LKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE------------- 163
Cdd:cd14138    78 DHMLIQNEYCNGGSLADAISENYRIMsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRtsipnaaseegde 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  164 ------NAEVKLVDFG-----VSAQLDRtvgrrntfiGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEmAEGAPP 232
Cdd:cd14138   158 dewasnKVIFKIGDLGhvtrvSSPQVEE---------GDSRFLANEVL----QENYTHLPKADIFALALTVVC-AAGAEP 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578829925  233 LC----DMHPMRALFLiPRNPpprlksKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFP 287
Cdd:cd14138   224 LPtngdQWHEIRQGKL-PRIP------QVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
99-248 4.99e-10

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 61.89  E-value: 4.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGAGSVTDLVKNTKGNALKEDcIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQL 178
Cdd:cd05115    76 EALMLVMEMASGGPLNKFLSGKKDEITVSN-VVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKAL 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578829925  179 --DRTVGRRNTFIGTPY-WMAPEVIACDEnpdatYDYRSDIWSLGITAIE-MAEGAPPLCDMHPMRALFLIPRN 248
Cdd:cd05115   155 gaDDSYYKARSAGKWPLkWYAPECINFRK-----FSSRSDVWSYGVTMWEaFSYGQKPYKKMKGPEVMSFIEQG 223
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
26-226 6.58e-10

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: 61.97  E-value: 6.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   26 ELVEVVGNGTYGQV---------------YKGRHVKTG-QLAAIKVM--DVTEDEEEEIKQEINMLKKYsHHRNIATYYG 87
Cdd:cd05051     8 EFVEKLGEGQFGEVhlceanglsdltsddFIGNDNKDEpVLVAVKMLrpDASKNAREDFLKEVKIMSQL-KDPNIVRLLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   88 AFIkksppgNDDQLWLVMEFCGAGS----------VTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQ 157
Cdd:cd05051    87 VCT------RDEPLCMIVEYMENGDlnqflqkheaETQGASATNSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  158 NVLLTENAEVKLVDFGVSaqldrtvgrRNTFIGTPY-----------WMAPEVIACDEnpdatYDYRSDIWSLGITAIEM 226
Cdd:cd05051   161 NCLVGPNYTIKIADFGMS---------RNLYSGDYYriegravlpirWMAWESILLGK-----FTTKSDVWAFGVTLWEI 226
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
24-226 1.07e-09

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 62.07  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   24 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQ---EINMLKkYSHHRNIatyYGAFIKKSPPGND-- 98
Cdd:cd07853     1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRvfrELKMLC-FFKHDNV---LSALDILQPPHIDpf 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   99 DQLWLVMEFCGagsvTDLVKNTKGN-ALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ 177
Cdd:cd07853    77 EEIYVVTELMQ----SDLHKIIVSPqPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARV 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVGRRNTF-IGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEM 226
Cdd:cd07853   153 EEPDESKHMTQeVVTQYYRAPEILMGSRH----YTSAVDIWSVGCIFAEL 198
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
21-226 1.09e-09

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: 61.00  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   21 PAGIFELVEVVGNGTYGQVYKGRH--VKTGQ---LAAIKVM--DVTEDEEEEIKQEINMLKKYSHhRNIATYYGAFIKKS 93
Cdd:cd05050     3 PRNNIEYVRDIGQGAFGRVFQARApgLLPYEpftMVAVKMLkeEASADMQADFQREAALMAEFDH-PNIVKLLGVCAVGK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   94 PpgnddqLWLVMEF------------------CGAGSVTDLVKNTKGNALKEDCIAYIC--REILRGLAHLHAHKVIHRD 153
Cdd:cd05050    82 P------MCLLFEYmaygdlneflrhrspraqCSLSHSTSSARKCGLNPLPLSCTEQLCiaKQVAAGMAYLSERKFVHRD 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578829925  154 IKGQNVLLTENAEVKLVDFGVSAQL---DRTVGRRNTFIGTpYWMAPEVIACdenpdATYDYRSDIWSLGITAIEM 226
Cdd:cd05050   156 LATRNCLVGENMVVKIADFGLSRNIysaDYYKASENDAIPI-RWMPPESIFY-----NRYTTESDVWAYGVVLWEI 225
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
30-290 1.09e-09

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 60.63  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925   30 VVGNGTYGQVYKGRHVKTGQLAAIKVMD-------VTEDEEEEIKQEINMLKKY---SHHRNIATYYGAFikKSPPGndd 99
Cdd:cd14101     7 LLGKGGFGTVYAGHRISDGLQVAIKQISrnrvqqwSKLPGVNPVPNEVALLQSVgggPGHRGVIRLLDWF--EIPEG--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  100 qLWLVMEF-CGAGSVTDLVknTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLL-TENAEVKLVDFGVSAQ 177
Cdd:cd14101    82 -FLLVLERpQHCQDLFDYI--TERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVdLRTGDIKLIDFGSGAT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  178 LDRTVgrRNTFIGTPYWMAPEVIacdenpdATYDYRS---DIWSLGITAIEMAEGAPPL-CDMHPMRALFLIPrnppprl 253
Cdd:cd14101   159 LKDSM--YTDFDGTRVYSPPEWI-------LYHQYHAlpaTVWSLGILLYDMVCGDIPFeRDTDILKAKPSFN------- 222
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578829925  254 ksKKWSKKFIDFIDTCLIKTYLSRPPTEQLLKFPFIR 290
Cdd:cd14101   223 --KRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
PHA03247 PHA03247
large tegument protein UL36; Provisional
564-809 7.57e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 60.72  E-value: 7.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  564 SPLAKSKPGSTGPEPPIPQASPGPPGPLSQTP----PMQRPVEPQEGPHKSLV----------AHRVPLKPYAAPVPRSQ 629
Cdd:PHA03247 2805 ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPtappPPPGPPPPSLPLGGSVApggdvrrrppSRSPAAKPAAPARPPVR 2884
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  630 SL-QDQPTRNLAAFPASHDPDPAIPAPTATPSARgaviRQNSDPTSEGPGPSPNPPAwvRPDNEAPPK-----VPQRTSS 703
Cdd:PHA03247 2885 RLaRPAVSRSTESFALPPDQPERPPQPQAPPPPQ----PQPQPPPPPQPQPPPPPPP--RPQPPLAPTtdpagAGEPSGA 2958
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  704 IATALNTSGAGGSRPAQAVRASNPdlrrsDPGWERSDSVLPASHGHLPQAGSLERNRVGVSSKPDSSPV------LSPGN 777
Cdd:PHA03247 2959 VPQPWLGALVPGRVAVPRFRVPQP-----APSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVslkqtlWPPDD 3033
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578829925  778 KAKPDDHRSRPGRPADFvllKERTLDEAPRPP 809
Cdd:PHA03247 3034 TEDSDADSLFDSDSERS---DLEALDPLPPEP 3062
PHA03247 PHA03247
large tegument protein UL36; Provisional
546-812 7.04e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 7.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  546 PAWAREVEERTrmnkqQNSPLAKSKPGSTGPEPPipqasPGPPGPLSQTPPMQRPVEPQEGPHKSLVAHRVPLKPYAA-- 623
Cdd:PHA03247 2478 PVYRRPAEARF-----PFAAGAAPDPGGGGPPDP-----DAPPAPSRLAPAILPDEPVGEPVHPRMLTWIRGLEELASdd 2547
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  624 ---PVPRSQSLQDQPTRNLAAFPASHDPDPAIPA-------PTATP-SARGAVIRQNSDPTSEGPGPSPNPPAWVRPDne 692
Cdd:PHA03247 2548 agdPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAvtsrarrPDAPPqSARPRAPVDDRGDPRGPAPPSPLPPDTHAPD-- 2625
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  693 apPKVPQRTSSIATALNTSGAGGSRPAQAVRASNPdlRRSDPGWERSDSVLPASHGHLPQAGSLERNRVGVSSKPDSSPV 772
Cdd:PHA03247 2626 --PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP--GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADP 2701
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578829925  773 LSPGNKAKPDDHRSRPGRPADFVLLKER------TLDEAPRPPKKA 812
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARqaspalPAAPAPPAVPAG 2747
PHA03247 PHA03247
large tegument protein UL36; Provisional
569-796 1.81e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  569 SKPGSTGPEPPIPQASPGPPGPLSQTPPMQRPVEPQ-------------EGPHKSLVAHRVPLKPYAAPVPRSQSLQDQP 635
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFalppdqperppqpQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  636 TRNLAAFPASHDPDPAIPAPT--ATPSARGAVIRQ---NSDPTSEGPGPSPNPPAwvrpdNEAPPKVPQRTSSIATALNT 710
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWlgALVPGRVAVPRFrvpQPAPSREAPASSTPPLT-----GHSLSRVSSWASSLALHEET 3017
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  711 SGAGGS------RPAQAVRASNPDLRRSDPGWERSDSVLP-ASHGHLPQAgslernrvgvssKPDSSPVLSPGNKAKPDD 783
Cdd:PHA03247 3018 DPPPVSlkqtlwPPDDTEDSDADSLFDSDSERSDLEALDPlPPEPHDPFA------------HEPDPATPEAGARESPSS 3085
                         250
                  ....*....|...
gi 578829925  784 HRSRPGRPADFVL 796
Cdd:PHA03247 3086 QFGPPPLSANAAL 3098
PHA03247 PHA03247
large tegument protein UL36; Provisional
565-782 5.88e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 5.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  565 PLAKSKPGStgPEPPIPQASPGPP-------GPLSQTPPMQRPVEPQEGPHKSLVAHRVPLKPyAAPVPRSQS------L 631
Cdd:PHA03247 2736 PAAPAPPAV--PAGPATPGGPARParppttaGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE-SLPSPWDPAdppaavL 2812
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  632 QDQPTRNLAAFPASHDPDPAIPAPTATPSARGAVirqnSDPTSEGPGPSPNPPAWVRPDNEAPPKVPqrtssiatalnts 711
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP----PPSLPLGGSVAPGGDVRRRPPSRSPAAKP------------- 2875
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578829925  712 gAGGSRPaQAVRASNPDLRRSdpgwERSDSVLPASHGHLPQAGSLERNRVGVSSKPDSSPVLSPGNKAKPD 782
Cdd:PHA03247 2876 -AAPARP-PVRRLARPAVSRS----TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ 2940
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
543-731 5.28e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  543 ADKPAWAREVEERtrmnkQQNSPLAKSKPGSTGPE-PPIPQASPGPPGPLSQTPPMQRPVEPQEGPHKSLVAHRVPLKPY 621
Cdd:PHA03307  807 PAADAASRTASKR-----KSRSHTPDGGSESSGPArPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRA 881
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  622 AAPVPRSQSlqDQPTRNLAAFPASHDPDPAI----PAPTATPSARGAVIRQNSDPTsEGPGPSPN--------------- 682
Cdd:PHA03307  882 RPGAAAPPK--AAAAAPPAGAPAPRPRPAPRvklgPMPPGGPDPRGGFRRVPPGDL-HTPAPSAAalaaycppevvaelv 958
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578829925  683 -----PPAWvRPdneAPPKVPQRTSSIATALNTSGAGGSRPAQAVRASNPdLRR 731
Cdd:PHA03307  959 dhplfPEPW-RP---ALAFDPEALAEIAARCGGPPPRSGSAFGPLRASGP-LRR 1007
PHA03247 PHA03247
large tegument protein UL36; Provisional
572-732 1.71e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  572 GSTGPEPPIPQASPGPPG--------------PLSQTPPMQR-PVEPQEGPHKSLVAHRV---------PLKPYAAPVPR 627
Cdd:PHA03247  274 GATGPPPPPEAAAPNGAAappdgvwgaalagaPLALPAPPDPpPPAPAGDAEEEDDEDGAmevvsplprPRQHYPLGFPK 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  628 SQSLQDQPTRNLAAFPASHDPDPAIPAPT---------ATPSARGAVIRQNSDPTSEGPGPSPNP-----PAWVRPDNEA 693
Cdd:PHA03247  354 RRRPTWTPPSSLEDLSAGRHHPKRASLPTrkrrsarhaATPFARGPGGDDQTRPAAPVPASVPTPaptpvPASAPPPPAT 433
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 578829925  694 PPKVPQRTSSIATALNTSGAGGSRPAQAVRASNPDLRRS 732
Cdd:PHA03247  434 PLPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDDATRK 472
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
610-793 1.99e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  610 SLVAHRV-PLKPYAAPVPRSQS---------LQDQPTRNLAAFPASHDPDPAIPAPTAT---PSARGAVIRQNSDPTSEG 676
Cdd:PHA03307  727 SLVARTVaPLVRYSPRRARARAsawditdalFSNPSLVPAKLAEALALLEPAEPQRGAGsspPVRAEAAFRRPGRLRRSG 806
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  677 PG-PSPNPPAWVRPDNEAPPKVPQRTSSIATAlntSGAGGSRPAQAVRASNPDLRRSDPGWERSDSVLPASHGHLPQAGS 755
Cdd:PHA03307  807 PAaDAASRTASKRKSRSHTPDGGSESSGPARP---PGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARP 883
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578829925  756 LE-RNRVGVSSKPDS-SPVLSPGNKAKPDDHRSRPGRPAD 793
Cdd:PHA03307  884 GAaAPPKAAAAAPPAgAPAPRPRPAPRVKLGPMPPGGPDP 923
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
542-762 2.96e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  542 PADKPAWAREVEERTRMNKQQNSPLAKSKPGSTGPEPPIPQASPGPPGPLSQTPPMQRPVEPQEGPHKSlvAHRVPLKPY 621
Cdd:PHA03307  136 EMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASP--RPPRRSSPI 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  622 AAPVPRSQSLqdqPTRNlAAFPAS---------------HDPDPAIPAPTATPSARGAVIRQNSDPTSEGPGPSPNP--- 683
Cdd:PHA03307  214 SASASSPAPA---PGRS-AADDAGasssdssssessgcgWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASsss 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  684 ------PAWVRPDNEAPPKVP----------QRTSSIATALNTS----------GAGGSRPaqAVRASNPDLRRSDPGWE 737
Cdd:PHA03307  290 sprersPSPSPSSPGSGPAPSsprassssssSRESSSSSTSSSSessrgaavspGPSPSRS--PSPSRPPPPADPSSPRK 367
                         250       260
                  ....*....|....*....|....*
gi 578829925  738 RSDSVLPASHGHLPqAGSLERNRVG 762
Cdd:PHA03307  368 RPRPSRAPSSPAAS-AGRPTRRRAR 391
PHA03247 PHA03247
large tegument protein UL36; Provisional
542-672 3.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829925  542 PADKPawareveERTRMNKQQNSPLAKSKPGSTGPEPPIPQASPGPPGPLSQTPPMQRPVEPQEGPHKSLVAHRVPLKpy 621
Cdd:PHA03247 2901 PPDQP-------ERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR-- 2971
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578829925  622 aAPVPRSQSLQDQPTRNLAAfpASHDPDPAIPAPTATPSARGAVIRQNSDP 672
Cdd:PHA03247 2972 -VAVPRFRVPQPAPSREAPA--SSTPPLTGHSLSRVSSWASSLALHEETDP 3019
 
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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